Lipid lysination by MprF contributes to hemolytic pigment retention in group B Streptococcus.

Autor: Caliot E; Institut Pasteur, Université Paris Cité, CNRS UMR6047, Biology of Gram-positive Pathogens Unit, F-75015 Paris, France., Firon A; Institut Pasteur, Université Paris Cité, CNRS UMR6047, Biology of Gram-positive Pathogens Unit, F-75015 Paris, France., Solgadi A; UMS-IPSIT SAMM Facility, Université Paris-Saclay, Inserm, CNRS, Ingénierie et Plateformes au Service de l'Innovation Thérapeutique, F-91400 Orsay, France., Trieu-Cuot P; Institut Pasteur, Université Paris Cité, CNRS UMR6047, Biology of Gram-positive Pathogens Unit, F-75015 Paris, France. Electronic address: patrick.trieu-cuot@pasteur.fr., Dramsi S; Institut Pasteur, Université Paris Cité, CNRS UMR6047, Biology of Gram-positive Pathogens Unit, F-75015 Paris, France. Electronic address: shaynoor.dramsi@pasteur.fr.
Jazyk: angličtina
Zdroj: Research in microbiology [Res Microbiol] 2024 Nov-Dec; Vol. 175 (8), pp. 104231. Date of Electronic Publication: 2024 Aug 26.
DOI: 10.1016/j.resmic.2024.104231
Abstrakt: Group B Streptococcus (GBS) is the leading cause of neonatal sepsis and meningitis. A major virulence factor is a pigmented beta-haemolytic/cyto-lysin (β-h/c) toxin with an ornithine rhamnolipid structure. We initially observed that absence of MprF enzyme altered pigmentation and haemolytic activity in GBS. Next, we showed that MprF-dependent lipid lysination contributes to the retention of the ornithine rhamnolipid within GBS membrane. Furthermore, cationic lipidation by MprF altered membrane properties contributing to resistance to the cyclic lipopeptide daptomycin and to acidic pH. This study highlights the importance of cationic lipids in cell envelope homeostasis and in modulating β-h/c activity.
Competing Interests: Declaration of competing interest We declare that there is no conflict of interest.
(Copyright © 2024 The Authors. Published by Elsevier Masson SAS.. All rights reserved.)
Databáze: MEDLINE
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