Cited by 49Bacillus and Francisella bacterial researchBacterial Genetics and BiotechnologyEscherichia coli research studies

The DOI matches its Crossref record; 60 of the 60 references it cites were found in a registry or an index.

Distinct functions of polysaccharide deacetylases in cell shape, neutral polysaccharide synthesis and virulence of Bacillus anthracis

Abstract

Summary: Peptidoglycan deacetylases (PGNG‐dacs) belong to the C arbohydrate E sterase F amily 4 (CE 4) and have been described as required for bacterial evasion to lysozyme and innate immune responses. Interestingly, there is an unusual occurrence of 10 putative polysaccharide deacetylases, including five PGNG‐dacs, in the B acillus sp. genomes, especially B. cereus and B. anthracis. To elucidate the physiological role of these multiple deacetylases, we employed genetic analysis and protein localization studies of five putative PGNG‐dacs from B. anthracis as well as biochemical analysis of their corresponding homologues from B. cereus. Our data confirm that three enzymes are PGNG‐dacs. While BA 1977, associated with lateral peptidoglycan synthesis, is a bona fide peptidoglycan deacetylase involved in resistance to host lysozyme and required for full virulence, BA 1961 and BA 3679 participate in the biogenesis of the peptidoglycan during both elongation and cell division. Furthermore, two enzymes are important for neutral polysaccharide attachment to PG and consequently anchoring of S‐layer proteins (BA 5436) and for polysaccharide modification (BA 2944). Our results provide novel and fundamental insights into the function of polysaccharide deacetylases in a major bioterrorism agent.

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Crossref · 10.1111/mmi.12137

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Research works printed but not linked: 2

  1. Reed L.J., 1938, A simple method of estimating fifty percent endpoints, Am J Hyg, 27, 493
  2. US Department of Health and Human Services National Institute of Allergy and Infectious Diseases (NIAID)(2006)Biodefense Research Agenda for CDC Category A Agents:Progress Report pp.15–23.

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Metadata

Authors
Balomenou, S., Fouet, A., Tzanodaskalaki, M., Couture‐Tosi, E., Bouriotis, V., & Boneca, I. G.
Affiliations
  • University of Crete (GR)
  • Institut Pasteur Unite Toxines et Pathogénie Bacteriénnes 25‐28 rue de Dr Roux 75724 Paris Cedex 15 France
  • FORTH Institute of Molecular Biology and Biotechnology (GR)
  • Centre National de la Recherche Scientifique (FR)
  • Inserm (FR)
Corresponding author
  • Bouriotis, Vassilis
  • Boneca, Ivo G.
Venue
Molecular Microbiology
Publisher
Wiley
Published
2013-01-21
Volume
87
Issue
4
Pages
867-883
ISSN
  • 0950-382X (ISSN-L)
  • 1365-2958
OpenAlex
W1951059500
Cited by
49
References
60
Citations by year
2025: 2 · 2024: 4 · 2023: 3 · 2022: 1 · 2021: 4 · 2020: 6 · 2019: 4 · 2018: 8 · 2017: 4 · 2015: 5 · 2014: 7 · 2013: 1
FWCI
1.94
Type
journal article
Language
en
Open access
closed
Locations
  • Molecular Microbiology (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bacillus and Francisella bacterial research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
  • Life Sciences › Immunology and Microbiology › Microbiology › Escherichia coli research studies
Keywords
polysaccharide deacetylase, Bacillus anthracis, Bacillus cereus, lysozyme resistance, bacterial virulence, S-layer proteins, cell shape, cell division, bioterrorism agents
MeSH terms
Amidohydrolases, Animals, Anthrax, Bacillus anthracis, Bacterial Proteins, Female, Humans, Male, Mice, Inbred BALB C, Polysaccharides, Bacterial, Virulence, Protein Transport, Mice

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