Teichoic acids are temporal and spatial regulators of peptidoglycan cross-linking in <i>Staphylococcus aureus</i>
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- Magda L. Atilano
- Laboratory of Bacterial Cell Surfaces and Pathogenesis and
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- Pedro M. Pereira
- Laboratory of Bacterial Cell Biology, Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, 2781-901 Oeiras, Portugal
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- James Yates
- Laboratory of Bacterial Cell Surfaces and Pathogenesis and
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- Patricia Reed
- Laboratory of Bacterial Cell Biology, Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, 2781-901 Oeiras, Portugal
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- Helena Veiga
- Laboratory of Bacterial Cell Biology, Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, 2781-901 Oeiras, Portugal
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- Mariana G. Pinho
- Laboratory of Bacterial Cell Biology, Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, 2781-901 Oeiras, Portugal
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- Sérgio R. Filipe
- Laboratory of Bacterial Cell Surfaces and Pathogenesis and
説明
<jats:p> The cell wall of <jats:italic>Staphylococcus aureus</jats:italic> 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. </jats:p>
収録刊行物
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- Proceedings of the National Academy of Sciences
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Proceedings of the National Academy of Sciences 107 (44), 18991-18996, 2010-10-13
Proceedings of the National Academy of Sciences