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Antibiotics
Special Issues
The Role of the Cell Wall in Host-Microbe Interactions
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The Role of the Cell Wall in Host-Microbe Interactions

A special issue of Antibiotics (ISSN 2079-6382).

Deadline for manuscript submissions: closed (20 July 2021) | Viewed by 11215

Special Issue Editor

Prof. Dr. Ivo Gomperts-Boneca

E-Mail Website
Guest Editor
Department of Microbiology, Institut Pasteur, Paris, France
Interests: peptidoglycan; cell envelope; beta-lactam; penicillin-binding protein; resistance; peptidoglycan binding protein; lysozyme; PG hydrolase; innate immunity; Nod-like receptors; Toll-like receptors

Special Issue Information

Dear Colleagues,

In the last three decades, due to the discovery of innate immune receptors, it has become apparent that microbes and hosts communicate constantly both during healthy symbiotic interactions as well as during pathogenesis. The cell wall of bacteria is directly exposed to the external environment and accessible to the host for interactions and detection. Hence, the bacterial cell wall has been at the center of the field since its emergence. The aim of this Special Issue is to publish the latest developments regarding the bacterial cell wall and its role in host‐microbe interactions during homeostasis, dysbiosis and pathogenesis. Contributions can be in the form of reviews of the literature as well as original work and may include, but are not limited to, cell wall biochemistry and physiology, surface structures involved in interactions, modifications of the cell wall to adapt to the host and to anti-biotherapy, and mechanisms of warfare among bacteria and with the host, etc.

Prof. Dr. Ivo Gomperts-Boneca
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 submissions that pass pre-check are 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. Antibiotics 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 2900 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

  • Cell wall
  • antibiotic
  • antimicrobial peptide
  • lysozyme
  • innate immune receptor
  • TLR
  • NLR
  • lipopolysaccharide
  • lipoprotein
  • peptidoglycan
  • capsule
  • polysaccharide
  • adhesin
  • pilus
  • secretion system
  • motility
  • flagellum

Published Papers (2 papers)

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Research

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17 pages, 2687 KiB  
Article
PBP4 Is Likely Involved in Cell Division of the Longitudinally Dividing Bacterium Candidatus Thiosymbion Oneisti
by Jinglan Wang, Laura Alvarez, Silvia Bulgheresi, Felipe Cava and Tanneke den Blaauwen
Antibiotics 2021, 10(3), 274; https://doi.org/10.3390/antibiotics10030274 - 9 Mar 2021
Cited by 2 | Viewed by 2474
Abstract
Peptidoglycan (PG) is essential for bacterial survival and maintaining cell shape. The rod-shaped model bacterium Escherichia coli has a set of seven endopeptidases that remodel the PG during cell growth. The gamma proteobacterium Candidatus Thiosymbion oneisti is also rod-shaped and attaches to the [...] Read more.
Peptidoglycan (PG) is essential for bacterial survival and maintaining cell shape. The rod-shaped model bacterium Escherichia coli has a set of seven endopeptidases that remodel the PG during cell growth. The gamma proteobacterium Candidatus Thiosymbion oneisti is also rod-shaped and attaches to the cuticle of its nematode host by one pole. It widens and divides by longitudinal fission using the canonical proteins MreB and FtsZ. The PG layer of Ca. T. oneisti has an unusually high peptide cross-linkage of 67% but relatively short glycan chains with an average length of 12 disaccharides. Curiously, it has only two predicted endopeptidases, MepA and PBP4. Cellular localization of symbiont PBP4 by fluorescently labeled antibodies reveals its polar localization and its accumulation at the constriction sites, suggesting that PBP4 is involved in PG biosynthesis during septum formation. Isolated symbiont PBP4 protein shows a different selectivity for β-lactams compared to its homologue from E. coli. Bocillin-FL binding by PBP4 is activated by some β-lactams, suggesting the presence of an allosteric binding site. Overall, our data point to a role of PBP4 in PG cleavage during the longitudinal cell division and to a PG that might have been adapted to the symbiotic lifestyle. Full article
(This article belongs to the Special Issue The Role of the Cell Wall in Host-Microbe Interactions)
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Review

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15 pages, 1658 KiB  
Review
Peptidoglycan O-Acetylation as a Virulence Factor: Its Effect on Lysozyme in the Innate Immune System
by Ashley S. Brott and Anthony J. Clarke
Antibiotics 2019, 8(3), 94; https://doi.org/10.3390/antibiotics8030094 - 18 Jul 2019
Cited by 38 | Viewed by 8036
Abstract
The peptidoglycan sacculus of both Gram-positive and Gram-negative bacteria acts as a protective mesh and provides structural support around the entirety of the cell. The integrity of this structure is of utmost importance for cell viability and so naturally is the first target [...] Read more.
The peptidoglycan sacculus of both Gram-positive and Gram-negative bacteria acts as a protective mesh and provides structural support around the entirety of the cell. The integrity of this structure is of utmost importance for cell viability and so naturally is the first target for attack by the host immune system during bacterial infection. Lysozyme, a muramidase and the first line of defense of the innate immune system, targets the peptidoglycan sacculus hydrolyzing the β-(1→4) linkage between repeating glycan units, causing lysis and the death of the invading bacterium. The O-acetylation of N-acetylmuramoyl residues within peptidoglycan precludes the productive binding of lysozyme, and in doing so renders it inactive. This modification has been shown to be an important virulence factor in pathogens such as Staphylococcus aureus and Neisseria gonorrhoeae and is currently being investigated as a novel target for anti-virulence therapies. This article reviews interactions made between peptidoglycan and the host immune system, specifically with respect to lysozyme, and how the O-acetylation of the peptidoglycan interrupts these interactions, leading to increased pathogenicity. Full article
(This article belongs to the Special Issue The Role of the Cell Wall in Host-Microbe Interactions)
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