Complete And Incomplete Ibc Protein Fraction in Group B Streptococci

Bevanger, Lars; Mæeland, Johan A.

doi:10.1111/j.1699-0463.1979.tb02402.x

Cited by 23 publications

(11 citation statements)

References 9 publications

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“…The Z antigen was surface exposed, was susceptible to pepsin and trypsin digestion, and resisted m-periodate oxidation, consistent with the protein nature of the antigen. Its susceptibility to trypsin digestion was similar to that of R3 (12), and this makes a distinction between the Z and R3 antigens on the one hand and the trypsin-resistant alpha-like proteins of GBS on the other (3,8).…”

Section: Discussionmentioning

confidence: 95%

Putative Novel Surface-Exposed Streptococcus agalactiae Protein Frequently Expressed by the Group B Streptococcus from Zimbabwe

Mavenyengwa

Mæland

Moyo

2009

Clin Vaccine Immunol

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Group B streptococci (GBS) express a variety of surface-exposed and strain-variable proteins which function as phenotypic markers and as antigens which are able to induce protective immunity in experimental settings. Among these proteins, the chimeric and immunologically cross-reacting alpha-like proteins are particularly important. Another protein, R3, which has been less well studied, occurred at a frequency of 21.5% in GBS from Zimbabwe and, notably, occurred in serotype V strains at a frequency of 75.9%. Working with rabbit antiserum raised against the R3 reference strain ATCC 49447 (strain 10/84; serotype V/R3) to detect the expression of the R3 protein, we recorded findings which suggested that strain 10/84 expressed a strain-variable protein antigen, in addition to R3. The antigen was detected by various enzyme-linked immunosorbent assay-based tests by using acid extract antigens or GBS whole-cell coats and by whole-cell-based Western blotting. We named the putative novel antigen the Z antigen. The Z antigen was a high-molecular-mass antigen that was susceptible to degradation by pepsin and trypsin but that was resistant to m-periodate oxidation and failed to show immunological cross-reactivity with any of a variety of other GBS protein antigens. The Z antigen was expressed by 33/121 (27.2%) of strains of a Zimbabwean GBS strain collection and by 64.2% and 72.4% of the type Ib and type V strains, respectively, and was occasionally expressed by GBS of other capsular serotypes. Thus, the putative novel GBS protein named Z showed distinct capsular antigen associations and presented as an important phenotypic marker in GBS from Zimbabwe. It may be an important antigen in GBS from larger areas of southern Africa. Its prevalence in GBS from Western countries is not known.Streptococcus agalactiae (the group B streptococcus [GBS]) possesses genotypic and phenotypic markers which are important in epidemiological settings. Among the established phenotypic markers, the capsular polysaccharides (CPSs) Ia, Ib, and II through IX play prominent roles in the classification of GBS, in the pathogenesis of GBS disease, and as targets of protective antibodies (15). A variety of surface-anchored and strain-variable proteins are also important GBS markers. These proteins make it possible to define GBS serosubtypes within each CPS type by using antibody-based or gene-based methods for subtyping (6, 11 19, 22). These proteins include Cß and the alpha-like proteins (Alps) C␣, Alp1 (formerly epsilon), Alp2 and Alp3 (formerly probably R1), and Rib (another designation for the R4 protein) (28). The Alps are characterized, among other ways, by a repeat-containing region which has a causal relation to the ladder-like patterns formed by these proteins on sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE) and Western blotting. The Alps possess chimeric sequences, show variable immunological crossreactivities, and induce increased resistance to GBS infections in experimental models (1,13,15,18,30). For this reason, th...

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Section: Discussionmentioning

confidence: 95%

Putative Novel Surface-Exposed Streptococcus agalactiae Protein Frequently Expressed by the Group B Streptococcus from Zimbabwe

Mavenyengwa

Mæland

Moyo

2009

Clin Vaccine Immunol

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“…The Ibc proteins of group B streptococci include two distinct antigens, the a and p antigens (7). The potentiality of these antigens as markers in the serological classification of group B streptococci has been investigated (4, 9).…”

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confidence: 99%

Mouse‐Protective Antibodies Against The Ibc Proteins of Group B Streptococci

Bevanger¹,

Néss²

1985

Acta Pathologica Microbiologica Scandinavica Series B: Microbio

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Antiserum to each of the α and β antigens of the Ibc protein fraction of group B streptococci was raised in rabbits. A possible protective effect of the antisera in mice challenged by group B streptococci was evaluated. Antiserum against each of the antigens significantly increased the survival rates of mice challenged by bacteria which produced the corresponding antigen, but not of those challenged by bacteria which produced only the heterologous antigen. Animals challenged with a strain which produced both of the α and β antigens were protected by antiserum to the β antigen but not by antiserum to the α antigen. In this case the effect of the anti‐α serum was a postponement of death of the animals. The antisera showed no protection of animals challenged by a group B streptococcal strain which did not produce any of the Ibc protein antigens.

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“…The trypsin-sensitive antigen (C␤) was a non-Alp, but the trypsin-resistant antigen might have been the alpha antigen (C␣). In 1979, Bevanger and Maeland (6) described two precipitinogens in HCl extracts from the CPS type Ia strain A909 and the type Ib strain H36B and one precipitinogen in the type Ia strain 335 (6). The strain 335 antigen cross-reacted immunologically with one of the two A909 and H36B antigens and was trypsin resistant but sensitive to pepsin digestion.…”

mentioning

confidence: 99%

“…The second A909 and H36B antigen which was sensitive to trypsin was called C␤. Today, we know that the trypsin-resistant 335 antigen was Alp1, which at that time was erroneously considered to be C␣ due to immunological crossreactivity (see below), while the trypsin-resistant A909 and H36B antigens were true C␣ (6). Strain A909 has since been a prototype strain for C␣.…”

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Survey of Immunological Features of the Alpha-Like Proteins of Streptococcus agalactiae

Mæland

Afset

Lyng

et al. 2014

Clin. Vaccine Immunol.

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bNearly all Streptococcus agalactiae (group B streptococcus [GBS]) strains express a protein which belongs to the so-called alphalike proteins (Alps), of which C␣, 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.

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Complete And Incomplete Ibc Protein Fraction in Group B Streptococci

Cited by 23 publications

References 9 publications

Putative Novel Surface-Exposed Streptococcus agalactiae Protein Frequently Expressed by the Group B Streptococcus from Zimbabwe

Putative Novel Surface-Exposed Streptococcus agalactiae Protein Frequently Expressed by the Group B Streptococcus from Zimbabwe

Mouse‐Protective Antibodies Against The Ibc Proteins of Group B Streptococci

Survey of Immunological Features of the Alpha-Like Proteins of Streptococcus agalactiae

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