title: Survey of immunological features of the alpha-like proteins of Streptococcus agalactiae.
abstract: Nearly all Streptococcus agalactiae (group B streptococcus [GBS]) strains express a protein which belongs to the so-called alpha-like proteins (Alps), of which Cα, Alp1, Alp2, Alp3, Rib, and Alp4 are known to occur in GBS. The Alps are chimeras which form mosaic structures on the GBS surface. Both N- and C-terminal stretches of the Alps possess immunogenic sites of dissimilar immunological specificity. In this review, we have compiled data dealing with the specificity of the N- and C-terminal immunogenic sites of the Alps. The majority of N-terminal sites show protein specificity while the C-terminal sites show broader cross-reactivity. Molecular serotyping has revealed that antibody-based serotyping has often resulted in erroneous Alp identification, due to persistence of cross-reacting antibodies in antisera for serotyping. Retrospectively, this could be expected on the basis of sequence analysis results. Some of the historical R proteins are in fact Alps. The data included in the review may provide a basis for decisions regarding techniques for the preparation of specific antisera for serotyping of GBS, for use in other approaches in GBS research, and for decision making in the context of GBS vaccine developments.
authors.affiliation: Department of Laboratory Medicine, Children's and Women's Health, Norwegian University of Science and Technology, Trondheim, Norway.
authors.forename: Johan A
authors.initials: JA
authors.lastname: Maeland
authors.affiliation: Department of Laboratory Medicine, Children's and Women's Health, Norwegian University of Science and Technology, Trondheim, Norway Department of Medical Microbiology, St. Olav's University Hospital, Trondheim, Norway.
authors.forename: Jan E
authors.initials: JE
authors.lastname: Afset
authors.affiliation: Department of Medical Microbiology, St. Olav's University Hospital, Trondheim, Norway.
authors.forename: Randi V
authors.initials: RV
authors.lastname: Lyng
authors.affiliation: Department of Laboratory Medicine, Children's and Women's Health, Norwegian University of Science and Technology, Trondheim, Norway Department of Medical Microbiology, St. Olav's University Hospital, Trondheim, Norway andreas.radtke@ntnu.no.
authors.forename: Andreas
authors.initials: A
authors.lastname: Radtke
mesh_terms: D000818:Animals; D000907:Antibodies, Bacterial / Q000097:blood; D000942:Antigens, Bacterial / Q000276:immunology*; D001426:Bacterial Proteins / Q000276:immunology*; D003429:Cross Reactions; D000939:Epitopes / Q000276:immunology; D006801:Humans; D008565:Membrane Proteins / Q000276:immunology; D017434:Protein Structure, Tertiary; D012703:Serotyping; D013292:Streptococcus agalactiae / Q000145:classification / Q000276:immunology*
chemical_list: D000907:Antibodies, Bacterial; D000942:Antigens, Bacterial; D001426:Bacterial Proteins; D000939:Epitopes; D008565:Membrane Proteins