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Infection and Immunity, October 1998, p. 4777-4782, Vol. 66, No. 10
Department of Oral Biology, School of
Dentistry, University of Washington, Seattle, Washington 98195
Received 11 March 1998/Returned for modification 11 June
1998/Accepted 17 July 1998
Porphyromonas gingivalis can induce its uptake by host
epithelial cells; however, the nature and role of the P. gingivalis molecules involved in this invasion process have yet
to be determined. In this study, modulation of secreted P. gingivalis proteins following association with gingival
epithelial cells was investigated. Western immunoblot analysis showed
that contact with epithelial cells or epithelial cell growth media
induces P. gingivalis 33277 to secrete several proteins
with molecular masses between 35 and 95 kDa. Secretion of the
Arg-gingipain and Lys-gingipain proteases was repressed under these
conditions. The contact-induced secreted protein profile was altered in
Arg-gingipain-deficient and Lys-gingipain-deficient mutants, indicating
a possible role for these proteases in the secretion pathway. The
P. gingivalis contact-dependent protein secretion pathway
differs to some extent from type III protein secretion pathways in
enteric pathogens, as a gene homologous to the invA family
genes was not detected in P. gingivalis. The secreted
proteins of P. gingivalis may play a role in the
interactions of the organism with host cells.
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Contact-Dependent Protein Secretion in
Porphyromonas gingivalis
*
Corresponding author. Mailing address: Department of
Oral Biology, University of Washington, Box 357132, Seattle, WA
98195. Phone: (206) 543-5477. Fax: (206) 685-3162. E-mail:
lamon{at}u.washington.edu.
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