Relationship Between Group B Streptococcal Serotypes and Cell Surface Hydrophobicity

Abstract

Cell surface hydrophobicities of streptococci of serological group B were determined by the adherence of the bacteria to hexadecane droplets. A significant adherence to hexadecane was observed with the group B streptococcal type reference strains Ib, V, Ic, Rand X, but not with those of serotype Ia, 11, 111 and IV. Cultivation of the bacteria in microcapsule-inducing media reduced the hexadecane adherence properties. The adherence to hexadecane was not related to fibrinogen binding properties of the cultures. Screening a large number of group B streptococci isolated from humans and bovines revealed that those with polysaccharide type antigen alone were generally hydrophilic, those with protein antigen alone or with protein antigen in combination with polysaccharide antigen were mostly hydrophobic. Cultivation of the bacteria under microaerobic conditions or after a single mouse passage enhanced microcapsule production and correspondingly reduced the hexadecane adherence values. Treatment of the bacteria by guanidinium chloride or by neuraminidase enhanced the hexadecane adherence. The hydrophobic component on group B streptococcal surface appeared to be partly inactivated by heat or proteolytic treatment of the bacteria. * Corresponding author. US. Copyright Clearance Center Code Statement: 093 1 -1793/92/3905 -0376$02.50/0 Relationship Between Group B Streptococcal Serotypes 377group A streptococci could also be determined by partition of the bacteria in an aqueous dextran polyethylene glycol two-phase system (13) and by the adherence of the bacteria to hexadecane droplets (19).

The Novel Fibrinogen-Binding Protein FbsB PromotesStreptococcus agalactiaeInvasion into Epithelial Cells

“…Numerous studies have described the ability of clinical S. agalactiae isolates to interact with human fibrinogen (11,56,62,81). Recently, Schubert et al (57) identified in S. agalactiae a fibrinogen-binding protein, which was termed FbsA.…”

FbsA, a fibrinogen-binding protein from Streptococcus agalactiae, mediates platelet aggregation

“…26 Strain 7805 (serotype Ib) was kindly provided by G. S. Chhatwal (Department of Microbial Pathogenesis and Vaccine Research, German Research Center for Biotechnology [GBF], Braunschweig, Germany), and strain 1504 (serotype V) was obtained from the collection of the National Reference Center for Streptococci in Aachen, Germany. S agalactiae was cultivated at 37°C in Todd-Hewitt broth containing 1% yeast extract.…”

FbsA-Driven Fibrinogen Polymerization: A Bacterial “Deceiving Strategy”

“…GBS cultures (strain 6313, serotype III, see [13]), were exposed to fibrinogen tagged by Fluorescein isothiocyanate (FITC) for 2 h at 22 C in an end-over-end mixer, and then centrifuged/resuspended to get rid of unbound FITC-Fbg. The microscope image in Fig.…”