Metallopeptidases produced by group B Streptococcus: Influence of proteolytic inhibitors on growth and on interaction with human cell lineages
Group B Streptococcus (GBS) is a major etiologic agent of neonatal bacterial infections and is the most common cause of sepsis and pneumonia in newborns. Surface and secreted molecules of GBS are often essential virulence factors which are involved in the adherence of the bacteria to host cells or a...
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Veröffentlicht in: | International journal of molecular medicine 2008-07, Vol.22 (1), p.119-125 |
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Zusammenfassung: | Group B Streptococcus (GBS) is a major etiologic agent of neonatal bacterial
infections and is the most common cause of sepsis and pneumonia in newborns. Surface
and secreted molecules of GBS are often essential virulence factors which are
involved in the adherence of the bacteria to host cells or are required to suppress
the defense mechanisms of hosts. We analyzed the peptidase profiles of GBS by
detection of proteolytic activities on SDS-PAGE containing copolymerized gelatin
as substrate. Based on the inhibition by o-phenathroline and EGTA, three distinct
peptidases of 220, 200 and 180 kDa were identified in the culture medium, besides
one major cell-associated proteolytic activity, a 200-kDa metallopeptidase, suggesting
that all were zinc-metallopeptidases. GBS culture supernatants, rich in metallotype
peptidases, also cleaved fibronectin, laminin, type IV collagen, fibrinogen and
albumin. Cleavage of the host extracellular matrix by GBS may be a relevant factor
in the process of bacterial dissemination and/or invasion. Notably, metallopeptidase
inhibitors strongly blocked GBS growth as well as its interaction with human cell
lineages. Understanding the contribution of peptidases to the pathogenesis of
GBS disease may broaden our perception of how this significant pathogen causes
severe infections in newborn infants. |
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ISSN: | 1107-3756 1791-244X |
DOI: | 10.3892/ijmm.22.1.119 |