VimA is part of the maturation pathway for the major gingipains of Porphyromonas gingivalis W83.
The authors have shown previously that the vimA gene, which is part of the bcp-recA-vimA operon, plays an important role in protease activation in Porphyromonas gingivalis. The gingipain RgpB proenzyme is secreted in the vimA-defective mutant P. gingivalis FLL92. An important question that is raised is whether the vimA gene product could directly interact with the proteases for their activation or regulate a pathway responsible for protease activation. To further study the mechanism(s) of VimA-dependent protease activation, the vimA gene product was further characterized. A 39 kDa protein consistent with the size of the predicted VimA protein was purified. In protein-protein interaction studies, the VimA protein was shown to interact with gingipains RgpA, RgpB and Kgp. Immune sera from mice immunized with P. gingivalis immunoreacted with the purified VimA protein. Taken together, these data suggest an interaction of VimA with the gingipains and further confirm the role of this protein in their regulation or maturation.
Vanterpool
E
E
Department of Biochemistry and Microbiology, School of Medicine, Loma Linda University, Loma Linda, CA 92350, USA.
Roy
F
F
Department of Biochemistry and Microbiology, School of Medicine, Loma Linda University, Loma Linda, CA 92350, USA.
Zhan
W
W
Department of Biochemistry and Microbiology, School of Medicine, Loma Linda University, Loma Linda, CA 92350, USA.
Sheets
S M
SM
Department of Biochemistry and Microbiology, School of Medicine, Loma Linda University, Loma Linda, CA 92350, USA.
Sangberg
L
L
Department of Biochemistry and Microbiology, School of Medicine, Loma Linda University, Loma Linda, CA 92350, USA.
Fletcher
H M
HM
Department of Biochemistry and Microbiology, School of Medicine, Loma Linda University, Loma Linda, CA 92350, USA.
D018829:Adhesins, Bacterial / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D000918:Antibody Specificity; D001057:Apolipoproteins E / Q000172:deficiency / Q000235:genetics; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000502:physiology*; D016866:Bacteroidaceae Infections / Q000276:immunology; D003546:Cysteine Endopeptidases / Q000235:genetics / Q000378:metabolism*; D004789:Enzyme Activation; D004792:Enzyme Precursors / Q000235:genetics / Q000378:metabolism*; D005260:Female; D015964:Gene Expression Regulation, Bacterial; D005798:Genes, Bacterial; D000080867:Gingipain Cysteine Endopeptidases; D006388:Hemagglutinins / Q000235:genetics / Q000378:metabolism*; D007106:Immune Sera / Q000276:immunology; D007114:Immunization; D008297:Male; D051379:Mice; D008810:Mice, Inbred C57BL; D008815:Mice, Inbred Strains; D008970:Molecular Weight; D009154:Mutation; D009876:Operon; D016966:Porphyromonas gingivalis / Q000201:enzymology* / Q000276:immunology / Q000472:pathogenicity; D011485:Protein Binding; D014774:Virulence / Q000235:genetics*
D018829:Adhesins, Bacterial; D001057:Apolipoproteins E; D001425:Bacterial Outer Membrane Proteins; D004792:Enzyme Precursors; D000080867:Gingipain Cysteine Endopeptidases; D006388:Hemagglutinins; D007106:Immune Sera; D003546:Cysteine Endopeptidases