N-terminal anchor in surface immunogenic protein of Streptococcus agalactiae and its influence on immunity elicitation
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Amino Acid Motifs MeSH
- Antigens, Bacterial chemistry genetics immunology MeSH
- Humans MeSH
- Molecular Sequence Data MeSH
- Mice, Inbred BALB C MeSH
- Mice MeSH
- Antibodies, Bacterial blood MeSH
- Amino Acid Sequence MeSH
- Streptococcus agalactiae chemistry genetics immunology MeSH
- Streptococcal Infections immunology microbiology MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Male MeSH
- Mice MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Antigens, Bacterial MeSH
- Antibodies, Bacterial MeSH
- SIP protein, Streptococcus group B MeSH Browser
A multiplex PCR method was developed to characterize the potential variability within the sip gene from bovine isolates of Streptococcus agalactiae. An incomplete sip gene (ncosip) was found in four isolates of S. agalactiae. According to the in silico analysis of the missing region at amino acid level, the N-terminal of surface immunogenic protein (Sip) was found to contain a LysM domain motif; whilst the incomplete Sip (NcoSip) lacked a part of this motif. Immunity elicitation against Sip was confirmed by immunization of mice. This response was partially observed also with NcoSip.
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