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Volume 152, Issue 11

VimA is part of the maturation pathway for the major gingipains of W83 Free

Abstract

The authors have shown previously that the gene, which is part of the operon, plays an important role in protease activation in . The gingipain RgpB proenzyme is secreted in the -defective mutant FLL92. An important question that is raised is whether the 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 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 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.

  • Received:
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2006-11-01
2024-04-20
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VimA is part of the maturation pathway for the major gingipains of Porphyromonas gingivalis W83
Microbiology 152, 3383 (2006); https://doi.org/10.1099/mic.0.29146-0
/content/journal/micro/10.1099/mic.0.29146-0
/content/journal/micro/10.1099/mic.0.29146-0
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