Literature DB >> 15206915

Serum antibodies against the hemoglobin-binding domain (HA2) of Porphyromonas gingivalis.

Arthur A DeCarlo1, Mangala Nadkarni, Mayuri Paramaesvaran, Peter W Yun, Charles A Collyer, Neil Hunter.   

Abstract

BACKGROUND: The hemoglobin-binding domain (HA2) of the Porphyromonasgingivalis gingipains and hemagglutinins strongly binds hemoglobin and hemin and is thought to play a key role in acquisition of this essential metabolite by the microorganism.
METHODS: In this report, we partially characterized human anti-HA2 humoral antibodies and their relationship to periodontal disease in an analysis of titer and function.
RESULTS: Overall, serum anti-HA2 antibodies were relatively low and dominated by the immunoglobulin M (IgM) isotype. Pre-therapy titers had a direct association with periodontal health. Levels of P. gingivalis in the plaque were directly related to pre-therapy anti-HA2 IgG levels, and were an important covariant in a significant direct relationship between pre- and post-therapy anti-HA2 titers. Post-therapy anti-HA2 IgG antibody titers were directly related to the capacity of serum IgG fractions to neutralize hemoglobin binding by Lys-gingipain (Kgp). Further, lower levels of neutralizing activity post-therapy were directly related to severe periodontitis within the patient cohort.
CONCLUSIONS: These data suggest that anti-HA2 IgG antibodies correspond directly with periodontal health, possibly through their ability to neutralize P. gingivalis hemoglobin capture. The data also suggest that inadvertent or therapeutic inoculation of P. gingivalis in the plaque may contribute to generation of neutralizing anti-HA2 IgG and improvement of periodontal prognosis. Copyright Blackwell Munksgaard, 2004

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Year:  2004        PMID: 15206915     DOI: 10.1111/j.1600-0765.2004.00730.x

Source DB:  PubMed          Journal:  J Periodontal Res        ISSN: 0022-3484            Impact factor:   4.419


  5 in total

1.  The hemoglobin receptor protein of porphyromonas gingivalis inhibits receptor activator NF-kappaB ligand-induced osteoclastogenesis from bone marrow macrophages.

Authors:  Yuji Fujimura; Hitoshi Hotokezaka; Naoya Ohara; Mariko Naito; Eiko Sakai; Mamiko Yoshimura; Yuka Narita; Hideki Kitaura; Noriaki Yoshida; Koji Nakayama
Journal:  Infect Immun       Date:  2006-05       Impact factor: 3.441

2.  Hemoglobin receptor protein from Porphyromonas gingivalis induces interleukin-8 production in human gingival epithelial cells through stimulation of the mitogen-activated protein kinase and NF-κB signal transduction pathways.

Authors:  Yuki Fujita; Masaaki Nakayama; Mariko Naito; Eiki Yamachika; Tetsuyoshi Inoue; Koji Nakayama; Seiji Iida; Naoya Ohara
Journal:  Infect Immun       Date:  2013-10-14       Impact factor: 3.441

Review 3.  Gingipains from Porphyromonas gingivalis - Complex domain structures confer diverse functions.

Authors:  N Li; C A Collyer
Journal:  Eur J Microbiol Immunol (Bp)       Date:  2011-03

4.  Identification and Modification of Porphyromonas gingivalis Cysteine Protease, Gingipain, Ideal for Screening Periodontitis.

Authors:  Kimito Hirai; Tomoko Yamaguchi-Tomikawa; Toru Eguchi; Hiroshi Maeda; Shogo Takashiba
Journal:  Front Immunol       Date:  2020-06-05       Impact factor: 7.561

5.  In situ visualization of plasma cells producing antibodies reactive to Porphyromonas gingivalis in periodontitis: the application of the enzyme-labeled antigen method.

Authors:  Y Mizutani; S Tsuge; H Takeda; Y Hasegawa; K Shiogama; T Onouchi; K Inada; T Sawasaki; Y Tsutsumi
Journal:  Mol Oral Microbiol       Date:  2014-05-10       Impact factor: 3.563

  5 in total

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