Abstract
Our previous reports implicated the Hsp90 homologue (HtpG) of Porphyromonas gingivalis (Pg) in its virulence in periodontal disease. We investigated the role of the HtpG stress protein in the virulence of Pg. This report describes the (i) expression of a recombinant Pg HtpG (rHtpG), (ii) generation and characterization of a polyclonal rabbit anti-Pg rHtpG antiserum, and (iii) construction of a Pg htpG isogenic mutant and evaluation of the growth, adherence and invasion properties compared to the wild-type parental strain. The disruption of the htpG gene did not significantly affect growth, and had no effect on Pg adherence to and invasion of cultured human cells.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Antibodies, Bacterial
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Bacterial Adhesion / genetics
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Bacterial Proteins / genetics*
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Bacterial Proteins / immunology
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Base Sequence
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Cell Line
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DNA, Bacterial / genetics
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HSP90 Heat-Shock Proteins / genetics*
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HSP90 Heat-Shock Proteins / immunology
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Humans
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Mutagenesis
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Plasmids / genetics
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Porphyromonas gingivalis / genetics*
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Porphyromonas gingivalis / immunology
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Porphyromonas gingivalis / pathogenicity
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Rabbits
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Recombinant Proteins / genetics
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Recombinant Proteins / immunology
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Virulence / genetics
Substances
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Antibodies, Bacterial
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Bacterial Proteins
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DNA, Bacterial
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HSP90 Heat-Shock Proteins
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Recombinant Proteins
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HtpG protein, bacteria