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- W2153399124 endingPage "2765" @default.
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- W2153399124 abstract "ABSTRACT Inactivation of sortase gene srtA in Streptococcus pneumoniae strain R6 caused the release of β-galactosidase and neuraminidase A (NanA) from the cell wall into the surrounding medium. Both of these surface proteins contain the LPXTG motif in the C-terminal domain. Complementation with plasmid-borne srtA reversed protein release. Deletion of murM , a gene involved in the branching of pneumococcal peptidoglycan, also caused partial release of β-galactosidase, suggesting preferential attachment of the protein to branched muropeptides in the cell wall. Inactivation of srtA caused decreased adherence to human pharyngeal cells in vitro but had no effect on the virulence of a capsular type III strain of S. pneumoniae in the mouse intraperitoneal model. The observations suggest that—as in other gram-positive bacteria—sortase-dependent display of proteins occurs in S. pneumoniae and that some of these proteins may be involved in colonization of the human host." @default.
- W2153399124 created "2016-06-24" @default.
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- W2153399124 date "2003-05-01" @default.
- W2153399124 modified "2023-09-27" @default.
- W2153399124 title "Inactivation of the<i>srtA</i>Gene Affects Localization of Surface Proteins and Decreases Adhesion of<i>Streptococcus pneumoniae</i>to Human Pharyngeal Cells In Vitro" @default.
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- W2153399124 doi "https://doi.org/10.1128/iai.71.5.2758-2765.2003" @default.
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