The collagenase activity ofPorphyromonas gingivalisis due to Arg-gingipain

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The collagenase activity of Porphyromonas gingivalis is due to Arg-gingipain.

Degradation of type I collagen by Porphyromonas gingivalis was monitored by fluorogenic, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and growth assays. All three assays showed that inactivation of both the rgpA and rgpB genes was necessary to completely eliminate the capacity of P. gingivalis to cleave type I collagen. Leupeptin, an Arg-gingipain-specific protease inhi...

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Generation of lys-gingipain protease activity in Porphyromonas gingivalis W50 is independent of Arg-gingipain protease activities.

Porphyromonas gingivalis, a black-pigmenting anaerobe implicated in the aetiology of periodontal disease, contains two loci, rgpA and rgpB, encoding the extracellular Arg-X specific proteases (RGPs, Arg-gingipains), and kgp, which encodes a Lys-X specific protease (KGP, Lys-gingipain). The rgpA and kgp genes encode polyproteins comprising pro-peptide and catalytic domain with large N- and C-ter...

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Sequential autolytic processing activates the zymogen of Arg-gingipain.

Most proteases are synthesized as inactive precursors to protect the synthetic machinery of the cell and allow timing of activation. The mechanisms used to render latency are varied but tend to be conserved within protease families. Proteases belonging to the caspase family have a unique mechanism mediated by transitions of two surface loops, and on the basis of conservation of mechanism one wo...

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Role of Arg-gingipain A in virulence of Porphyromonas gingivalis.

In order to access the role of the Porphyromonas gingivalis Arg-gingipain proteases in the virulence of this organism, a mutant defective in the rgpA gene was constructed in strain 381. This mutant, MT10, displayed only 40% of the Arg-specific cysteine protease activity of the wild-type strain. In addition, MT10, as well as the recently characterized protease mutant G-102, which is defective in...

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Antibody Responses to Arg-gingipain of Porphyromonas gingivalis in Periodontitis Patients

Arginine-specific cysteine proteinase (Arg-gingipain: Rgp) produced by Porphyromonas gingivalis is a major virulence factor of this periodontal pathogen, which is thought to play an important role in periodontitis by interrupting host defense mechanisms and by participating in the penetration and destruction of host connective tissues. We studied the IgG response against Rgp A components in pat...

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ژورنال

عنوان ژورنال: FEMS Microbiology Letters

سال: 2003

ISSN: 0378-1097,1574-6968

DOI: 10.1016/s0378-1097(03)00178-2