Microbiology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Microbiology 152 (2006), 3383-3389; DOI  10.1099/mic.0.29146-0
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Vanterpool, E.
Right arrow Articles by Fletcher, H. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Vanterpool, E.
Right arrow Articles by Fletcher, H. M.
Agricola
Right arrow Articles by Vanterpool, E.
Right arrow Articles by Fletcher, H. M.
Microbiology 152 (2006), 3383-3389; DOI  10.1099/mic.0.29146-0
© 2006 Society for General Microbiology

VimA is part of the maturation pathway for the major gingipains of Porphyromonas gingivalis W83

E. Vanterpool{dagger}, F. Roy{ddagger}, W. Zhan{ddagger}, S. M. Sheets, L. Sangberg and H. M. Fletcher

Department of Biochemistry and Microbiology, School of Medicine, Loma Linda University, Loma Linda, CA 92350, USA

Correspondence
H. M. Fletcher
hfletcher{at}llu.edu

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.

{dagger}Present address: Department of Biological Sciences, Oakwood College, Huntsville, AL, USA.

{ddagger}Present address: School of Public Health, Tianjin Medical University, China.






HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 2006 Society for General Microbiology.