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Infection and Immunity, July 2005, p. 3971-3982, Vol. 73, No. 7
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.7.3971-3982.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Inactivation of vimF, a Putative Glycosyltransferase Gene Downstream of vimE, Alters Glycosylation and Activation of the Gingipains in Porphyromonas gingivalis W83

Elaine Vanterpool,* Francis Roy, and Hansel M. Fletcher

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

Received 15 September 2004/ Returned for modification 11 January 2005/ Accepted 16 February 2005

Regulation/activation of the Porphyromonas gingivalis gingipains is poorly understood. A 1.2-kb open reading frame, a putative glycosyltransferase, downstream of vimE, was cloned, insertionally inactivated using the ermF-ermAM antibiotic resistance cassette, and used to create a defective mutant by allelic exchange. In contrast to the wild-type W83 strain, this mutant, designated P. gingivalis FLL95, was nonpigmented and nonhemolytic when plated on Brucella blood agar. Arginine- and lysine-specific gingipain activities were reduced by approximately 97% and 96%, respectively, relative to that of the parent strain. These activities were unaffected by the growth phase, in contrast to the vimA-defective mutant P. gingivalis FLL92. Expression of the rgpA, rgpB, and kgp gingipain genes was unaffected in P. gingivalis FLL95 in comparison to the wild-type strain. In nonactive gingipain extracellular protein fractions, multiple high-molecular-weight proteins immunoreacted with gingipain-specific antibodies. The specific gingipain-associated sugar moiety recognized by monoclonal antibody 1B5 was absent in FLL95. Taken together, these results suggest that the vimE downstream gene, designated vimF (virulence modulating gene F), which is a putative glycosyltransferase group 1, is involved in the regulation of the major virulence factors of P. gingivalis.

* Corresponding author. Mailing address: Department of Biochemistry and Microbiology, Loma Linda University School of Medicine, Loma Linda, CA 92350. Phone: (909) 558-4472. Fax: (909) 558-4035. E-mail: eguiness02x{at}som.llu.edu.

Editor: A. D. O'Brien

Infection and Immunity, July 2005, p. 3971-3982, Vol. 73, No. 7
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.7.3971-3982.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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