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Infection and Immunity, November 2001, p. 6731-6737, Vol. 69, No. 11
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.11.6731-6737.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Association of Mitogen-Activated Protein Kinase Pathways with Gingival Epithelial Cell Responses to Porphyromonas gingivalis Infection

Kiyoko Watanabe,1,2 Özlem Yilmaz,1 Simin F. Nakhjiri,1 Carol M. Belton,1 and Richard J. Lamont1,*

Department of Oral Biology, University of Washington, Seattle, Washington 98195,1 and Department of Oral Microbiology, Kanagawa Dental College, Yokosuka, Kanagawa, 238-8580, Japan2

Received 6 June 2001/Returned for modification 3 July 2001/Accepted 3 August 2001

Mitogen-activated protein (MAP) kinase pathways are key factors in host signaling events and can also play important roles in the internalization of pathogenic bacteria by host cells. Porphyromonas gingivalis, a periodontal pathogen, can efficiently invade human gingival epithelial cells (GECs). In this study, we examined the activation of MAP kinase pathways in GECs infected with P. gingivalis. c-Jun N-terminal kinase (JNK) was activated after 5 min of infection with P. gingivalis, whereas noninvasive Streptococcus gordonii did not have a significant effect on JNK activation. In contrast, extracellular signal-regulated kinase (ERK) 1/2 was downregulated in a dose-dependent manner by P. gingivalis, but not by S. gordonii, after a 15-min exposure. Nonmetabolically active P. gingivalis cells were unable to modulate MAP kinase activity. U0126, a specific inhibitor of MEK1/2 (ERK1/2 kinase), and toxin B, a specific inhibitor of Rho family GTPases, had no effect on P. gingivalis invasion. Genistein, a tyrosine protein kinase inhibitor, blocked uptake of P. gingivalis. The transcriptional regulator NF-kappa B was not activated by P. gingivalis. These results suggest that P. gingivalis can selectively target components of the MAP kinase pathways. ERK1/2, while not involved in P. gingivalis invasion of GECs, may be downregulated by internalized P. gingivalis. Activation of JNK is associated with the invasive process of P. gingivalis.

* Corresponding author. Mailing address: Department of Oral Biology, Box 357132, University of Washington, Seattle WA 98195. Phone: (206) 543-5477. Fax: (206) 685-3162. E-mail: lamon{at}u.washington.edu.

Infection and Immunity, November 2001, p. 6731-6737, Vol. 69, No. 11
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.11.6731-6737.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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