Affiliation:
1. Department of Microbiology and Biotechnology, University of Ulm, Ulm,1 and
2. Department of Microbiology, National Research Center for Biotechnology, Braunschweig,2 Germany
Abstract
ABSTRACT
Group B streptococcus (GBS) is the leading cause of bacterial sepsis and meningitis in neonates. N-terminal sequencing of major proteins in the culture supernatant of a clinical isolate of GBS identified a protein of about 50 kDa which could be detected in all of 27 clinical isolates tested. The corresponding gene, designated
pcsB
, was isolated from a GBS cosmid library and subsequently sequenced. The deduced PcsB polypeptide consists of 447 amino acid residues (
M
r
, 46,754), carries a potential N-terminal signal peptide sequence of 25 amino acids, and shows significant similarity to open reading frames of unknown function from different organisms and to the murein hydrolase P45 from
Listeria monocytogenes
. Northern blot analysis revealed a monocistronic transcriptional organization for
pcsB
in GBS. Insertional inactivation of
pcsB
in the genome of GBS resulted in mutant strain Sep1 exhibiting a drastically reduced growth rate compared to the parental GBS strain and showing an increased susceptibility to osmotic pressure and to various antibiotics. Electron microscopic analysis of GBS mutant Sep1 revealed growth in clumps, cell separation in several planes, and multiple division septa within single cells. These data suggest a pivotal role of PcsB for cell division and antibiotic tolerance of GBS.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
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