ArticleInfection and immunity2000
Identification of group B streptococcal Sip protein, which elicits cross-protective immunity.
Article in Infection and immunity, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
64 citing papers in PubMed, 159 citations in OpenAlex.
- Role of pilus proteins in adherence and invasion of Streptococcus agalactiae to the lung and cervical epithelial cells.The Journal of biological chemistry · 2013Trial
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- A CRISPRi Library Screen in Group BbioRxiv : the preprint server for biology · 2024Article
- Surface protein distribution in Group B Streptococcus isolates from South Africa and identifying vaccine targets through in silico analysis.Scientific reports · 2024Article
- Article
- Exploring the Immunoprotective Potential of a Nanocarrier Immersion Vaccine Encoding Sip againstVaccines · 2023Article
- Ultra-Fast Impedimetric Immunoassay for Detection ofMicromachines · 2023Article
- Characterization and virulence ofFrontiers in microbiology · 2023Article
- Designing multi-epitope-based vaccine targeting surface immunogenic protein of Streptococcus agalactiae using immunoinformatics to control mastitis in dairy cattle.BMC veterinary research · 2022Article
- Protein-Based Adjuvants for Vaccines as Immunomodulators of the Innate and Adaptive Immune Response: Current Knowledge, Challenges, and Future Opportunities.Pharmaceutics · 2022Review
- Virulence Factor Genes and Cytotoxicity ofMicrobiology spectrum · 2022Article
- Streptococcal bacterial components in cancer therapy.Cancer gene therapy · 2022Review
- Immunogenic Proteins of Group B Streptococcus-Potential Antigens in Immunodiagnostic Assay for GBS Detection.Pathogens (Basel, Switzerland) · 2021Review
- Clinical utilization of species-specific immunoassays for identification of Staphylococcus aureus and Streptococcus agalactiae in orthopedic infections.Journal of orthopaedic research : official publication of the Orthopaedic Research Society · 2021Article
- Bacterial protein domains with a novel Ig-like fold target human CEACAM receptors.The EMBO journal · 2021Article
- The Recombinant Expression Proteins FnBP and ClfA FromFrontiers in veterinary science · 2021Article
- Multidrug-ResistantMicroorganisms · 2020Article
- Development and analytical validation of real-time PCR for the detection of Streptococcus agalactiae in pregnant women.BMC pregnancy and childbirth · 2020Article
- Mucosal Vaccination withVaccines · 2020Article
4 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A protein of group B streptococci (GBS), named Sip for surface immunogenic protein, which is distinct from previously described surface proteins, was identified after immunological screening of a genomic library. Immunoblots using a Sip-specific monoclonal antibody indicated that a protein band with an approximate molecular mass of 53 kDa which did not vary in size was present in every GBS strain tested. Representatives of all nine GBS serotypes were included in the panel of strains. Cloning and sequencing of the sip gene revealed an open reading frame of 1,305 nucleotides coding for a polypeptide of 434 amino acid residues, with a calculated pI of 6. 84 and molecular mass of 45.5 kDa. Comparison of the nucleotide sequences from six different strains confirmed with 98% identity that the sip gene is highly conserved among GBS isolates. N-terminal amino acid sequencing also indicated the presence of a 25-amino-acid signal peptide which is cleaved in the mature protein. More importantly, immunization with the recombinant Sip protein efficiently protected CD-1 mice against deadly challenges with six GBS strains of serotypes Ia/c, Ib, II/R, III, V, and VI. The data presented in this study suggest that this highly conserved protein induces cross-protective immunity against GBS infections and emphasize its potential as a universal vaccine candidate.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.