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Special Issue "Lectins"

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A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Natural Products".

Deadline for manuscript submissions: closed (15 November 2014)

Special Issue Editors

Guest Editor
Prof. Dr. Tzi Bun NG

School of Biomedical Sciences, Faculty of Medicine, The Chinese University of Hong Kong, China
Website | E-Mail
Phone: 39436872
Interests: biomolecules of mammalian; plant and microbial origins with antipathogenic activities including lectins; antimicrobial peptides; and anticancer proteins and peptides
Guest Editor
Dr. Jack Ho WONG

School of Biomedical Sciences, Faculty of Medicine, The Chinese University of Hong Kong, China
E-Mail
Interests: plant and mushroom lectins, mushroom laccases; protease inhibitors; ribosome inactivating proteins; antifungal proteins; defensins, cathelicidins; milk proteins; and natural products with antioxidant activity
Guest Editor
Dr. Evandro Fei FANG

Laboratory of Molecular Gerontology, National Institute on Aging, National Institutes of Health, Baltimore, Maryland, USA
E-Mail
Interests: natural products with anticancer activity comprising lectins; ribosome inactivating proteins; ribonucleases; and trypsin inhibitors; etc.; molecular mechanisms of aging and anti-aging interventions including mitochondria and premature aging studies; balance of mitophagy and apoptosis in aging and associated preaging disorders; DNA repair deficiency and aging; anti-aging interventions and screening of anti-aging natural compounds, especially with effects on aging-predisposed cancer

Special Issue Information

Dear Colleagues,

Lectins are a class of carbohydrate binding proteins of tremendous importance as attested to by the voluminous literature.They are produced by different organisms ranging from microbes to humans. These proteins display a diversity of structures, carbohydrate binding specificities, and functions.

The current Special Issue is devoted to reviewing published results as well as presenting original data on the classification and families, carbohydrate binding activity, characteristics, functions, production and applications of lectins of different origins.

Lectin researchers are invited to contribute articles to this Special Issue. The themes include, but are not limited to, those indicated by the keywords below.

Prof. Tzi Bun NG
Dr. Jack Ho WONG
Dr. Evandro Fei FANG
Guest Editors

Submission

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. Papers will be published continuously (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are refereed through a peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Molecules is an international peer-reviewed Open Access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1800 CHF (Swiss Francs).

Keywords

• mammalian lectins
• submammalian vertebrate lectins
• invertebrate lectins
• plant lectins
• fungal lectins
• mushroom lectins
• microbial lectins
• families and classification
• production
• carbohydrate binding activity
• characteristics and functions

Published Papers (24 papers)

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Research

Jump to: Review, Other

Open AccessArticle Targeting the Cryptococcus neoformans var. grubii Cell Wall Using Lectins: Study of the Carbohydrate-Binding Domain
Molecules 2015, 20(3), 3776-3782; doi:10.3390/molecules20033776
Received: 15 November 2014 / Revised: 9 January 2015 / Accepted: 16 January 2015 / Published: 25 February 2015
PDF Full-text (806 KB) | HTML Full-text | XML Full-text
Abstract
Cryptococcus neoformans var. grubii is considered to be the major cause of cryptococcosis in immunosuppressed patients. Understanding cell wall glycoproteins using lectins is of medical interest and can contribute to specific therapy. The aim of this study was to evaluate the carbohydrates on
[...] Read more.
Cryptococcus neoformans var. grubii is considered to be the major cause of cryptococcosis in immunosuppressed patients. Understanding cell wall glycoproteins using lectins is of medical interest and can contribute to specific therapy. The aim of this study was to evaluate the carbohydrates on the cell wall of Cryptococcus neoformans var. grubii clinical isolates, using a fluorescein isothiocyanate-lectin binding protocol. Thirty yeast strains stocked in the culture collection were cultivated for 2 days at 30 °C with shaking. Cells were obtained by centrifugation, washed in phosphate-buffered saline, and a suspension of 107 cells/mL was obtained. To determine the binding profile of lectins, concanavalin A (Con A), wheat germ agglutinin (WGA), Ulex europaeus agglutinin I (UEA-I), and peanut agglutinin (PNA) conjugated to fluorescein were used. All the tested clinical isolates of Cryptococcus neoformans var. grubii were intensely stained by WGA, moderately stained by Con A, and weakly stained by PNA and UEA-I. Thus, Cryptococcus can be detected in clinical specimens such as blood and cerebrospinal fluid using the fluorescent lectin WGA, which may be considered as an option for detection in cases of suspected cryptococcosis with low laboratory sensitivity. Future applications may be developed using this basic tool. Full article
(This article belongs to the Special Issue Lectins)
Open AccessArticle Distribution and Evolution of the Lectin Family in Soybean (Glycine max)
Molecules 2015, 20(2), 2868-2891; doi:10.3390/molecules20022868
Received: 28 November 2014 / Accepted: 6 February 2015 / Published: 11 February 2015
Cited by 4 | PDF Full-text (1170 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
Lectins are a diverse group of proteins that bind specific carbohydrates and are found throughout all kingdoms. In plants, lectins are involved in a range of important processes such as plant defense and stress signaling. Although the genome sequence of Glycine max (soybean)
[...] Read more.
Lectins are a diverse group of proteins that bind specific carbohydrates and are found throughout all kingdoms. In plants, lectins are involved in a range of important processes such as plant defense and stress signaling. Although the genome sequence of Glycine max (soybean) has been published, little is known about the abundance and expansion patterns of lectin genes in soybean. Using BLAST and hidden Markov models, a total of 359 putative lectin genes have been identified. Furthermore, these sequences could be classified in nine of the twelve plant lectin families identified today. Analysis of the domain organization demonstrated that most of the identified lectin genes encode chimerolectins, consisting of one or multiple lectin domains combined with other known protein domains. Both tandem and segmental duplication events have contributed to the expansion of the lectin gene family. These data provide a detailed understanding of the domain architecture and molecular evolution of the lectin gene family in soybean. Full article
(This article belongs to the Special Issue Lectins)
Open AccessArticle Isolation and Biochemical Characterization of Apios Tuber Lectin
Molecules 2015, 20(1), 987-1002; doi:10.3390/molecules20010987
Received: 30 November 2014 / Accepted: 5 January 2015 / Published: 9 January 2015
Cited by 3 | PDF Full-text (1674 KB) | HTML Full-text | XML Full-text
Abstract
Apios tuber lectin, named ATL, was isolated from Apios americana Medikus by two chromatography steps, hydrophobic chromatography and anion-exchange chromatography. The minimum concentration required for the hemagglutination activity toward rabbit erythrocytes of ATL was 4 μg/mL. ATL was composed of a homodimer of
[...] Read more.
Apios tuber lectin, named ATL, was isolated from Apios americana Medikus by two chromatography steps, hydrophobic chromatography and anion-exchange chromatography. The minimum concentration required for the hemagglutination activity toward rabbit erythrocytes of ATL was 4 μg/mL. ATL was composed of a homodimer of 28.4 kDa subunits. The amino acid sequence of ATL was similar to those of other legume lectins. The lectin showed moderate stability toward heating and acidic pH, and the binding affinity against several monosaccharides, such as D-glucosamine and D-galactosamine. ATL also bound to desialylated or agalactosylated glycoproteins such as asialo and agalacto transferrin. ATL decreased the transepithelial electrical resistance across human intestinal Caco-2 cell monolayers, suggesting the effect on the tight junction-mediated paracellular transport. Full article
(This article belongs to the Special Issue Lectins)
Open AccessArticle Are Vicilins Another Major Class of Legume Lectins?
Molecules 2014, 19(12), 20350-20373; doi:10.3390/molecules191220350
Received: 21 August 2014 / Revised: 11 November 2014 / Accepted: 19 November 2014 / Published: 5 December 2014
Cited by 3 | PDF Full-text (2315 KB) | HTML Full-text | XML Full-text
Abstract
Legume lectins comprise a structurally related, Ca/Mn-dependent, widespread, abundant and well characterized lectin family when compared to the large number of lectins from other sources described in the literature. Strangely enough, no specific function has been assigned to them aside from a possible
[...] Read more.
Legume lectins comprise a structurally related, Ca/Mn-dependent, widespread, abundant and well characterized lectin family when compared to the large number of lectins from other sources described in the literature. Strangely enough, no specific function has been assigned to them aside from a possible role in storage and/or defense. Using a recent and fine-tuned methodology capable of specific lectin identification, β-conglutin, Vicia faba vicilin and β-lathyrin, the vicilin storage globulins from Lupinus albus, V. faba and Lathyrus sativus, respectively, were shown to be capable of affinity binding to thoroughly washed erythrocyte membranes and of specific elution with appropriate sugars. Based on this evidence and on sparse data published in the literature, a second family of legume lectins is proposed: the 7S family of storage proteins from leguminous seeds, or family II of legume lectins. These lectins are also structurally related, widespread and well characterized. In addition, they self-aggregate in a Ca/Mg, electrostatic dependent manner and are even more abundant than the family I of legume lectins. Using the same evidence, reserve and defense roles may be attributed to family II of legume lectins. Full article
(This article belongs to the Special Issue Lectins)
Figures

Open AccessArticle Alteration of N-glycans and Expression of Their Related Glycogenes in the Epithelial-Mesenchymal Transition of HCV29 Bladder Epithelial Cells
Molecules 2014, 19(12), 20073-20090; doi:10.3390/molecules191220073
Received: 31 October 2014 / Revised: 23 November 2014 / Accepted: 24 November 2014 / Published: 1 December 2014
Cited by 5 | PDF Full-text (2890 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
The epithelial-mesenchymal transition (EMT) is an essential step in the proliferation and metastasis of solid tumor cells, and glycosylation plays a crucial role in the EMT process. Certain aberrant glycans have been reported as biomarkers during bladder cancer progression, but global variation of
[...] Read more.
The epithelial-mesenchymal transition (EMT) is an essential step in the proliferation and metastasis of solid tumor cells, and glycosylation plays a crucial role in the EMT process. Certain aberrant glycans have been reported as biomarkers during bladder cancer progression, but global variation of N-glycans in this type of cancer has not been previously studied. We examined the profiles of N-glycan and glycogene expression in transforming growth factor-beta (TGFβ)-induced EMT using non-malignant bladder transitional epithelium HCV29 cells. These expression profiles were analyzed by mass spectrometry, lectin microarray analysis, and GlycoV4 oligonucleotide microarray analysis, and confirmed by lectin histochemistry and real-time RT-PCR. The expression of 5 N-glycan-related genes were notably altered in TGFβ-induced EMT. In particular, reduced expression of glycogene man2a1, which encodes α-mannosidase 2, contributed to the decreased proportions of bi-, tri- and tetra-antennary complex N-glycans, and increased expression of hybrid-type N-glycans. Decreased expression of fuca1 gene, which encodes Type 1 α-L-fucosidase, contributed to increased expression of fucosylated N-glycans in TGFβ-induced EMT. Taken together, these findings clearly demonstrate the involvement of aberrant N-glycan synthesis in EMT in these cells. Integrated glycomic techniques as described here will facilitate discovery of glycan markers and development of novel diagnostic and therapeutic approaches to bladder cancer. Full article
(This article belongs to the Special Issue Lectins)
Open AccessArticle Isolation and Characterization of a Novel Lectin from the Edible Mushroom Stropharia rugosoannulata
Molecules 2014, 19(12), 19880-19891; doi:10.3390/molecules191219880
Received: 14 October 2014 / Revised: 18 November 2014 / Accepted: 24 November 2014 / Published: 28 November 2014
Cited by 6 | PDF Full-text (813 KB) | HTML Full-text | XML Full-text
Abstract
To date, only a few steroids have been isolated from the mushroom Stropharia rugosoannulata which can be cultivated. In this paper, a novel lectin (SRL) with a molecular weight of 38 kDa, and a unique IKSGVYRIVSWQGALGPEAR N-terminal sequence was isolated from S. rugosoannulata
[...] Read more.
To date, only a few steroids have been isolated from the mushroom Stropharia rugosoannulata which can be cultivated. In this paper, a novel lectin (SRL) with a molecular weight of 38 kDa, and a unique IKSGVYRIVSWQGALGPEAR N-terminal sequence was isolated from S. rugosoannulata, which represents the first protein isolated from the mushroom. The purification methods included (NH4)2SO4 precipitation, ion exchange chromatography on CM-cellulose, Q-Sepharose, and SP-Sepharose, and gel- filtration on Superdex-75. The lectin was adsorbed on all three types of ion exchangers and was purified more than 450-fold. The lectin was stable below 70 °C (with half of the activity preserved at 80 °C), and in the presence of NaOH and HCl solutions up to a concentration of 12.5 mM and 25 mM, respectively. The hemagglutinating activity of SRL was inhibited by inulin. Cd2+ and Hg2+ ions strongly reduced the hemagglutinating activity at concentrations from 1.25 mM to 10 mM. SRL exhibited anti-proliferative activity toward both hepatoma Hep G2 cells and leukemia L1210 cells, with an IC50 of 7 μM and 19 μM, respectively. The activity of HIV-1 reverse transcriptase could also be inhibited by SRL, with an IC50 of 10 μM. Full article
(This article belongs to the Special Issue Lectins)
Open AccessArticle A Galactose-Binding Lectin Isolated from Aplysia kurodai (Sea Hare) Eggs Inhibits Streptolysin-Induced Hemolysis
Molecules 2014, 19(9), 13990-14003; doi:10.3390/molecules190913990
Received: 13 July 2014 / Revised: 21 August 2014 / Accepted: 2 September 2014 / Published: 5 September 2014
Cited by 4 | PDF Full-text (1082 KB) | HTML Full-text | XML Full-text | Correction
Abstract
A specific galactose-binding lectin was shown to inhibit the hemolytic effect of streptolysin O (SLO), an exotoxin produced by Streptococcus pyogenes. Commercially available lectins that recognize N-acetyllactosamine (ECA), T-antigen (PNA), and Tn-antigen (ABA) agglutinated rabbit erythrocytes, but had no effect on
[...] Read more.
A specific galactose-binding lectin was shown to inhibit the hemolytic effect of streptolysin O (SLO), an exotoxin produced by Streptococcus pyogenes. Commercially available lectins that recognize N-acetyllactosamine (ECA), T-antigen (PNA), and Tn-antigen (ABA) agglutinated rabbit erythrocytes, but had no effect on SLO-induced hemolysis. In contrast, SLO-induced hemolysis was inhibited by AKL, a lectin purified from sea hare (Aplysia kurodai) eggs that recognizes α-galactoside oligosaccharides. This inhibitory effect was blocked by the co-presence of d-galactose, which binds to AKL. A possible explanation for these findings is that cholesterol-enriched microdomains containing glycosphingolipids in the erythrocyte membrane become occupied by tightly stacked lectin molecules, blocking the interaction between cholesterol and SLO that would otherwise result in penetration of the membrane. Growth of S. pyogenes was inhibited by lectins from a marine invertebrate (AKL) and a mushroom (ABA), but was promoted by a plant lectin (ECA). Both these inhibitory and promoting effects were blocked by co-presence of galactose in the culture medium. Our findings demonstrate the importance of glycans and lectins in regulating mechanisms of toxicity, creation of pores in the target cell membrane, and bacterial growth. Full article
(This article belongs to the Special Issue Lectins)

Review

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Open AccessReview Lectins with Potential for Anti-Cancer Therapy
Molecules 2015, 20(3), 3791-3810; doi:10.3390/molecules20033791
Received: 2 December 2014 / Revised: 13 February 2015 / Accepted: 15 February 2015 / Published: 26 February 2015
Cited by 17 | PDF Full-text (929 KB) | HTML Full-text | XML Full-text
Abstract
This article reviews lectins of animal and plant origin that induce apoptosis and autophagy of cancer cells and hence possess the potential of being developed into anticancer drugs. Apoptosis-inducing lectins encompass galectins, C-type lectins, annexins, Haliotis discus discus lectin, Polygonatum odoratum lectin, mistletoe
[...] Read more.
This article reviews lectins of animal and plant origin that induce apoptosis and autophagy of cancer cells and hence possess the potential of being developed into anticancer drugs. Apoptosis-inducing lectins encompass galectins, C-type lectins, annexins, Haliotis discus discus lectin, Polygonatum odoratum lectin, mistletoe lectin, and concanavalin A, fucose-binding Dicentrarchus labrax lectin, and Strongylocentrotus purpuratus lectin, Polygonatum odoratum lectin, and mistletoe lectin, Polygonatum odoratum lectin, autophagy inducing lectins include annexins and Polygonatum odoratum lectin. Full article
(This article belongs to the Special Issue Lectins)
Open AccessReview Nkrp1 Family, from Lectins to Protein Interacting Molecules
Molecules 2015, 20(2), 3463-3478; doi:10.3390/molecules20023463
Received: 15 November 2014 / Revised: 6 February 2015 / Accepted: 11 February 2015 / Published: 17 February 2015
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Abstract
The C-type lectin-like receptors include the Nkrp1 protein family that regulates the activity of natural killer (NK) cells. Rat Nkrp1a was reported to bind monosaccharide moieties in a Ca2+-dependent manner in preference order of GalNac > GlcNAc >> Fuc >> Gal
[...] Read more.
The C-type lectin-like receptors include the Nkrp1 protein family that regulates the activity of natural killer (NK) cells. Rat Nkrp1a was reported to bind monosaccharide moieties in a Ca2+-dependent manner in preference order of GalNac > GlcNAc >> Fuc >> Gal > Man. These findings established for rat Nkrp1a have been extrapolated to all additional Nkrp1 receptors and have been supported by numerous studies over the past two decades. However, since 1996 there has been controversy and another article showed lack of interactions with saccharides in 1999. Nevertheless, several high affinity saccharide ligands were synthesized in order to utilize their potential in antitumor therapy. Subsequently, protein ligands were introduced as specific binders for Nkrp1 proteins and three dimensional models of receptor/protein ligand interaction were derived from crystallographic data. Finally, for at least some members of the NK cell C-type lectin-like proteins, the “sweet story” was impaired by two reports in recent years. It has been shown that the rat Nkrp1a and CD69 do not bind saccharide ligands such as GlcNAc, GalNAc, chitotetraose and saccharide derivatives (GlcNAc-PAMAM) do not directly and specifically influence cytotoxic activity of NK cells as it was previously described. Full article
(This article belongs to the Special Issue Lectins)
Open AccessReview Entamoeba histolytica: Adhesins and Lectins in the Trophozoite Surface
Molecules 2015, 20(2), 2802-2815; doi:10.3390/molecules20022802
Received: 16 November 2014 / Accepted: 13 January 2015 / Published: 9 February 2015
Cited by 3 | PDF Full-text (685 KB) | HTML Full-text | XML Full-text
Abstract
Entamoeba histolytica is the causative agent of amebiasis in humans and is responsible for 100,000 deaths annually, making it the third leading cause of death due to a protozoan parasite. Pathogenesis appears to result from the potent cytotoxic activity of the parasite, which
[...] Read more.
Entamoeba histolytica is the causative agent of amebiasis in humans and is responsible for 100,000 deaths annually, making it the third leading cause of death due to a protozoan parasite. Pathogenesis appears to result from the potent cytotoxic activity of the parasite, which kills host cells within minutes. Although the mechanism is unknown, it is well established to be contact-dependent. The life cycle of the parasite alternates with two forms: the resistant cyst and the invasive trophozoite. The adhesive interactions between the parasite and surface glycoconjugates of host cells, as well as those lining the epithelia, are determinants for invasion of human tissues, for its cytotoxic activity, and finally for the outcome of the disease. In this review we present an overview of the information available on the amebic lectins and adhesins that are responsible of those adhesive interactions and we also refer to their effect on the host immune response. Finally, we present some concluding remarks and perspectives in the field. Full article
(This article belongs to the Special Issue Lectins)
Open AccessReview Elderberries: A Source of Ribosome-Inactivating Proteins with Lectin Activity
Molecules 2015, 20(2), 2364-2387; doi:10.3390/molecules20022364
Received: 17 November 2014 / Revised: 20 January 2015 / Accepted: 22 January 2015 / Published: 30 January 2015
Cited by 5 | PDF Full-text (2152 KB) | HTML Full-text | XML Full-text
Abstract
Sambucus (Adoxaceae) species have been used for both food and medicine purposes. Among these, Sambucus nigra L. (black elder), Sambucus ebulus L. (dwarf elder), and Sambucus sieboldiana L. are the most relevant species studied. Their use has been somewhat restricted due
[...] Read more.
Sambucus (Adoxaceae) species have been used for both food and medicine purposes. Among these, Sambucus nigra L. (black elder), Sambucus ebulus L. (dwarf elder), and Sambucus sieboldiana L. are the most relevant species studied. Their use has been somewhat restricted due to the presence of bioactive proteins or/and low molecular weight compounds whose ingestion could trigger deleterious effects. Over the last few years, the chemical and pharmacological characteristics of Sambucus species have been investigated. Among the proteins present in Sambucus species both type 1, and type 2 ribosome-inactivating proteins (RIPs), and hololectins have been reported. The biological role played by these proteins remains unknown, although they are conjectured to be involved in defending plants against insect predators and viruses. These proteins might have an important impact on the nutritional characteristics and food safety of elderberries. Type 2 RIPs are able to interact with gut cells of insects and mammals triggering a number of specific and mostly unknown cell signals in the gut mucosa that could significantly affect animal physiology. In this paper, we describe all known RIPs that have been isolated to date from Sambucus species, and comment on their antiviral and entomotoxic effects, as well as their potential uses. Full article
(This article belongs to the Special Issue Lectins)
Open AccessReview Emerging Structural Insights into Glycoprotein Quality Control Coupled with N-Glycan Processing in the Endoplasmic Reticulum
Molecules 2015, 20(2), 2475-2491; doi:10.3390/molecules20022475
Received: 8 December 2014 / Revised: 4 January 2015 / Accepted: 22 January 2015 / Published: 30 January 2015
Cited by 9 | PDF Full-text (3221 KB) | HTML Full-text | XML Full-text
Abstract
In the endoplasmic reticulum (ER), the sugar chain is initially introduced onto newly synthesized proteins as a triantennary tetradecasaccharide (Glc3Man9GlcNAc2). The attached oligosaccharide chain is subjected to stepwise trimming by the actions of specific glucosidases and mannosidases.
[...] Read more.
In the endoplasmic reticulum (ER), the sugar chain is initially introduced onto newly synthesized proteins as a triantennary tetradecasaccharide (Glc3Man9GlcNAc2). The attached oligosaccharide chain is subjected to stepwise trimming by the actions of specific glucosidases and mannosidases. In these processes, the transiently expressed N-glycans, as processing intermediates, function as signals for the determination of glycoprotein fates, i.e., folding, transport, or degradation through interactions of a series of intracellular lectins. The monoglucosylated glycoforms are hallmarks of incompletely folded states of glycoproteins in this system, whereas the outer mannose trimming leads to ER-associated glycoprotein degradation. This review outlines the recently emerging evidence regarding the molecular and structural basis of this glycoprotein quality control system, which is regulated through dynamic interplay among intracellular lectins, glycosidases, and glycosyltransferase. Structural snapshots of carbohydrate-lectin interactions have been provided at the atomic level using X-ray crystallographic analyses. Conformational ensembles of uncomplexed triantennary high-mannose-type oligosaccharides have been characterized in a quantitative manner using molecular dynamics simulation in conjunction with nuclear magnetic resonance spectroscopy. These complementary views provide new insights into glycoprotein recognition in quality control coupled with N-glycan processing. Full article
(This article belongs to the Special Issue Lectins)
Open AccessReview Human Lectins and Their Roles in Viral Infections
Molecules 2015, 20(2), 2229-2271; doi:10.3390/molecules20022229
Received: 17 November 2014 / Revised: 21 January 2015 / Accepted: 23 January 2015 / Published: 29 January 2015
Cited by 12 | PDF Full-text (2601 KB) | HTML Full-text | XML Full-text
Abstract
Innate recognition of virus proteins is an important component of the immune response to viral pathogens. A component of this immune recognition is the family of lectins; pattern recognition receptors (PRRs) that recognise viral pathogen-associated molecular patterns (PAMPs) including viral glycoproteins. In this
[...] Read more.
Innate recognition of virus proteins is an important component of the immune response to viral pathogens. A component of this immune recognition is the family of lectins; pattern recognition receptors (PRRs) that recognise viral pathogen-associated molecular patterns (PAMPs) including viral glycoproteins. In this review we discuss the contribution of soluble and membrane-associated PRRs to immunity against virus pathogens, and the potential role of these molecules in facilitating virus replication. These processes are illustrated with examples of viruses including human immunodeficiency virus (HIV), hepatitis C virus (HCV) and Ebola virus (EBOV). We focus on the structure, function and genetics of the well-characterised C-type lectin mannose-binding lectin, the ficolins, and the membrane-bound CD209 proteins expressed on dendritic cells. The potential for lectin-based antiviral therapies is also discussed. Full article
(This article belongs to the Special Issue Lectins)
Open AccessReview The Roles of Direct Recognition by Animal Lectins in Antiviral Immunity and Viral Pathogenesis
Molecules 2015, 20(2), 2272-2295; doi:10.3390/molecules20022272
Received: 28 August 2014 / Accepted: 21 January 2015 / Published: 29 January 2015
Cited by 5 | PDF Full-text (3659 KB) | HTML Full-text | XML Full-text
Abstract
Lectins are a group of proteins with carbohydrate recognition activity. Lectins are categorized into many families based on their different cellular locations as well as their specificities for a variety of carbohydrate structures due to the features of their carbohydrate recognition domain (CRD)
[...] Read more.
Lectins are a group of proteins with carbohydrate recognition activity. Lectins are categorized into many families based on their different cellular locations as well as their specificities for a variety of carbohydrate structures due to the features of their carbohydrate recognition domain (CRD) modules. Many studies have indicated that the direct recognition of particular oligosaccharides on viral components by lectins is important for interactions between hosts and viruses. Herein, we aim to globally review the roles of this recognition by animal lectins in antiviral immune responses and viral pathogenesis. The different classes of mammalian lectins can either recognize carbohydrates to activate host immunity for viral elimination or can exploit those carbohydrates as susceptibility factors to facilitate viral entry, replication or assembly. Additionally, some arthropod C-type lectins were recently identified as key susceptibility factors that directly interact with multiple viruses and then facilitate infection. Summarization of the pleiotropic roles of direct viral recognition by animal lectins will benefit our understanding of host-virus interactions and could provide insight into the role of lectins in antiviral drug and vaccine development. Full article
(This article belongs to the Special Issue Lectins)
Open AccessReview Insecticidal Activity of Plant Lectins and Potential Application in Crop Protection
Molecules 2015, 20(2), 2014-2033; doi:10.3390/molecules20022014
Received: 8 November 2014 / Revised: 15 January 2015 / Accepted: 19 January 2015 / Published: 27 January 2015
Cited by 10 | PDF Full-text (876 KB) | HTML Full-text | XML Full-text
Abstract
Lectins constitute a complex group of proteins found in different organisms. These proteins constitute an important field for research, as their structural diversity and affinity for several carbohydrates makes them suitable for numerous biological applications. This review addresses the classification and insecticidal activities
[...] Read more.
Lectins constitute a complex group of proteins found in different organisms. These proteins constitute an important field for research, as their structural diversity and affinity for several carbohydrates makes them suitable for numerous biological applications. This review addresses the classification and insecticidal activities of plant lectins, providing an overview of the applicability of these proteins in crop protection. The likely target sites in insect tissues, the mode of action of these proteins, as well as the use of lectins as biotechnological tools for pest control are also described. The use of initial bioassays employing artificial diets has led to the most recent advances in this field, such as plant breeding and the construction of fusion proteins, using lectins for targeting the delivery of toxins and to potentiate expected insecticide effects. Based on the data presented, we emphasize the contribution that plant lectins may make as tools for the development of integrated insect pest control strategies. Full article
(This article belongs to the Special Issue Lectins)
Open AccessReview Lectins: Getting Familiar with Translators of the Sugar Code
Molecules 2015, 20(2), 1788-1823; doi:10.3390/molecules20021788
Received: 2 December 2014 / Revised: 23 December 2014 / Accepted: 8 January 2015 / Published: 22 January 2015
Cited by 22 | PDF Full-text (27563 KB) | HTML Full-text | XML Full-text
Abstract
The view on the significance of the presence of glycans in glycoconjugates is undergoing a paradigmatic change. Initially mostly considered to be rather inert and passive, the concept of the sugar code identifies glycans as highly versatile platform to store information. Their chemical
[...] Read more.
The view on the significance of the presence of glycans in glycoconjugates is undergoing a paradigmatic change. Initially mostly considered to be rather inert and passive, the concept of the sugar code identifies glycans as highly versatile platform to store information. Their chemical properties endow carbohydrates to form oligomers with unsurpassed structural variability. Owing to their capacity to engage in hydrogen (and coordination) bonding and C-H/π-interactions these “code words” can be “read” (in Latin, legere) by specific receptors. A distinct class of carbohydrate-binding proteins are the lectins. More than a dozen protein folds have developed carbohydrate-binding capacity in vertebrates. Taking galectins as an example, distinct expression patterns are traced. The availability of labeled endogenous lectins facilitates monitoring of tissue reactivity, extending the scope of lectin histochemistry beyond that which traditionally involved plant lectins. Presentation of glycan and its cognate lectin can be orchestrated, making a glycan-based effector pathway in growth control of tumor and activated T cells possible. In order to unravel the structural basis of lectin specificity for particular glycoconjugates mimetics of branched glycans and programmable models of cell surfaces are being developed by strategic combination of lectin research with synthetic and supramolecular chemistry. Full article
(This article belongs to the Special Issue Lectins)
Open AccessReview The Giant Adhesin SiiE of Salmonella enterica
Molecules 2015, 20(1), 1134-1150; doi:10.3390/molecules20011134
Received: 16 November 2014 / Accepted: 4 January 2015 / Published: 12 January 2015
Cited by 1 | PDF Full-text (5784 KB) | HTML Full-text | XML Full-text
Abstract
Salmonella enterica is a Gram-negative, food-borne pathogen, which colonizes the intestinal tract and invades enterocytes. Invasion of polarized cells depends on the SPI1-encoded type III secretion system (T3SS) and the SPI4-encoded type I secretion system (T1SS). The substrate of this T1SS is the
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Salmonella enterica is a Gram-negative, food-borne pathogen, which colonizes the intestinal tract and invades enterocytes. Invasion of polarized cells depends on the SPI1-encoded type III secretion system (T3SS) and the SPI4-encoded type I secretion system (T1SS). The substrate of this T1SS is the non-fimbrial giant adhesin SiiE. With a size of 595 kDa, SiiE is the largest protein of the Salmonella proteome and consists of 53 repetitive bacterial immunoglobulin (BIg) domains, each containing several conserved residues. As known for other T1SS substrates, such as E. coli HlyA, Ca2+ ions bound by conserved D residues within the BIg domains stabilize the protein and facilitate secretion. The adhesin SiiE mediates the first contact to the host cell and thereby positions the SPI1-T3SS to initiate the translocation of a cocktail of effector proteins. This leads to actin remodeling, membrane ruffle formation and bacterial internalization. SiiE binds to host cell apical membranes in a lectin-like manner. GlcNAc and α2–3 linked sialic acid-containing structures are ligands of SiiE. Since SiiE shows repetitive domain architecture, we propose a zipper-like binding mediated by each individual BIg domain. In this review, we discuss the characteristics of the SPI4-T1SS and the giant adhesin SiiE. Full article
(This article belongs to the Special Issue Lectins)
Open AccessReview The Lectin Frontier Database (LfDB), and Data Generation Based on Frontal Affinity Chromatography
Molecules 2015, 20(1), 951-973; doi:10.3390/molecules20010951
Received: 24 November 2014 / Accepted: 31 December 2014 / Published: 8 January 2015
Cited by 4 | PDF Full-text (1667 KB) | HTML Full-text | XML Full-text
Abstract
Lectins are a large group of carbohydrate-binding proteins, having been shown to comprise at least 48 protein scaffolds or protein family entries. They occur ubiquitously in living organisms—from humans to microorganisms, including viruses—and while their functions are yet to be fully elucidated, their
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Lectins are a large group of carbohydrate-binding proteins, having been shown to comprise at least 48 protein scaffolds or protein family entries. They occur ubiquitously in living organisms—from humans to microorganisms, including viruses—and while their functions are yet to be fully elucidated, their main underlying actions are thought to mediate cell-cell and cell-glycoconjugate interactions, which play important roles in an extensive range of biological processes. The basic feature of each lectin’s function resides in its specific sugar-binding properties. In this regard, it is beneficial for researchers to have access to fundamental information about the detailed oligosaccharide specificities of diverse lectins. In this review, the authors describe a publicly available lectin database named “Lectin frontier DataBase (LfDB)”, which undertakes the continuous publication and updating of comprehensive data for lectin-standard oligosaccharide interactions in terms of dissociation constants (Kd’s). For Kd determination, an advanced system of frontal affinity chromatography (FAC) is used, with which quantitative datasets of interactions between immobilized lectins and >100 fluorescently labeled standard glycans have been generated. The FAC system is unique in its clear principle, simple procedure and high sensitivity, with an increasing number (>67) of associated publications that attest to its reliability. Thus, LfDB, is expected to play an essential role in lectin research, not only in basic but also in applied fields of glycoscience. Full article
(This article belongs to the Special Issue Lectins)
Open AccessReview Lectins with Anti-HIV Activity: A Review
Molecules 2015, 20(1), 648-668; doi:10.3390/molecules20010648
Received: 17 November 2014 / Accepted: 29 November 2014 / Published: 6 January 2015
Cited by 13 | PDF Full-text (719 KB) | HTML Full-text | XML Full-text
Abstract
Lectins including flowering plant lectins, algal lectins, cyanobacterial lectins, actinomycete lectin, worm lectins, and the nonpeptidic lectin mimics pradimicins and benanomicins, exhibit anti-HIV activity. The anti-HIV plant lectins include Artocarpus heterophyllus (jacalin) lectin, concanavalin A, Galanthus nivalis (snowdrop) agglutinin-related lectins, Musa acuminata
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Lectins including flowering plant lectins, algal lectins, cyanobacterial lectins, actinomycete lectin, worm lectins, and the nonpeptidic lectin mimics pradimicins and benanomicins, exhibit anti-HIV activity. The anti-HIV plant lectins include Artocarpus heterophyllus (jacalin) lectin, concanavalin A, Galanthus nivalis (snowdrop) agglutinin-related lectins, Musa acuminata (banana) lectin, Myrianthus holstii lectin, Narcissus pseudonarcissus lectin, and Urtica diocia agglutinin. The anti-HIV algal lectins comprise Boodlea coacta lectin, Griffithsin, Oscillatoria agardhii agglutinin. The anti-HIV cyanobacterial lectins are cyanovirin-N, scytovirin, Microcystis viridis lectin, and microvirin. Actinohivin is an anti-HIV actinomycete lectin. The anti-HIV worm lectins include Chaetopterus variopedatus polychaete marine worm lectin, Serpula vermicularis sea worm lectin, and C-type lectin Mermaid from nematode (Laxus oneistus). The anti-HIV nonpeptidic lectin mimics comprise pradimicins and benanomicins. Their anti-HIV mechanisms are discussed. Full article
(This article belongs to the Special Issue Lectins)
Open AccessReview Insights into Animal and Plant Lectins with Antimicrobial Activities
Molecules 2015, 20(1), 519-541; doi:10.3390/molecules20010519
Received: 7 November 2014 / Accepted: 22 December 2014 / Published: 5 January 2015
Cited by 13 | PDF Full-text (1730 KB) | HTML Full-text | XML Full-text
Abstract
Lectins are multivalent proteins with the ability to recognize and bind diverse carbohydrate structures. The glyco -binding and diverse molecular structures observed in these protein classes make them a large and heterogeneous group with a wide range of biological activities in microorganisms, animals
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Lectins are multivalent proteins with the ability to recognize and bind diverse carbohydrate structures. The glyco -binding and diverse molecular structures observed in these protein classes make them a large and heterogeneous group with a wide range of biological activities in microorganisms, animals and plants. Lectins from plants and animals are commonly used in direct defense against pathogens and in immune regulation. This review focuses on sources of animal and plant lectins, describing their functional classification and tridimensional structures, relating these properties with biotechnological purposes, including antimicrobial activities. In summary, this work focuses on structural-functional elucidation of diverse lectin groups, shedding some light on host-pathogen interactions; it also examines their emergence as biotechnological tools through gene manipulation and development of new drugs. Full article
(This article belongs to the Special Issue Lectins)
Open AccessReview Lectins from Edible Mushrooms
Molecules 2015, 20(1), 446-469; doi:10.3390/molecules20010446
Received: 6 November 2014 / Accepted: 23 December 2014 / Published: 31 December 2014
Cited by 10 | PDF Full-text (746 KB) | HTML Full-text | XML Full-text
Abstract
Mushrooms are famous for their nutritional and medicinal values and also for the diversity of bioactive compounds they contain including lectins. The present review is an attempt to summarize and discuss data available on molecular weights, structures, biological properties, N-terminal sequences and possible
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Mushrooms are famous for their nutritional and medicinal values and also for the diversity of bioactive compounds they contain including lectins. The present review is an attempt to summarize and discuss data available on molecular weights, structures, biological properties, N-terminal sequences and possible applications of lectins from edible mushrooms. It further aims to update and discuss/examine the recent advancements in the study of these lectins regarding their structures, functions, and exploitable properties. A detailed tabling of all the available data for N-terminal sequences of these lectins is also presented here. Full article
(This article belongs to the Special Issue Lectins)
Open AccessReview Marine Sponge Lectins: Actual Status on Properties and Biological Activities
Molecules 2015, 20(1), 348-357; doi:10.3390/molecules20010348
Received: 15 September 2014 / Accepted: 18 December 2014 / Published: 26 December 2014
Cited by 3 | PDF Full-text (1449 KB) | HTML Full-text | XML Full-text
Abstract
Marine sponges are primitive metazoans that produce a wide variety of molecules that protect them against predators. In studies that search for bioactive molecules, these marine invertebrates stand out as promising sources of new biologically-active molecules, many of which are still unknown or
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Marine sponges are primitive metazoans that produce a wide variety of molecules that protect them against predators. In studies that search for bioactive molecules, these marine invertebrates stand out as promising sources of new biologically-active molecules, many of which are still unknown or little studied; thus being an unexplored biotechnological resource of high added value. Among these molecules, lectins are proteins that reversibly bind to carbohydrates without modifying them. In this review, various structural features and biological activities of lectins derived from marine sponges so far described in the scientific literature are discussed. From the results found in the literature, it could be concluded that lectins derived from marine sponges are structurally diverse proteins with great potential for application in the production of biopharmaceuticals, especially as antibacterial and antitumor agents. Full article
(This article belongs to the Special Issue Lectins)
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Open AccessReview Banana Lectin: A Brief Review
Molecules 2014, 19(11), 18817-18827; doi:10.3390/molecules191118817
Received: 9 October 2014 / Revised: 5 November 2014 / Accepted: 12 November 2014 / Published: 17 November 2014
Cited by 5 | PDF Full-text (254 KB) | HTML Full-text | XML Full-text
Abstract
Lectins are a group of proteins of non-immune origin that recognize and bind to carbohydrates without modifying them. Banana is the common name for both herbaceous plants of the genus Musa and for the fruit they produce. They are indeed a promising source
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Lectins are a group of proteins of non-immune origin that recognize and bind to carbohydrates without modifying them. Banana is the common name for both herbaceous plants of the genus Musa and for the fruit they produce. They are indeed a promising source for many medicinal applications. Banana lectins have the potential for inhibiting HIV-1 reverse transcriptase activity, suppressing cancer cell proliferation and stimulating macrophage activities. Nevertheless, compared to other plant lectins, there is relatively little information in the literature on banana lectins, particularly with respect to their structure and biological functions. Herein we focus our review on the structure, functions and exploitable properties of banana lectins. Full article
(This article belongs to the Special Issue Lectins)

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Open AccessCorrection Correction: Hasan, I., et al. A Galactose-Binding Lectin Isolated from Aplysia kurodai (Sea Hare) Eggs Inhibits Streptolysin-Induced Hemolysis. Molecules 2014, 19, 13990–14003
Molecules 2016, 21(1), 129; doi:10.3390/molecules21010129
Received: 4 January 2016 / Accepted: 6 January 2016 / Published: 21 January 2016
PDF Full-text (153 KB) | HTML Full-text | XML Full-text
Abstract The authors wish to make the following correction to their paper [1]. [...] Full article
(This article belongs to the Special Issue Lectins)

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