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Special Issue "Plant Lectins: From Model Species to Crop Plants"

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Botany".

Deadline for manuscript submissions: closed (30 April 2017)

Special Issue Editor

Guest Editor
Prof. Dr. Els Van Damme

Ghent University, Belgium
Website | E-Mail
Interests: lectins; carbohydrate-binding proteins; protein-carbohydrate interactions; carbohydrate recognition; glycosylation; biological activity; ribosome inactivating proteins; toxin domain; physiological importance; defense and immunity; stress proteins; glycobiology

Special Issue Information

Dear Colleagues,

Lectins—also called carbohydrate-binding proteins—are defined as “proteins that possess at least one non-catalytic domain that binds reversibly to a specific mono- or oligosaccharide”. Numerous plant species consist of one or more proteins containing a lectin domain, enabling these proteins to recognize and bind to specific carbohydrate structures. The group of plant lectins is quite heterogeneous since lectins differ in their molecular structure, specificity for carbohydrate structures, and biological activities. The significant expansion of available genome sequence data enabled the retrieval of sequences encoding lectin motifs from every plant species studied. Based on the sequence conservation of their carbohydrate-recognition domain, plant lectins can be divided into different families of evolutionary related proteins. In spite of decades of research, the function of most lectins has not yet been elucidated.

Protein-carbohydrate interactions underlie many important biological events, including cellular signalling and recognition processes. Carbohydrate chains of glycoproteins, glycolipids, proteoglycans, and polysaccharides play a fundamental role in multiple biological processes. Although there is strong evidence for the importance of protein-carbohydrate interactions in vertebrates, little is known on their implications for the growth and development of plants.

In this Special Issue we aim to collect manuscripts from different research disciplines covering the current knowledge of plant lectins, their molecular characteristics, their biological activities, and their applications.

Prof. Els Van Damme
Guest Editor

Manuscript Submission Information

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. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short 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 thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences 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). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • lectin
  • agglutinin
  • protein carbohydrate interaction
  • carbohydrate binding
  • glycan
  • sugar specificity
  • biological activity
  • evolution

Published Papers (12 papers)

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Research

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Open AccessArticle ArtinM Mediates Murine T Cell Activation and Induces Cell Death in Jurkat Human Leukemic T Cells
Int. J. Mol. Sci. 2017, 18(7), 1400; doi:10.3390/ijms18071400
Received: 8 May 2017 / Revised: 22 June 2017 / Accepted: 25 June 2017 / Published: 30 June 2017
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Abstract
The recognition of cell surface glycans by lectins may be critical for the innate and adaptive immune responses. ArtinM, a d-mannose-binding lectin from Artocarpus heterophyllus, activates antigen-presenting cells by recognizing TLR2 N-glycans and induces Th1 immunity. We recently demonstrated that
[...] Read more.
The recognition of cell surface glycans by lectins may be critical for the innate and adaptive immune responses. ArtinM, a d-mannose-binding lectin from Artocarpus heterophyllus, activates antigen-presenting cells by recognizing TLR2 N-glycans and induces Th1 immunity. We recently demonstrated that ArtinM stimulated CD4+ T cells to produce proinflammatory cytokines. Here, we further studied the effects of ArtinM on adaptive immune cells. We showed that ArtinM activates murine CD4+ and CD8+ T cells, augmenting their positivity for CD25, CD69, and CD95 and showed higher interleukin (IL)-2 and interferon (IFN)-γ production. The CD4+ T cells exhibited increased T-bet expression in response to ArtinM, and IL-2 production by CD4+ and CD8+ T cells depended on the recognition of CD3εγ-chain glycans by ArtinM. The ArtinM effect on aberrantly-glycosylated neoplastic lymphocytes was studied in Jurkat T cells, in which ArtinM induced IL-2, IFN-γ, and IL-1β production, but decreased cell viability and growth. A higher frequency of AnnexinV- and propidium iodide-stained cells demonstrated the induction of Jurkat T cells apoptosis by ArtinM, and this apoptotic response was reduced by caspases and protein tyrosine kinase inhibitors. The ArtinM effects on murine T cells corroborated with the immunomodulatory property of lectin, whereas the promotion of Jurkat T cells apoptosis may reflect a potential applicability of ArtinM in novel strategies for treating lymphocytic leukemia. Full article
(This article belongs to the Special Issue Plant Lectins: From Model Species to Crop Plants)
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Open AccessArticle Sugar-Binding Profiles of Chitin-Binding Lectins from the Hevein Family: A Comprehensive Study
Int. J. Mol. Sci. 2017, 18(6), 1160; doi:10.3390/ijms18061160
Received: 28 April 2017 / Revised: 18 May 2017 / Accepted: 21 May 2017 / Published: 30 May 2017
Cited by 1 | PDF Full-text (2912 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
Chitin-binding lectins form the hevein family in plants, which are defined by the presence of single or multiple structurally conserved GlcNAc (N-acetylglucosamine)-binding domains. Although they have been used as probes for chito-oligosaccharides, their detailed specificities remain to be investigated. In this
[...] Read more.
Chitin-binding lectins form the hevein family in plants, which are defined by the presence of single or multiple structurally conserved GlcNAc (N-acetylglucosamine)-binding domains. Although they have been used as probes for chito-oligosaccharides, their detailed specificities remain to be investigated. In this study, we analyzed six chitin-binding lectins, DSA, LEL, PWM, STL, UDA, and WGA, by quantitative frontal affinity chromatography. Some novel features were evident: WGA showed almost comparable affinity for pyridylaminated chitotriose and chitotetraose, while LEL and UDA showed much weaker affinity, and DSA, PWM, and STL had no substantial affinity for the former. WGA showed selective affinity for hybrid-type N-glycans harboring a bisecting GlcNAc residue. UDA showed extensive binding to high-mannose type N-glycans, with affinity increasing with the number of Man residues. DSA showed the highest affinity for highly branched N-glycans consisting of type II LacNAc (N-acetyllactosamine). Further, multivalent features of these lectins were investigated by using glycoconjugate and lectin microarrays. The lectins showed substantial binding to immobilized LacNAc as well as chito-oligosaccharides, although the extents to which they bound varied among them. WGA showed strong binding to heavily sialylated glycoproteins. The above observations will help interpret lectin-glycoprotein interactions in histochemical studies and glyco-biomarker investigations. Full article
(This article belongs to the Special Issue Plant Lectins: From Model Species to Crop Plants)
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Open AccessArticle Comparative Study of Lectin Domains in Model Species: New Insights into Evolutionary Dynamics
Int. J. Mol. Sci. 2017, 18(6), 1136; doi:10.3390/ijms18061136
Received: 6 May 2017 / Revised: 20 May 2017 / Accepted: 22 May 2017 / Published: 25 May 2017
PDF Full-text (12743 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
Lectins are present throughout the plant kingdom and are reported to be involved in diverse biological processes. In this study, we provide a comparative analysis of the lectin families from model species in a phylogenetic framework. The analysis focuses on the different plant
[...] Read more.
Lectins are present throughout the plant kingdom and are reported to be involved in diverse biological processes. In this study, we provide a comparative analysis of the lectin families from model species in a phylogenetic framework. The analysis focuses on the different plant lectin domains identified in five representative core angiosperm genomes (Arabidopsis thaliana, Glycine max, Cucumis sativus, Oryza sativa ssp. japonica and Oryza sativa ssp. indica). The genomes were screened for genes encoding lectin domains using a combination of Basic Local Alignment Search Tool (BLAST), hidden Markov models, and InterProScan analysis. Additionally, phylogenetic relationships were investigated by constructing maximum likelihood phylogenetic trees. The results demonstrate that the majority of the lectin families are present in each of the species under study. Domain organization analysis showed that most identified proteins are multi-domain proteins, owing to the modular rearrangement of protein domains during evolution. Most of these multi-domain proteins are widespread, while others display a lineage-specific distribution. Furthermore, the phylogenetic analyses reveal that some lectin families evolved to be similar to the phylogeny of the plant species, while others share a closer evolutionary history based on the corresponding protein domain architecture. Our results yield insights into the evolutionary relationships and functional divergence of plant lectins. Full article
(This article belongs to the Special Issue Plant Lectins: From Model Species to Crop Plants)
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Open AccessArticle Isolation of Rice Bran Lectins and Characterization of Their Unique Behavior in Caco-2 Cells
Int. J. Mol. Sci. 2017, 18(5), 1052; doi:10.3390/ijms18051052
Received: 29 March 2017 / Revised: 5 May 2017 / Accepted: 10 May 2017 / Published: 13 May 2017
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Abstract
Rice bran lectins, named as RBA1 and RBA2, were isolated from Oryza sativa in two chromatography steps: affinity chromatography and cation-exchange chromatography. RBA1 was found to be composed of a covalently linked heterodimer of 20- and 12-kDa subunits, and RBA2 was a noncovalently
[...] Read more.
Rice bran lectins, named as RBA1 and RBA2, were isolated from Oryza sativa in two chromatography steps: affinity chromatography and cation-exchange chromatography. RBA1 was found to be composed of a covalently linked heterodimer of 20- and 12-kDa subunits, and RBA2 was a noncovalently linked dimer of 12-kDa subunits. Both RBA1 and RBA2 bound to desialylated complex glycoproteins such as fetuin, α1-acid glycoprotein, and transferrin, and agalactosylated complex glycoproteins such as agalacto fetuin, agalacto-α1-acid glycoprotein, and agalacto-transferrin, in addition to chitooligosacchrides. RBAs were heat stable up to 80 °C and stable at pH 4–10. RBA1 increased the transport of the fluorescent marker, rhodamine 123, which is known to be transported via the P-glycoprotein-mediated efflux pathway across human intestinal Caco-2 cell monolayers. Furthermore, RBA1 itself was transported to the basolateral side of the monolayers via an endocytotic pathway. Full article
(This article belongs to the Special Issue Plant Lectins: From Model Species to Crop Plants)
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Open AccessArticle Anti-Neuroblastoma Properties of a Recombinant Sunflower Lectin
Int. J. Mol. Sci. 2017, 18(1), 92; doi:10.3390/ijms18010092
Received: 25 November 2016 / Revised: 18 December 2016 / Accepted: 20 December 2016 / Published: 10 January 2017
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Abstract
According to their sugar recognition specificity, plant lectins are proposed as bioactive proteins with potential in cancer treatment and diagnosis. Helja is a mannose-specific jacalin-like lectin from sunflower which was shown to inhibit the growth of certain fungi. Here, we report its recombinant
[...] Read more.
According to their sugar recognition specificity, plant lectins are proposed as bioactive proteins with potential in cancer treatment and diagnosis. Helja is a mannose-specific jacalin-like lectin from sunflower which was shown to inhibit the growth of certain fungi. Here, we report its recombinant expression in a prokaryotic system and its activity in neurobalstoma cells. Helja coding sequence was fused to the pET-32 EK/LIC, the enterokinase/Ligation-independent cloning vector and a 35 kDa protein was obtained in Escherichia coli representing Helja coupled to thioredoxin (Trx). The identity of this protein was verified using anti-Helja antibodies. This chimera, named Trx-rHelja, was enriched in the soluble bacterial extracts and was purified using Ni+2-Sepharose and d-mannose-agarose chromatography. Trx-rHelja and the enterokinase-released recombinant Helja (rHelja) both displayed toxicity on human SH-SY5Y neuroblastomas. rHelja decreased the viability of these tumor cells by 75% according to the tetrazolium reduction assay, and microscopic analyses revealed that the cell morphology was disturbed. Thus, the stellate cells of the monolayer became spheroids and were isolated. Our results indicate that rHelja is a promising tool for the development of diagnostic or therapeutic methods for neuroblastoma cells, the most common solid tumors in childhood. Full article
(This article belongs to the Special Issue Plant Lectins: From Model Species to Crop Plants)
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Open AccessArticle The Distribution of Lectins across the Phylum Nematoda: A Genome-Wide Search
Int. J. Mol. Sci. 2017, 18(1), 91; doi:10.3390/ijms18010091
Received: 18 November 2016 / Revised: 20 December 2016 / Accepted: 28 December 2016 / Published: 4 January 2017
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Abstract
Nematodes are a very diverse phylum that has adapted to nearly every ecosystem. They have developed specialized lifestyles, dividing the phylum into free-living, animal, and plant parasitic species. Their sheer abundance in numbers and presence in nearly every ecosystem make them the most
[...] Read more.
Nematodes are a very diverse phylum that has adapted to nearly every ecosystem. They have developed specialized lifestyles, dividing the phylum into free-living, animal, and plant parasitic species. Their sheer abundance in numbers and presence in nearly every ecosystem make them the most prevalent animals on earth. In this research nematode-specific profiles were designed to retrieve predicted lectin-like domains from the sequence data of nematode genomes and transcriptomes. Lectins are carbohydrate-binding proteins that play numerous roles inside and outside the cell depending on their sugar specificity and associated protein domains. The sugar-binding properties of the retrieved lectin-like proteins were predicted in silico. Although most research has focused on C-type lectin-like, galectin-like, and calreticulin-like proteins in nematodes, we show that the lectin-like repertoire in nematodes is far more diverse. We focused on C-type lectins, which are abundantly present in all investigated nematode species, but seem to be far more abundant in free-living species. Although C-type lectin-like proteins are omnipresent in nematodes, we have shown that only a small part possesses the residues that are thought to be essential for carbohydrate binding. Curiously, hevein, a typical plant lectin domain not reported in animals before, was found in some nematode species. Full article
(This article belongs to the Special Issue Plant Lectins: From Model Species to Crop Plants)
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Review

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Open AccessReview An Update on Jacalin-Like Lectins and Their Role in Plant Defense
Int. J. Mol. Sci. 2017, 18(7), 1592; doi:10.3390/ijms18071592
Received: 30 June 2017 / Revised: 17 July 2017 / Accepted: 20 July 2017 / Published: 22 July 2017
Cited by 1 | PDF Full-text (3334 KB) | HTML Full-text | XML Full-text
Abstract
Plant lectins are proteins that reversibly bind carbohydrates and are assumed to play an important role in plant development and resistance. Through the binding of carbohydrate ligands, lectins are involved in the perception of environmental signals and their translation into phenotypical responses. These
[...] Read more.
Plant lectins are proteins that reversibly bind carbohydrates and are assumed to play an important role in plant development and resistance. Through the binding of carbohydrate ligands, lectins are involved in the perception of environmental signals and their translation into phenotypical responses. These processes require down-stream signaling cascades, often mediated by interacting proteins. Fusing the respective genes of two interacting proteins can be a way to increase the efficiency of this process. Most recently, proteins containing jacalin-related lectin (JRL) domains became a subject of plant resistance responses research. A meta-data analysis of fusion proteins containing JRL domains across different kingdoms revealed diverse partner domains ranging from kinases to toxins. Among them, proteins containing a JRL domain and a dirigent domain occur exclusively within monocotyledonous plants and show an unexpected high range of family member expansion compared to other JRL-fusion proteins. Rice, wheat, and barley plants overexpressing OsJAC1, a member of this family, are resistant against important fungal pathogens. We discuss the possibility that JRL domains also function as a decoy in fusion proteins and help to alert plants of the presence of attacking pathogens. Full article
(This article belongs to the Special Issue Plant Lectins: From Model Species to Crop Plants)
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Open AccessReview Plant Lectins as Medical Tools against Digestive System Cancers
Int. J. Mol. Sci. 2017, 18(7), 1403; doi:10.3390/ijms18071403
Received: 26 April 2017 / Revised: 21 June 2017 / Accepted: 25 June 2017 / Published: 3 July 2017
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Abstract
Digestive system cancers—those of the esophagus, stomach, small intestine, colon-rectum, liver, and pancreas—are highly related to genetics and lifestyle. Most are considered highly mortal due to the frequency of late diagnosis, usually in advanced stages, caused by the absence of symptoms or masked
[...] Read more.
Digestive system cancers—those of the esophagus, stomach, small intestine, colon-rectum, liver, and pancreas—are highly related to genetics and lifestyle. Most are considered highly mortal due to the frequency of late diagnosis, usually in advanced stages, caused by the absence of symptoms or masked by other pathologies. Different tools are being investigated in the search of a more precise diagnosis and treatment. Plant lectins have been studied because of their ability to recognize and bind to carbohydrates, exerting a variety of biological activities on animal cells, including anticancer activities. The present report integrates existing information on the activity of plant lectins on various types of digestive system cancers, and surveys the current state of research into their properties for diagnosis and selective treatment. Full article
(This article belongs to the Special Issue Plant Lectins: From Model Species to Crop Plants)
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Open AccessReview Lectins from Mycelia of Basidiomycetes
Int. J. Mol. Sci. 2017, 18(7), 1334; doi:10.3390/ijms18071334
Received: 27 April 2017 / Revised: 15 June 2017 / Accepted: 16 June 2017 / Published: 22 June 2017
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Abstract
Lectins are proteins of a nonimmunoglobulin nature that are capable of specific recognition of and reversible binding to the carbohydrate moieties of complex carbohydrates, without altering the covalent structure of any of the recognized glycosyl ligands. They have a broad range of biological
[...] Read more.
Lectins are proteins of a nonimmunoglobulin nature that are capable of specific recognition of and reversible binding to the carbohydrate moieties of complex carbohydrates, without altering the covalent structure of any of the recognized glycosyl ligands. They have a broad range of biological activities important for the functioning of the cell and the whole organism and, owing to the high specificity of reversible binding to carbohydrates, are valuable tools used widely in biology and medicine. Lectins can be produced by many living organisms, including basidiomycetes. Whereas lectins from the fruit bodies of basidiomycetes have been studied sufficiently well, mycelial lectins remain relatively unexplored. Here, we review and comparatively analyze what is currently known about lectins isolated from the vegetative mycelium of macrobasidiomycetes, including their localization, properties, and carbohydrate specificities. Particular attention is given to the physiological role of mycelial lectins in fungal growth and development. Full article
(This article belongs to the Special Issue Plant Lectins: From Model Species to Crop Plants)
Open AccessReview Legume Lectins: Proteins with Diverse Applications
Int. J. Mol. Sci. 2017, 18(6), 1242; doi:10.3390/ijms18061242
Received: 29 April 2017 / Revised: 1 June 2017 / Accepted: 5 June 2017 / Published: 12 June 2017
Cited by 2 | PDF Full-text (831 KB) | HTML Full-text | XML Full-text
Abstract
Lectins are a diverse class of proteins distributed extensively in nature. Among these proteins; legume lectins display a variety of interesting features including antimicrobial; insecticidal and antitumor activities. Because lectins recognize and bind to specific glycoconjugates present on the surface of cells and
[...] Read more.
Lectins are a diverse class of proteins distributed extensively in nature. Among these proteins; legume lectins display a variety of interesting features including antimicrobial; insecticidal and antitumor activities. Because lectins recognize and bind to specific glycoconjugates present on the surface of cells and intracellular structures; they can serve as potential target molecules for developing practical applications in the fields of food; agriculture; health and pharmaceutical research. This review presents the current knowledge of the main structural characteristics of legume lectins and the relationship of structure to the exhibited specificities; provides an overview of their particular antimicrobial; insecticidal and antitumor biological activities and describes possible applications based on the pattern of recognized glyco-targets. Full article
(This article belongs to the Special Issue Plant Lectins: From Model Species to Crop Plants)
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Open AccessReview Plant Lectins Targeting O-Glycans at the Cell Surface as Tools for Cancer Diagnosis, Prognosis and Therapy
Int. J. Mol. Sci. 2017, 18(6), 1232; doi:10.3390/ijms18061232
Received: 13 April 2017 / Revised: 26 May 2017 / Accepted: 31 May 2017 / Published: 9 June 2017
PDF Full-text (2728 KB) | HTML Full-text | XML Full-text
Abstract
Aberrant O-glycans expressed at the surface of cancer cells consist of membrane-tethered glycoproteins (T and Tn antigens) and glycolipids (Lewis a, Lewis x and Forssman antigens). All of these O-glycans have been identified as glyco-markers of interest for the diagnosis and
[...] Read more.
Aberrant O-glycans expressed at the surface of cancer cells consist of membrane-tethered glycoproteins (T and Tn antigens) and glycolipids (Lewis a, Lewis x and Forssman antigens). All of these O-glycans have been identified as glyco-markers of interest for the diagnosis and the prognosis of cancer diseases. These epitopes are specifically detected using T/Tn-specific lectins isolated from various plants such as jacalin from Artocarpus integrifola, and fungi such as the Agaricus bisporus lectin. These lectins accommodate T/Tn antigens at the monosaccharide-binding site; residues located in the surrounding extended binding-site of the lectins often participate in the binding of more extended epitopes. Depending on the shape and size of the extended carbohydrate-binding site, their fine sugar-binding specificity towards complex O-glycans readily differs from one lectin to another, resulting in a great diversity in their sugar-recognition capacity. T/Tn-specific lectins have been extensively used for the histochemical detection of cancer cells in biopsies and for the follow up of the cancer progression and evolution. T/Tn-specific lectins also induce a caspase-dependent apoptosis in cancer cells, often associated with a more or less severe inhibition of proliferation. Moreover, they provide another potential source of molecules adapted to the building of photosensitizer-conjugates allowing a specific targeting to cancer cells, for the photodynamic treatment of tumors. Full article
(This article belongs to the Special Issue Plant Lectins: From Model Species to Crop Plants)
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Open AccessReview Plant Lectins and Lectin Receptor-Like Kinases: How Do They Sense the Outside?
Int. J. Mol. Sci. 2017, 18(6), 1164; doi:10.3390/ijms18061164
Received: 28 April 2017 / Revised: 26 May 2017 / Accepted: 28 May 2017 / Published: 31 May 2017
PDF Full-text (2302 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
Lectins are fundamental to plant life and have important roles in cell-to-cell communication; development and defence strategies. At the cell surface; lectins are present both as soluble proteins (LecPs) and as chimeric proteins: lectins are then the extracellular domains of receptor-like kinases (LecRLKs)
[...] Read more.
Lectins are fundamental to plant life and have important roles in cell-to-cell communication; development and defence strategies. At the cell surface; lectins are present both as soluble proteins (LecPs) and as chimeric proteins: lectins are then the extracellular domains of receptor-like kinases (LecRLKs) and receptor-like proteins (LecRLPs). In this review; we first describe the domain architectures of proteins harbouring G-type; L-type; LysM and malectin carbohydrate-binding domains. We then focus on the functions of LecPs; LecRLKs and LecRLPs referring to the biological processes they are involved in and to the ligands they recognize. Together; LecPs; LecRLKs and LecRLPs constitute versatile recognition systems at the cell surface contributing to the detection of symbionts and pathogens; and/or involved in monitoring of the cell wall structure and cell growth. Full article
(This article belongs to the Special Issue Plant Lectins: From Model Species to Crop Plants)
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