Special Issue "Bacterial Adhesion"

Quicklinks

A special issue of Biology (ISSN 2079-7737).

Deadline for manuscript submissions: closed (31 March 2013)

Special Issue Editor

Guest Editor
Prof. Dr. Jukka Finne

Department of Biosciences, Division of Biochemistry and Biotechnology, University of Helsinki, P. O. Box 56 (Viikinkaari 9), Helsinki, FI 00014, Finland
Website | E-Mail
Phone: +358 9 191 59040
Interests: glycobiology; glycoproteins, polysialic acid; bacterial adhesion

Special Issue Information

Dear Collegues,

How bacteria attach themselves to surfaces, extracellular components or other cells plays a crucial role in many natural systems. Bacterial adherence has practical importance in applications in fields as varied as medicine or environmental engineering. Bacteria may bind to many types of living organisms including plants and animals, or even other bacteria. The bacteria may use special appendices, fimbriae or pili, for binding and often display specialized proteins, adhesins, to bind to their molecular targets, which are usually carbohydrates or proteins. Multivalent binding to the binding targets may often be used to overcome the dispersive forces of the environment that prevent adhesion. Biofilm formation is also an efficient strategy for bacterial persistence in diverse niches. Specific signaling may be involved in the process of bacterial adhesion.

The molecular background of bacterial adherence to their targets has been intensively studied, and some mechanisms have been elucidated in detail. Knowledge of the molecular mechanisms is of central importance for practical application such as the development of binding receptor analogues that could be used as novel antibacterial agents. This special issue will cover original research papers and reviews on the broad topic of bacterial adhesion.

Prof. Dr. Jukka Finne
Guest Editor

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. Biology is an international peer-reviewed Open Access quarterly 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 600 CHF (Swiss Francs). English correction and/or formatting fees of 250 CHF (Swiss Francs) will be charged in certain cases for those articles accepted for publication that require extensive additional formatting and/or English corrections.


Keywords

  • adhesins
  • adhesion inhibition
  • antibacterial agents
  • bacterial adherence
  • fimbriae
  • glycoconjugates
  • multivalency
  • pili

Published Papers (10 papers)

View options order results:
result details:
Displaying articles 1-10
Export citation of selected articles as:

Research

Jump to: Review

Open AccessArticle Effect of Aminophenyl and Aminothiahexyl α-D-Glycosides of the Manno-, Gluco-, and Galacto-Series on Type 1 Fimbriae-Mediated Adhesion of Escherichia coli
Biology 2013, 2(3), 1135-1149; doi:10.3390/biology2031135
Received: 15 July 2013 / Revised: 17 August 2013 / Accepted: 28 August 2013 / Published: 3 September 2013
Cited by 4 | PDF Full-text (630 KB) | HTML Full-text | XML Full-text
Abstract
Adhesion of bacteria to the glycosylated surface of their target cells is typically mediated by fimbrial lectins, exposed on the bacterial surface. Among the best-investigated and most important fimbriae are type 1 fimbriae, for which α-d-mannopyranoside-specificity has been described. This carbohydrate specificity is
[...] Read more.
Adhesion of bacteria to the glycosylated surface of their target cells is typically mediated by fimbrial lectins, exposed on the bacterial surface. Among the best-investigated and most important fimbriae are type 1 fimbriae, for which α-d-mannopyranoside-specificity has been described. This carbohydrate specificity is mediated by the type 1 fimbrial lectin FimH. In this account, we have employed four different set-ups to assay type 1 fimbriae-mediated bacterial adhesion, including tailor-made glycoarrays. The focus of our study was on testing FimH specificity with regard to the glycone part of a glycosidic ligand by testing a series of synthetic α-mannosides, as well as α-glucosides and α-galactosides. Unexpectedly, it was found that in solution all tested aminothiahexyl glycosides inhibit bacterial adhesion but that this effect is unspecific. Instead it is due to cytotoxicity of the respective glycosides at high mm concentrations. Full article
(This article belongs to the Special Issue Bacterial Adhesion)
Figures

Open AccessArticle Structural Sampling of Glycan Interaction Profiles Reveals Mucosal Receptors for Fimbrial Adhesins of Enterotoxigenic Escherichia coli
Biology 2013, 2(3), 894-917; doi:10.3390/biology2030894
Received: 1 April 2013 / Revised: 15 May 2013 / Accepted: 17 May 2013 / Published: 1 July 2013
Cited by 7 | PDF Full-text (1464 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
Fimbriae are long, proteinaceous adhesion organelles expressed on the bacterial envelope, evolutionarily adapted by Escherichia coli strains for the colonization of epithelial linings. Using glycan arrays of the Consortium for Functional Glycomics (CFG), the lectin domains were screened of the fimbrial adhesins F17G
[...] Read more.
Fimbriae are long, proteinaceous adhesion organelles expressed on the bacterial envelope, evolutionarily adapted by Escherichia coli strains for the colonization of epithelial linings. Using glycan arrays of the Consortium for Functional Glycomics (CFG), the lectin domains were screened of the fimbrial adhesins F17G and FedF from enterotoxigenic E. coli (ETEC) and of the FimH adhesin from uropathogenic E. coli. This has led to the discovery of a more specific receptor for F17G, GlcNAcb1,3Gal. No significant differences emerged from the glycan binding profiles of the F17G lectin domains from five different E. coli strains. However, strain-dependent amino acid variations, predominantly towards the positively charged arginine, were indicated by sulfate binding in FedF and F17G crystal structures. For FedF, no significant binders could be observed on the CFG glycan array. Hence, a shotgun array was generated from microvilli scrapings of the distal jejunum of a 3-week old piglet about to be weaned. On this array, the blood group A type 1 hexasaccharide emerged as a receptor for the FedF lectin domain and remarkably also for F18-fimbriated E. coli. F17G was found to selectively recognize glycan species with a terminal GlcNAc, typifying intestinal mucins. In conclusion, F17G and FedF recognize long glycan sequences that could only be identified using the shotgun approach. Interestingly, ETEC strains display a large capacity to adapt their fimbrial adhesins to ecological niches via charge-driven interactions, congruent with binding to thick mucosal surfaces displaying an acidic gradient along the intestinal tract. Full article
(This article belongs to the Special Issue Bacterial Adhesion)
Figures

Open AccessArticle Use of Tetravalent Galabiose for Inhibition of Streptococcus Suis Serotype 2 Infection in a Mouse Model
Biology 2013, 2(2), 702-718; doi:10.3390/biology2020702
Received: 14 March 2013 / Revised: 26 March 2013 / Accepted: 28 March 2013 / Published: 8 April 2013
Cited by 3 | PDF Full-text (851 KB) | HTML Full-text | XML Full-text
Abstract
Streptococcus suis is an important swine pathogen associated with a variety of infections such as meningitis, arthritis and septicemia. The bacterium is zoonotic and has been found to cause meningitis especially in humans occupationally exposed to infected pigs. Since adhesion is a prerequisite
[...] Read more.
Streptococcus suis is an important swine pathogen associated with a variety of infections such as meningitis, arthritis and septicemia. The bacterium is zoonotic and has been found to cause meningitis especially in humans occupationally exposed to infected pigs. Since adhesion is a prerequisite for colonization and subsequent infection, anti-adhesion treatment seems a natural alternative to traditional treatment with antibiotics. In order to optimize the inhibitory potency a multivalency approach was taken in the inhibitor design. A synthetic tetravalent galabiose compound was chosen which had previously shown promising anti-adhesion effects with S. suis in vitro. The aim of this study was to evaluate the in vivo effects of the compound using an infection peritonitis mouse model. As such S. suis serotype 2 infection and treatment were tested in vivo and the effects were compared to the effect of treatment with penicillin. Full article
(This article belongs to the Special Issue Bacterial Adhesion)
Figures

Review

Jump to: Research

Open AccessReview Dancing to Another Tune—Adhesive Moonlighting Proteins in Bacteria
Biology 2014, 3(1), 178-204; doi:10.3390/biology3010178
Received: 8 January 2014 / Revised: 26 February 2014 / Accepted: 27 February 2014 / Published: 10 March 2014
Cited by 13 | PDF Full-text (1137 KB) | HTML Full-text | XML Full-text
Abstract
Biological moonlighting refers to proteins which express more than one function. Moonlighting proteins occur in pathogenic and commensal as well as in Gram-positive and Gram-negative bacteria. The canonical functions of moonlighting proteins are in essential cellular processes, i.e., glycolysis, protein synthesis, chaperone
[...] Read more.
Biological moonlighting refers to proteins which express more than one function. Moonlighting proteins occur in pathogenic and commensal as well as in Gram-positive and Gram-negative bacteria. The canonical functions of moonlighting proteins are in essential cellular processes, i.e., glycolysis, protein synthesis, chaperone activity, and nucleic acid stability, and their moonlighting functions include binding to host epithelial and phagocytic cells, subepithelia, cytoskeleton as well as to mucins and circulating proteins of the immune and hemostatic systems. Sequences of the moonlighting proteins do not contain known motifs for surface export or anchoring, and it has remained open whether bacterial moonlighting proteins are actively secreted to the cell wall or whether they are released from traumatized cells and then rebind onto the bacteria. In lactobacilli, ionic interactions with lipoteichoic acids and with cell division sites are important for surface localization of the proteins. Moonlighting proteins represent an abundant class of bacterial adhesins that are part of bacterial interactions with the environment and in responses to environmental changes. Multifunctionality in bacterial surface proteins appears common: the canonical adhesion proteins fimbriae express also nonadhesive functions, whereas the mobility organelles flagella as well as surface proteases express adhesive functions. Full article
(This article belongs to the Special Issue Bacterial Adhesion)
Open AccessReview The Role of the Bacterial Flagellum in Adhesion and Virulence
Biology 2013, 2(4), 1242-1267; doi:10.3390/biology2041242
Received: 30 July 2013 / Revised: 27 September 2013 / Accepted: 30 September 2013 / Published: 25 October 2013
Cited by 20 | PDF Full-text (425 KB) | HTML Full-text | XML Full-text
Abstract
The bacterial flagellum is a complex apparatus assembled of more than 20 different proteins. The flagellar basal body traverses the cell wall, whereas the curved hook connects the basal body to the whip-like flagellar filament that protrudes several µm from the bacterial cell.
[...] Read more.
The bacterial flagellum is a complex apparatus assembled of more than 20 different proteins. The flagellar basal body traverses the cell wall, whereas the curved hook connects the basal body to the whip-like flagellar filament that protrudes several µm from the bacterial cell. The flagellum has traditionally been regarded only as a motility organelle, but more recently it has become evident that flagella have a number of other biological functions. The major subunit, flagellin or FliC, of the flagellum plays a well-documented role in innate immunity and as a dominant antigen of the adaptive immune response. Importantly, flagella have also been reported to function as adhesins. Whole flagella have been indicated as significant in bacterial adhesion to and invasion into host cells. In various pathogens, e.g., Escherichia coli, Pseudomonas aeruginosa and Clostridium difficile, flagellin and/or the distally located flagellar cap protein have been reported to function as adhesins. Recently, FliC of Shiga-toxigenic E. coli was shown to be involved in cellular invasion via lipid rafts. Here, we examine the latest or most important findings regarding flagellar adhesive and invasive properties, especially focusing on the flagellum as a potential virulence factor. Full article
(This article belongs to the Special Issue Bacterial Adhesion)
Open AccessReview The Role of Helicobacter pylori Outer Membrane Proteins in Adherence and Pathogenesis
Biology 2013, 2(3), 1110-1134; doi:10.3390/biology2031110
Received: 4 June 2013 / Revised: 26 July 2013 / Accepted: 13 August 2013 / Published: 27 August 2013
Cited by 10 | PDF Full-text (787 KB) | HTML Full-text | XML Full-text
Abstract
Helicobacter pylori is one of the most successful human pathogens, which colonizes the mucus layer of the gastric epithelium of more than 50% of the world’s population. This curved, microaerophilic, Gram-negative bacterium induces a chronic active gastritis, often asymptomatic, in all infected individuals.
[...] Read more.
Helicobacter pylori is one of the most successful human pathogens, which colonizes the mucus layer of the gastric epithelium of more than 50% of the world’s population. This curved, microaerophilic, Gram-negative bacterium induces a chronic active gastritis, often asymptomatic, in all infected individuals. In some cases, this gastritis evolves to more severe diseases such as peptic ulcer disease, gastric adenocarcinoma, and gastric mucosa-associated lymphoid tissue lymphoma. H. pylori has developed a unique set of factors, actively supporting its successful survival and persistence in its natural hostile ecological niche, the human stomach, throughout the individual’s life, unless treated. In the human stomach, the vast majority of H. pylori cells are motile in the mucus layer lining, but a small percentage adheres to the epithelial cell surfaces. Adherence to the gastric epithelium is important for the ability of H. pylori to cause disease because this intimate attachment facilitates: (1) colonization and persistence, by preventing the bacteria from being eliminated from the stomach, by mucus turnover and gastric peristalsis; (2) evasion from the human immune system and (3) efficient delivery of proteins into the gastric cell, such as the CagA oncoprotein. Therefore, bacteria with better adherence properties colonize the host at higher densities. H. pylori is one of the most genetically diverse bacterial species known and is equipped with an extraordinarily large set of outer membrane proteins, whose role in the infection and persistence process will be discussed in this review, as well as the different receptor structures that have been so far described for mucosal adherence. Full article
(This article belongs to the Special Issue Bacterial Adhesion)
Open AccessReview The Biology of Neisseria Adhesins
Biology 2013, 2(3), 1054-1109; doi:10.3390/biology2031054
Received: 2 May 2013 / Revised: 1 July 2013 / Accepted: 3 July 2013 / Published: 29 July 2013
Cited by 3 | PDF Full-text (1122 KB) | HTML Full-text | XML Full-text
Abstract
Members of the genus Neisseria include pathogens causing important human diseases such as meningitis, septicaemia, gonorrhoea and pelvic inflammatory disease syndrome. Neisseriae are found on the exposed epithelia of the upper respiratory tract and the urogenital tract. Colonisation of these exposed epithelia is
[...] Read more.
Members of the genus Neisseria include pathogens causing important human diseases such as meningitis, septicaemia, gonorrhoea and pelvic inflammatory disease syndrome. Neisseriae are found on the exposed epithelia of the upper respiratory tract and the urogenital tract. Colonisation of these exposed epithelia is dependent on a repertoire of diverse bacterial molecules, extending not only from the surface of the bacteria but also found within the outer membrane. During invasive disease, pathogenic Neisseriae also interact with immune effector cells, vascular endothelia and the meninges. Neisseria adhesion involves the interplay of these multiple surface factors and in this review we discuss the structure and function of these important molecules and the nature of the host cell receptors and mechanisms involved in their recognition. We also describe the current status for recently identified Neisseria adhesins. Understanding the biology of Neisseria adhesins has an impact not only on the development of new vaccines but also in revealing fundamental knowledge about human biology. Full article
(This article belongs to the Special Issue Bacterial Adhesion)
Open AccessReview Bacterial Adhesion of Streptococcus suis to Host Cells and Its Inhibition by Carbohydrate Ligands
Biology 2013, 2(3), 918-935; doi:10.3390/biology2030918
Received: 2 May 2013 / Revised: 22 May 2013 / Accepted: 22 May 2013 / Published: 1 July 2013
Cited by 5 | PDF Full-text (259 KB) | HTML Full-text | XML Full-text
Abstract
Streptococcus suis is a Gram-positive bacterium, which causes sepsis and meningitis in pigs and humans. This review examines the role of known S. suis virulence factors in adhesion and S. suis carbohydrate-based adhesion mechanisms, as well as the inhibition of S. suis adhesion
[...] Read more.
Streptococcus suis is a Gram-positive bacterium, which causes sepsis and meningitis in pigs and humans. This review examines the role of known S. suis virulence factors in adhesion and S. suis carbohydrate-based adhesion mechanisms, as well as the inhibition of S. suis adhesion by anti-adhesion compounds in in vitro assays. Carbohydrate-binding specificities of S. suis have been identified, and these studies have shown that many strains recognize Galα1-4Gal-containing oligosaccharides present in host glycolipids. In the era of increasing antibiotic resistance, new means to treat infections are needed. Since microbial adhesion to carbohydrates is important to establish disease, compounds blocking adhesion could be an alternative to antibiotics. The use of oligosaccharides as drugs is generally hampered by their relatively low affinity (micromolar) to compete with multivalent binding to host receptors. However, screening of a library of chemically modified Galα1-4Gal derivatives has identified compounds that inhibit S. suis adhesion in nanomolar range. Also, design of multivalent Galα1-4Gal-containing dendrimers has resulted in a significant increase of the inhibitory potency of the disaccharide. The S. suis adhesin binding to Galα1-4Gal-oligosaccharides, Streptococcal adhesin P (SadP), was recently identified. It has a Galα1-4Gal-binding N-terminal domain and a C-terminal LPNTG-motif for cell wall anchoring. The carbohydrate-binding domain has no homology to E. coli P fimbrial adhesin, which suggests that these Gram-positive and Gram-negative bacterial adhesins recognizing the same receptor have evolved by convergent evolution. SadP adhesin may represent a promising target for the design of anti-adhesion ligands for the prevention and treatment of S. suis infections. Full article
(This article belongs to the Special Issue Bacterial Adhesion)
Figures

Open AccessReview Ordered and Ushered; the Assembly and Translocation of the Adhesive Type I and P Pili
Biology 2013, 2(3), 841-860; doi:10.3390/biology2030841
Received: 12 April 2013 / Revised: 21 May 2013 / Accepted: 24 May 2013 / Published: 26 June 2013
Cited by 5 | PDF Full-text (712 KB) | HTML Full-text | XML Full-text
Abstract
Type I and P pili are chaperone-usher pili of uropathogenic Escherichia coli, which allow bacteria to adhere to host cell receptors. Pilus formation and secretion are orchestrated by two accessory proteins, a chaperone, which catalyses pilus subunit folding and maintains them in
[...] Read more.
Type I and P pili are chaperone-usher pili of uropathogenic Escherichia coli, which allow bacteria to adhere to host cell receptors. Pilus formation and secretion are orchestrated by two accessory proteins, a chaperone, which catalyses pilus subunit folding and maintains them in a polymerization-competent state, and an outer membrane-spanning nanomachine, the usher, which choreographs their assembly into a pilus and drives their secretion through the membrane. In this review, recent structures and kinetic studies are combined to examine the mechanism of type I and P pili assembly, as it is currently known. We also investigate how the knowledge of pilus biogenesis mechanisms has been exploited to design selective inhibitors of the process. Full article
(This article belongs to the Special Issue Bacterial Adhesion)
Open AccessReview Adhesion of Diarrheagenic Escherichia coli and Inhibition by Glycocompounds Engaged in the Mucosal Innate Immunity
Biology 2013, 2(2), 810-831; doi:10.3390/biology2020810
Received: 26 March 2013 / Revised: 18 May 2013 / Accepted: 22 May 2013 / Published: 7 June 2013
Cited by 3 | PDF Full-text (266 KB) | HTML Full-text | XML Full-text
Abstract
Escherichia coli colonizes the human intestine shortly after birth, with most strains engaging in a commensal relationship. However, some E. coli strains have evolved toward acquiring genetic traits associated with virulence. Currently, five categories of enteroadherent E. coli strains are well-recognized, and are
[...] Read more.
Escherichia coli colonizes the human intestine shortly after birth, with most strains engaging in a commensal relationship. However, some E. coli strains have evolved toward acquiring genetic traits associated with virulence. Currently, five categories of enteroadherent E. coli strains are well-recognized, and are classified in regard to expressed adhesins and the strategy used during the colonization. The high morbidity associated with diarrhea has motivated investigations focusing on E. coli adhesins, as well on factors that inhibit bacterial adherence. Breastfeeding has proved to be the most effective strategy for preventing diarrhea in children. Aside from the immunoglobulin content, glycocompounds and oligosaccharides in breast milk play a critical role in the innate immunity against diarrheagenic E. coli strains. This review summarizes the colonization factors and virulence strategies exploited by diarrheagenic E. coli strains, addressing the inhibitory effects that oligosaccharides and glycocompounds, such as lactoferrin and free secretory components, exert on the adherence and virulence of these strains. This review thus provides an overview of experimental data indicating that human milk glycocompounds are responsible for the universal protective effect of breastfeeding against diarrheagenic E. coli pathotypes. Full article
(This article belongs to the Special Issue Bacterial Adhesion)

Journal Contact

MDPI AG
Biology Editorial Office
St. Alban-Anlage 66, 4052 Basel, Switzerland
biology@mdpi.com
Tel. +41 61 683 77 34
Fax: +41 61 302 89 18
Editorial Board
Contact Details Submit to Biology
Back to Top