ArticleInfection and immunity2004
Characterization of the Streptococcus mutans P1 epitope recognized by immunomodulatory monoclonal antibody 6-11A.
Article in Infection and immunity, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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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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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- An intramolecular lock facilitates folding and stabilizes the tertiary structure of Streptococcus mutans adhesin P1.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Alterations in immunodominance of Streptococcus mutans AgI/II: lessons learned from immunomodulatory antibodies.Vaccine · 2014Article
- An intramolecular interaction involving the N terminus of a streptococcal adhesin affects its conformation and adhesive function.The Journal of biological chemistry · 2013Article
- Article
- Induction of neutralizing antibodies in mice immunized with an amino-terminal polypeptide of Streptococcus mutans P1 protein produced by a recombinant Bacillus subtilis strain.FEMS immunology and medical microbiology · 2010Article
- Beneficial immunomodulation by Streptococcus mutans anti-P1 monoclonal antibodies is Fc independent and correlates with increased exposure of a relevant target epitope.Journal of immunology (Baltimore, Md. : 1950) · 2009Article
- Requirements for surface expression and function of adhesin P1 from Streptococcus mutans.Infection and immunity · 2008Article
- Antibody-mediated immunomodulation: a strategy to improve host responses against microbial antigens.Infection and immunity · 2005Review
- Redirecting the humoral immune response against Streptococcus mutans antigen P1 with monoclonal antibodies.Infection and immunity · 2004Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Monoclonal antibody (MAb) 6-11A directed against Streptococcus mutans surface adhesin P1 was shown previously to influence the mucosal immunogenicity of this organism in BALB/c mice. The specificity of anti-P1 serum immunoglobulin G (IgG) and secretory IgA antibodies and the subclass distribution of anti-P1 serum IgG antibodies were altered, and the ability of elicited serum antibodies to inhibit S. mutans adherence in vitro was in certain cases increased. MAb 6-11A is known to recognize an epitope dependent on the presence of the proline-rich region of the protein, although it does not bind directly to the isolated P-region domain. In this report, we show that MAb 6-11A recognizes a complex discontinuous epitope that requires the simultaneous presence of the alanine-rich repeat domain (A-region) and the P-region. Formation of the core epitope requires the interaction of these segments of P1. Residues amino terminal to the A-region also contributed to recognition by MAb 6-11A but were not essential for binding. Characterization of the MAb 6-11A epitope will enable insight into potential mechanisms of immunomodulation and broaden our understanding of the tertiary structure of P1.
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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.