Competence remodels the pneumococcal cell wall exposing key surface virulence factors that mediate increased host adherence.
Journal
PLoS biology
ISSN: 1545-7885
Titre abrégé: PLoS Biol
Pays: United States
ID NLM: 101183755
Informations de publication
Date de publication:
01 2023
01 2023
Historique:
received:
17
08
2022
accepted:
04
01
2023
revised:
09
02
2023
pubmed:
31
1
2023
medline:
14
2
2023
entrez:
30
1
2023
Statut:
epublish
Résumé
Competence development in the human pathogen Streptococcus pneumoniae controls several features such as genetic transformation, biofilm formation, and virulence. Competent bacteria produce so-called "fratricins" such as CbpD that kill noncompetent siblings by cleaving peptidoglycan (PGN). CbpD is a choline-binding protein (CBP) that binds to phosphorylcholine residues found on wall and lipoteichoic acids (WTA and LTA) that together with PGN are major constituents of the pneumococcal cell wall. Competent pneumococci are protected against fratricide by producing the immunity protein ComM. How competence and fratricide contribute to virulence is unknown. Here, using a genome-wide CRISPRi-seq screen, we show that genes involved in teichoic acid (TA) biosynthesis are essential during competence. We demonstrate that LytR is the major enzyme mediating the final step in WTA formation, and that, together with ComM, is essential for immunity against CbpD. Importantly, we show that key virulence factors PspA and PspC become more surface-exposed at midcell during competence, in a CbpD-dependent manner. Together, our work supports a model in which activation of competence is crucial for host adherence by increased surface exposure of its various CBPs.
Identifiants
pubmed: 36716340
doi: 10.1371/journal.pbio.3001990
pii: PBIOLOGY-D-22-01793
pmc: PMC9910801
doi:
Substances chimiques
Virulence Factors
0
N-Acetylmuramoyl-L-alanine Amidase
EC 3.5.1.28
Choline
N91BDP6H0X
Bacterial Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e3001990Informations de copyright
Copyright: © 2023 Minhas et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Déclaration de conflit d'intérêts
The authors have declared that no competing interests exist.
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