Cloning and expression in Escherichia coli of a protective surface protein from type V group B streptococci.
This report describes a trypsin-resistant laddering protein purified from a type V strain, a serotype of important emerging clinical significance. This protein is present in a majority of type V clinical strains, elicits protective antibody in an animal model, and is cross-reactive with the alpha C protein and R1. The gene encoding this protein has been cloned; preliminary nucleotide sequence analysis reveals significant homology, though not identity, with the alpha C protein gene. These data support the hypothesis that there exists a family of related but distinct GBS surface proteins which may play a role in immunity to GBS infection.
Lachenauer
C S
CS
Channing Laboratory, Department of Medicine, Brigham and Women's Hospital, Boston, Massachusetts, USA.
Madoff
L C
LC
D000818:Animals; D000831:Animals, Newborn; D001426:Bacterial Proteins / Q000235:genetics* / Q000276:immunology; D003001:Cloning, Molecular; D003429:Cross Reactions; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D005798:Genes, Bacterial; D006801:Humans; D007116:Immunization, Passive; D007120:Immunochemistry; D008565:Membrane Proteins / Q000235:genetics / Q000276:immunology; D051379:Mice; D016133:Polymerase Chain Reaction; D012703:Serotyping; D013292:Streptococcus agalactiae / Q000145:classification / Q000235:genetics* / Q000276:immunology
D001426:Bacterial Proteins; D008565:Membrane Proteins