ArticleJournal of bacteriology2015
LytR-CpsA-Psr enzymes as determinants of Bacillus anthracis secondary cell wall polysaccharide assembly.
Article in Journal of bacteriology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Modifications of cell wall polymers in Gram-positive bacteria by multi-component transmembrane glycosylation systems.Current opinion in microbiology · 2021Review
- LytR-CpsA-Psr Glycopolymer Transferases: Essential Bricks in Gram-Positive Bacterial Cell Wall Assembly.International journal of molecular sciences · 2021Review
- TheMicroorganisms · 2020Review
- Distinct Pathways Carry Out α and β Galactosylation of Secondary Cell Wall Polysaccharide in Bacillus anthracis.Journal of bacteriology · 2020Article
- Impairment of the Cell Wall Ligase, LytR-CpsA-Psr Protein (LcpC), in Methicillin ResistantFrontiers in microbiology · 2020Article
- Article
- Extraction and Purification of Wall-Bound Polymers of Gram-Positive Bacteria.Methods in molecular biology (Clifton, N.J.) · 2019Article
- Streptococcal Lancefield polysaccharides are critical cell wall determinants for human Group IIA secreted phospholipase A2 to exert its bactericidal effects.PLoS pathogens · 2018Article
- In vivo virulence of Mycobacterium tuberculosis depends on a single homologue of the LytR-CpsA-Psr proteins.Scientific reports · 2018Article
- Galactosylation of the Secondary Cell Wall Polysaccharide of Bacillus anthracis and Its Contribution to Anthrax Pathogenesis.Journal of bacteriology · 2018Article
- Pneumococcal LytR Protein Is Required for the Surface Attachment of Both Capsular Polysaccharide and Teichoic Acids: Essential for Pneumococcal Virulence.Frontiers in microbiology · 2018Article
- Functional Characterization of Enzymatic Steps Involved in Pyruvylation of Bacterial Secondary Cell Wall Polymer Fragments.Frontiers in microbiology · 2018Article
- Article
- Assembly and Function of the Bacillus anthracis S-Layer.Annual review of microbiology · 2017Review
- Deficiency of RgpG Causes Major Defects in Cell Division and Biofilm Formation, and Deficiency of LytR-CpsA-Psr Family Proteins Leads to Accumulation of Cell Wall Antigens in Culture Medium by Streptococcus mutans.Applied and environmental microbiology · 2017Article
- In vitro reconstitution demonstrates the cell wall ligase activity of LCP proteins.Nature chemical biology · 2017Article
- Genes Required for Bacillus anthracis Secondary Cell Wall Polysaccharide Synthesis.Journal of bacteriology · 2017Article
- Enterococcus hirae LcpA (Psr), a new peptidoglycan-binding protein localized at the division site.BMC microbiology · 2016Article
- A Clostridium difficile Cell Wall Glycopolymer Locus Influences Bacterial Shape, Polysaccharide Production and Virulence.PLoS pathogens · 2016Article
- Assembling of the Mycobacterium tuberculosis Cell Wall Core.The Journal of biological chemistry · 2016Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Bacillus anthracis, the causative agent of anthrax, replicates as chains of vegetative cells by regulating the separation of septal peptidoglycan. Surface (S)-layer proteins and associated proteins (BSLs) function as chain length determinants and bind to the secondary cell wall polysaccharide (SCWP). In this study, we identified the B. anthracis lcpD mutant, which displays increased chain length and S-layer assembly defects due to diminished SCWP attachment to peptidoglycan. In contrast, the B. anthracis lcpB3 variant displayed reduced cell size and chain length, which could be attributed to increased deposition of BSLs. In other bacteria, LytR-CpsA-Psr (LCP) proteins attach wall teichoic acid (WTA) and polysaccharide capsule to peptidoglycan. B. anthracis does not synthesize these polymers, yet its genome encodes six LCP homologues, which, when expressed in S. aureus, promote WTA attachment. We propose a model whereby B. anthracis LCPs promote attachment of SCWP precursors to discrete locations in the peptidoglycan, enabling BSL assembly and regulated separation of septal peptidoglycan.
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