Porphyromonas gingivalis RgpA and Kgp Proteinases and Adhesins Are C Terminally Processed by the Carboxypeptidase CPG70
AUTOR(ES)
Veith, Paul D.
FONTE
American Society for Microbiology
RESUMO
Porphyromonas gingivalis is a bacterial pathogen that produces the polyproteins RgpA and Kgp, which are proteolytically processed into proteinases and adhesins. We have demonstrated that the RgpA and Kgp proteinases and adhesins are C terminally processed by carboxypeptidase CPG70 by sequencing C-terminal peptides from both the wild type and an isogenic CPG70 mutant, using ion trap mass spectrometry.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=415657Documentos Relacionados
- Role of RgpA, RgpB, and Kgp Proteinases in Virulence of Porphyromonas gingivalis W50 in a Murine Lesion Model
- Variable Carbohydrate Modifications to the Catalytic Chains of the RgpA and RgpB Proteases of Porphyromonas gingivalis W50
- RgpA-Kgp Peptide-Based Immunogens Provide Protection against Porphyromonas gingivalis Challenge in a Murine Lesion Model
- Immunization with the RgpA-Kgp Proteinase-Adhesin Complexes of Porphyromonas gingivalis Protects against Periodontal Bone Loss in the Rat Periodontitis Model
- Serum Immunoglobulin G (IgG) and IgG Subclass Responses to the RgpA-Kgp Proteinase-Adhesin Complex of Porphyromonas gingivalis in Adult Periodontitis