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Epidemiologically and clinically relevant Group B Streptococcus isolates do not bind collagen but display enhanced binding to human fibrinogen.
- Source :
-
Microbes and infection [Microbes Infect] 2012 Oct; Vol. 14 (12), pp. 1044-8. Date of Electronic Publication: 2012 Jul 24. - Publication Year :
- 2012
-
Abstract
- Group B Streptococcus (GBS) is the leading cause of neonatal septicemia and meningitis. Pili appendages were shown to play a critical role in bacterial adhesion and colonization of human tissues. Recently it was claimed that binding of the pilus-associated adhesin PilA to collagen is a critical, initial step in promoting interactions with the α2β1 integrin expressed on brain endothelial cells. Here we show that strain NCTC10/84 used in this study is not representative for GBS isolates and question the importance of collagen as a critical extracellular matrix component for GBS infections of the central nervous system.<br /> (Copyright © 2012 Institut Pasteur. Published by Elsevier Masson SAS. All rights reserved.)
Details
- Language :
- English
- ISSN :
- 1769-714X
- Volume :
- 14
- Issue :
- 12
- Database :
- MEDLINE
- Journal :
- Microbes and infection
- Publication Type :
- Academic Journal
- Accession number :
- 22841805
- Full Text :
- https://doi.org/10.1016/j.micinf.2012.07.004