Literature DB >> 19607856

The surface of Bacillus anthracis.

Agnès Fouet1.   

Abstract

Bacillus anthracis is a Gram positive organism possessing a complex parietal structure. An S-layer, a bi-dimensional crystalline layer, and a peptidic capsule surround the thick peptidoglycan of bacilli harvested during infection. A review of the current literature indicates that elements from each of these three structures, as well as membrane components, have been studied. So-called cell-wall secondary polymers, be they attached to the cell-wall or to the membrane play important functions, either per se or because they permit the anchoring of proteins. Some surface proteins, whichever compartment they are attached to, play, as had been hypothesized, key roles in virulence. Others, of yet unknown function, are nevertheless expressed in vivo. This review will focus on well-studied polymers or proteins and indicate, when appropriate, the mechanisms by which they are targeted to their respective locations.

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Year:  2009        PMID: 19607856     DOI: 10.1016/j.mam.2009.07.001

Source DB:  PubMed          Journal:  Mol Aspects Med        ISSN: 0098-2997


  34 in total

1.  Surface-layer (S-layer) proteins sap and EA1 govern the binding of the S-layer-associated protein BslO at the cell septa of Bacillus anthracis.

Authors:  Valerie J Kern; Justin W Kern; Julie A Theriot; Olaf Schneewind; Dominique Missiakas
Journal:  J Bacteriol       Date:  2012-05-18       Impact factor: 3.490

2.  Role of net charge on catalytic domain and influence of cell wall binding domain on bactericidal activity, specificity, and host range of phage lysins.

Authors:  Lieh Yoon Low; Chen Yang; Marta Perego; Andrei Osterman; Robert Liddington
Journal:  J Biol Chem       Date:  2011-08-04       Impact factor: 5.157

3.  Revisiting the Concept of Targeting Only Bacillus anthracis Toxins as a Treatment for Anthrax.

Authors:  Itai Glinert; Elad Bar-David; Assa Sittner; Shay Weiss; Josef Schlomovitz; Amir Ben-Shmuel; Adva Mechaly; Zeev Altboum; David Kobiler; Haim Levy
Journal:  Antimicrob Agents Chemother       Date:  2016-07-22       Impact factor: 5.191

Review 4.  The Bacillus cereus Group: Bacillus Species with Pathogenic Potential.

Authors:  Monika Ehling-Schulz; Didier Lereclus; Theresa M Koehler
Journal:  Microbiol Spectr       Date:  2019-05

5.  Structure of surface layer homology (SLH) domains from Bacillus anthracis surface array protein.

Authors:  Justin Kern; Rosemarie Wilton; Rongguang Zhang; T Andrew Binkowski; Andrzej Joachimiak; Olaf Schneewind
Journal:  J Biol Chem       Date:  2011-05-13       Impact factor: 5.157

Review 6.  Designing inhibitors of anthrax toxin.

Authors:  Ekaterina M Nestorovich; Sergey M Bezrukov
Journal:  Expert Opin Drug Discov       Date:  2014-01-22       Impact factor: 6.098

Review 7.  New developments in vaccines, inhibitors of anthrax toxins, and antibiotic therapeutics for Bacillus anthracis.

Authors:  J M Beierlein; A C Anderson
Journal:  Curr Med Chem       Date:  2011       Impact factor: 4.530

8.  PatB1 is an O-acetyltransferase that decorates secondary cell wall polysaccharides.

Authors:  David Sychantha; Dustin J Little; Robert N Chapman; Geert-Jan Boons; Howard Robinson; P Lynne Howell; Anthony J Clarke
Journal:  Nat Chem Biol       Date:  2017-10-30       Impact factor: 15.040

9.  Comprehensive Laboratory Evaluation of a Highly Specific Lateral Flow Assay for the Presumptive Identification of Bacillus anthracis Spores in Suspicious White Powders and Environmental Samples.

Authors:  Jason G Ramage; Kristin W Prentice; Lindsay DePalma; Kodumudi S Venkateswaran; Sruti Chivukula; Carol Chapman; Melissa Bell; Shomik Datta; Ajay Singh; Alex Hoffmaster; Jawad Sarwar; Nishanth Parameswaran; Mrinmayi Joshi; Nagarajan Thirunavkkarasu; Viswanathan Krishnan; Stephen Morse; Julie R Avila; Shashi Sharma; Peter L Estacio; Larry Stanker; David R Hodge; Segaran P Pillai
Journal:  Health Secur       Date:  2016 Sep-Oct

10.  The secondary cell wall polysaccharide of Bacillus anthracis provides the specific binding ligand for the C-terminal cell wall-binding domain of two phage endolysins, PlyL and PlyG.

Authors:  Jhuma Ganguly; Lieh Y Low; Nazia Kamal; Elke Saile; L Scott Forsberg; Gerardo Gutierrez-Sanchez; Alex R Hoffmaster; Robert Liddington; Conrad P Quinn; Russell W Carlson; Elmar L Kannenberg
Journal:  Glycobiology       Date:  2013-03-14       Impact factor: 4.313

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