Influence of proteins Bsp and FemH on cell shape and peptidoglycan composition in group B streptococcus c cThe GenBank accession number for the sequence reported in this paper is AJ305309

Autor:	Ralph W. Jack, Kerstin Ehlert, Claudia Stößer, Gursharan S. Chhatwal, Kerstin Möller, Dieter J. Reinscheid, Bernhard J. Eikmanns
Rok vydání:	2002
Předmět:	biology Streptococcus medicine.disease_cause Cell morphology Streptococcaceae biology.organism_classification Microbiology Molecular biology Group B chemistry.chemical_compound fluids and secretions stomatognathic system Streptococcus agalactiae chemistry medicine Peptidoglycan Gene Bacteria
Zdroj:	Microbiology. 148:3245-3254
ISSN:	1465-2080 1350-0872
DOI:	10.1099/00221287-148-10-3245
Popis:	Group B streptococcus (GBS) is surrounded by a capsule. However, little is known about peptidoglycan metabolism in these bacteria. In the present study, a 65 kDa protein was isolated from the culture supernatant of GBS and N-terminally sequenced, permitting isolation of the corresponding gene, termed bsp. The bsp gene was located close to another gene, designated femH, and reverse transcription-PCR revealed a bicistronic transcriptional organization for both genes. The Bsp protein was detected in the culture supernatant from 31 tested clinical isolates of GBS, suggesting a wide distribution of Bsp in these bacteria. Overexpression of bsp resulted in lens-shaped GBS cells, indicating a role for bsp in controlling cell morphology. Insertional disruption of femH resulted in a reduction of the L-alanine content of the peptidoglycan, suggesting that femH is involved in the incorporation of L-alanine residues in the interpeptide chain of the peptidoglycan of GBS.
Databáze:	OpenAIRE
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