Large, identical, tandem repeating units in the C protein alpha antigen gene, bca, of group B streptococci.
Michel James L,Lawrence C. Madoff,Kristin Olson,David E. Kling,Dennis L. Kasper,Frederick M. Ausubel +5 more
TL;DR: The C protein alpha antigen structural gene (named bca for group B, C protein, alpha) is cloned into Escherichia coli and demonstrates a regularly laddered pattern of heterogeneous polypeptides.
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Abstract: Group B Streptococcus (GBS) is the leading cause of neonatal sepsis and meningitis in the United States. The surface-associated C protein alpha antigen of GBS is thought to have a role in both virulence and immunity. We previously cloned the C protein alpha antigen structural gene (named bca for group B, C protein, alpha) into Escherichia coli. Western blots of both the native alpha antigen and the cloned gene product demonstrate a regularly laddered pattern of heterogeneous polypeptides. The nucleotide sequence of the bca locus reveals an open reading frame of 3060 nucleotides encoding a precursor protein of 108,705 Da. Cleavage of a putative signal sequence of 41 amino acids yields a mature protein of 104,106 Da. The 20,417-Da N-terminal region of the alpha antigen shows no homology to previously described protein sequences and is followed by a series of nine tandem repeating units that make up 74% of the mature protein. Each repeating unit is identical and consists of 82 amino acids with a molecular mass of 8665 Da, which is encoded by 246 nucleotides. The size of the repeating units corresponds to the observed size differences in the heterogeneous ladder of alpha C proteins expressed by GBS. The C-terminal region of the alpha antigen contains a membrane anchor domain motif that is shared by a number of Gram-positive surface proteins. The large region of identical repeating units in bca defines protective epitopes and may play a role in generating phenotypic and genotypic diversity of the alpha antigen.
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Citations
Patent
CLONING OF NON-IgA Fc BINDING FORMS OF THE GROUP B STREPTOCOCCAL BETA ANTIGENS
L. Jeannine Brady
- 15 May 1995
TL;DR: In this paper, genetic manipulation of the gene encoding a group B streptococcal (GBS) surface protein known as the beta antigen has been discussed, and a new polypeptide encoded by the altered beta antigen gene does not bind to IgA but does immunoreact with monospecific anti-beta antigen antisera raised against the wild type.
18
The Solution Structure of the C-terminal Modular Pair from Clostridium perfringens μ-Toxin Reveals a Noncellulosomal Dockerin Module
TL;DR: Size-exclusion chromatography and heteronuclear NMR-based chemical shift mapping studies indicate that the helical face of the dockerin module recognizes the CpGH84C X82 module, which may have important implications in the pathogenic properties of C. perfringens.
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Comparison of three different methods in monoclonal antibody-based detection of Streptococcus agalactiae protein serotype markers
TL;DR: Comparison of whole‐cell‐based fluorescent antibody testing (FAT), ELISA, and dot blotting for MAb‐based detection of surface‐exposed proteins in Streptococcus agalactiae considers all three methods acceptable for serotyping of GBS.
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Subdominance in Antibody Responses: Implications for Vaccine Development.
TL;DR: Overall, the available data indicate that subdominant protein regions are of much interest for vaccine development, not least in bacterial and protozoal systems, for which antibody subdominance remains largely unexplored.
17
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