Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 107, Issue 44, Pages 18991-18996Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1004304107
Keywords
cell division; cell wall; penicillin-binding proteins; transpeptidases; lysozyme
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Funding
- Fundacao para a Ciencia e Tecnologia [POCI/SAU-IMI/56501/2004, PTDC/SAU-MII/75696/2006, POCI/BIA-MIC/67845/2006, PTDC/BIA-MIC/099151/2008, SFRH/BD/28440/2006, SFRH/BD/41119/2007, SFRH/BPD/23838/2005, SFRH/BPD/23812/2005, SFRH/BD/38732/2007]
- European Molecular Biology Organization [ALTF 1042-2007]
- Fundação para a Ciência e a Tecnologia [SFRH/BD/41119/2007, SFRH/BD/38732/2007, SFRH/BD/28440/2006, SFRH/BPD/23838/2005, SFRH/BPD/23812/2005, PTDC/BIA-MIC/099151/2008, PTDC/SAU-MII/75696/2006, POCI/SAU-IMI/56501/2004] Funding Source: FCT
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The cell wall of Staphylococcus aureus is characterized by an extremely high degree of cross-linking within its peptidoglycan (PGN). Penicillin-binding protein 4 (PBP4) is required for the synthesis of this highly cross-linked peptidoglycan. We found that wall teichoic acids, glycopolymers attached to the peptidoglycan and important for virulence in Gram-positive bacteria, act as temporal and spatial regulators of PGN metabolism, controlling the level of cross-linking by regulating PBP4 localization. PBP4 normally localizes at the division septum, but in the absence of wall teichoic acids synthesis, it becomes dispersed throughout the entire cell membrane and is unable to function normally. As a consequence, the peptidoglycan of TagO null mutants, impaired in wall teichoic acid biosynthesis, has a decreased degree of cross-linking, which renders it more susceptible to the action of lysozyme, an enzyme produced by different host organisms as an initial defense against bacterial infection.
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