ArticleClinical and experimental immunology1997
The relationship between colonization and haemagglutination inhibiting and B cell epitopes of Porphyromonas gingivalis.
Article in Clinical and experimental immunology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 55 citations in OpenAlex.
- Disordered epitopes as peptide vaccines.Peptide science (Hoboken, N.J.) · 2018Review
- Strategies for the inhibition of gingipains for the potential treatment of periodontitis and associated systemic diseases.Journal of oral microbiology · 2014Review
- Both the unique and repeat regions of the Porphyromonas gingivalis hemagglutin A are involved in adhesion and invasion of host cells.Anaerobe · 2012Article
- HGP44 induces protection against Porphyromonas gingivalis-Induced alveolar bone loss in mice.Clinical and vaccine immunology : CVI · 2011Article
- Gingipains from Porphyromonas gingivalis - Complex domain structures confer diverse functions.European journal of microbiology & immunology · 2011Review
- Construction of recombinant hemagglutinin derived from the gingipain-encoding gene of Porphyromonas gingivalis, identification of its target protein on erythrocytes, and inhibition of hemagglutination by an interdomain regional peptide.Journal of bacteriology · 2007Article
- Inactivation of vimF, a putative glycosyltransferase gene downstream of vimE, alters glycosylation and activation of the gingipains in Porphyromonas gingivalis W83.Infection and immunity · 2005Article
- Cognate peptide-receptor ligand mapping by directed phage display.Proteome science · 2005Article
- The vimE gene downstream of vimA is independently expressed and is involved in modulating proteolytic activity in Porphyromonas gingivalis W83.Infection and immunity · 2004Article
- Distribution of Porphyromonas gingivalis biotypes defined by alleles of the kgp (Lys-gingipain) gene.Journal of clinical microbiology · 2004Article
- Humoral responses to Porphyromonas gingivalis gingipain adhesin domains in subjects with chronic periodontitis.Infection and immunity · 2004Article
- Enhancement of Th2 pathways and direct activation of B cells by the gingipains of Porphyromonas gingivalis.Clinical and experimental immunology · 2003Article
- Hydrolysis of epithelial junctional proteins by Porphyromonas gingivalis gingipains.Infection and immunity · 2002Article
- Porphyromonas gingivalis gingipains and adhesion to epithelial cells.Infection and immunity · 2001Article
- vimA gene downstream of recA is involved in virulence modulation in Porphyromonas gingivalis W83.Infection and immunity · 2001Article
- RgpA-Kgp peptide-based immunogens provide protection against Porphyromonas gingivalis challenge in a murine lesion model.Infection and immunity · 2000Article
- Serum immunoglobulin G (IgG) and IgG subclass responses to the RgpA-Kgp proteinase-adhesin complex of Porphyromonas gingivalis in adult periodontitis.Infection and immunity · 2000Article
- Variable carbohydrate modifications to the catalytic chains of the RgpA and RgpB proteases of Porphyromonas gingivalis W50.Infection and immunity · 1999Article
- Life below the gum line: pathogenic mechanisms of Porphyromonas gingivalis.Microbiology and molecular biology reviews : MMBR · 1998Review
- A peptide domain on gingipain R which confers immunity against Porphyromonas gingivalis infection in mice.Infection and immunity · 1998Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Passive immunization with the monoclonal antibody 61BG1.3 selectively prevents colonization by Porphyromonas gingivalis in humans (Booth V, Ashley FP, Lehner T. Infect Immun 1996; 64:422-7). The protective MoAb recognizes the beta component of the RI protease of P. gingivalis which is formed by proteolytic processing of a polyprotein precursor termed PrpR1. This subunit is both a haemagglutinin and an antigen which is recognized by sera from patients with periodontitis. In this study the relationship was investigated between a colonization epitope which is recognized by the MoAb 61BG1.3, a haemagglutinating and B cell epitope which are recognized by sera from patients with periodontitis. B cell epitopes were mapped by Western blotting with a series of truncated recombinant polypeptides spanning the adhesion domain within residues 784-1130 of PrpR1 and by ELISA using a panel of synthetic peptides spanning the same sequence. The epitope which is recognized by the protective MoAb was mapped within residues 907-931 of PrpR1, while serum responses of patients were directed predominantly to the adjacent carboxy-terminal sequence within residues 934-1042. The haemagglutinating epitope was mapped to residues 1073-1112. In view of our previous findings that the MoAb 61BG1.3 prevents colonization of P. gingivalis in vivo and inhibits haemagglutination, these two epitopes may be in proximity in the native protein. Active or passive immunization strategies which target the protective or haemagglutinating epitopes of the adhesion domain of PrpR1 may provide a means of preventing infection with P. gingivalis.
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