Molecular Dissection of the secA2 Locus of Group B Streptococcus Reveals that Glycosylation of the Srr1 LPXTG Protein Is Required for Full Virulence
| Autor: | Claire Poyart, Michel-Yves Mistou, Sara Brega, Shaynoor Dramsi, Patrick Trieu-Cuot |
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| Přispěvatelé: | Dramsi, Shaynoor, Programme de recherche transnational Pathogenomics (ERA-NET) - A comparative molecular analysis of GAS and GBS pathogenesis - - Strepvir2006 - ANR-06-PATH-0001 - PATHO - VALID, Biologie des Bactéries Pathogènes à Gram-positif, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Université Paris Descartes - Paris 5 (UPD5), Institut National de la Santé et de la Recherche Médicale (INSERM), Centre National de la Recherche Scientifique (CNRS), This work was supported by the Pasteur Institute (GPH no. 09) and by grants ANR-06-PATHO-001-01 from the Agence Nationale de la Recherche ERA-NET PathoGenoMics and LSHB-CT-2005-512061 from the Network of Excellence Europathogenomics., ANR-06-PATH-0001,Strepvir,A comparative molecular analysis of GAS and GBS pathogenesis(2006), Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2009 |
| Předmět: |
Glycosylation
Transcription Genetic [SDV]Life Sciences [q-bio] MESH: Trypsin MESH: Rats Sprague-Dawley MESH: Virulence medicine.disease_cause Polymerase Chain Reaction Bacterial Adhesion NF-κB MESH: Animals Newborn internalin Rats Sprague-Dawley chemistry.chemical_compound MESH: Streptococcal Infections Cell Wall Sortase Trypsin MESH: Animals MESH: Bacterial Proteins 0303 health sciences Aminoacyltransferases MESH: Glycosylation 3. Good health Cell biology [SDV] Life Sciences [q-bio] Cysteine Endopeptidases MESH: Rats Virulence Biology Microbiology Streptococcus agalactiae 03 medical and health sciences MESH: Cell Wall Bacterial Proteins Streptococcal Infections MESH: Aminoacyltransferases medicine Animals Secretion MESH: Bacterial Adhesion Molecular Biology Gene 030304 developmental biology Molecular Biology of Pathogens 030306 microbiology MESH: Transcription Genetic MESH: Polymerase Chain Reaction MESH: Streptococcus agalactiae anti-inflammation cytokines Rats Sialic acid virulence Animals Newborn chemistry Cytoplasm MESH: Cysteine Endopeptidases |
| Zdroj: | Journal of Bacteriology Journal of Bacteriology, 2009, 191 (13), pp.4195-4206. ⟨10.1128/JB.01673-08⟩ Journal of Bacteriology, American Society for Microbiology, 2009, 191 (13), pp.4195-4206. ⟨10.1128/JB.01673-08⟩ |
| ISSN: | 0021-9193 1098-5530 |
| Popis: | In streptococci, the secA2 locus includes genes encoding the following: (i) the accessory Sec components (SecA2, SecY2, and at least three accessory secretion proteins), (ii) two essential glycosyltranferases (GTs) (GtfA and GtfB), (iii) a variable number of dispensable additional GTs, and (iv) a secreted serine-rich LPXTG protein which is glycosylated in the cytoplasm and transported to the cell surface by this accessory Sec system. The secA2 locus of Streptococcus agalactiae strain NEM316 is structurally related to those found in other streptococci and encodes the serine-rich surface protein Srr1. We demonstrated that expression of Srr1 but not that of the SecA2 components and the associated GTs is regulated by the standalone transcriptional regulator Rga. Srr1 is synthesized as a glycosylated precursor, secreted by the SecA2 system, and anchored to the cell wall by the housekeeping sortase A. Srr1 was localized preferentially at the old poles. GtfA and/or GtfB, but not the six additional GTs, is essential for the production of Srr1. These GTs are involved in the attachment of GlcNac and sialic acid to Srr1. Full glycosylation of Srr1 is associated with the cell surface display of a protein that is more resistant to proteolytic attack. Srr1 contributes to bacterial adherence to human epithelial cell lines and virulence in a neonatal rat model. The extent of Srr1 glycosylation by GtfC to -H modulates bacterial adherence and virulence. |
| Databáze: | OpenAIRE |
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