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Volume 155, Issue 6

Identification of novel LPXTG-linked surface proteins from Free

Abstract

Surface adhesion plays an essential part in the survival of the commensal organism in the oral cavity as well as during opportunistic infections such as endocarditis. At least two types of cell surface protein involved in adhesion are found on the surface of Gram-positive bacteria: those anchored via an LPXTG motif by the enzyme sortase A (SrtA) and those associated with the cell surface by, as yet, unknown mechanisms. In mutants, LPXTG-containing proteins have been shown to be released rather than cross-linked to the cell wall. We have therefore used 2D gel electrophoresis of released proteins from an mutant as well as the wild-type strain, followed by peptide identification by MS, to identify a set of novel proteins predicted to be present on the surface of DL1. This includes two large LPXTG-linked proteins (SGO_0707 and SGO_1487), which both contain tandemly repeated sequences similar to those present in known fibrillar adhesins. A 5′-nucleotidase and a protein with a putative collagen-binding domain, both containing LPXTG motifs, were also identified. Anchorless proteins with known chaperone, stress response and elongation factor functions, apparently responsible for bacterial binding to keratinocytes and saliva-coated surfaces in the absence of the LPXTG-linked adhesins, were also associated with the cell surface. These data reveal a range of proteins to be present on the DL1 cell surface, the expression of which plays an important role in adhesion to epithelia and which represent likely candidates for novel virulence factors in .

  • Received:
  • Accepted:
  • Revised:
  • Published Online:
Keyword(s): EF-G, elongation factor G , EF-Tu, elongation factor Tu , IOD, integrated optical density and LC, liquid chromatography
SGM
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2009-06-01
2024-04-23
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Identification of novel LPXTG-linked surface proteins from Streptococcus gordonii
Microbiology 155, 1977 (2009); https://doi.org/10.1099/mic.0.027854-0
/content/journal/micro/10.1099/mic.0.027854-0
/content/journal/micro/10.1099/mic.0.027854-0
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