J Bacteriol Virol.  2002 Mar;32(1):47-54.

Functional Characterization of the Major Outer Membrane Protein ( MspTL ) of Treponema lecithinolyticum

Affiliations
  • 1Department of Periodontology, Yonsei University College of Dentistry, Yonsei University, Seoul, Korea.
  • 2Department of Oral Biology, Yonsei University College of Dentistry, Yonsei University, Seoul, Korea. ohisto@yumc.yonsei.ac.kr
  • 3Brain Korea 21 Project of Medical Sciences, Yonsei University, Seoul, Korea.

Abstract

Treponema lecithinolyticum is known to be associated with rapidly progressive periodontitis. The full-length gene encoding the major surface protein MspTL of this organism was cloned and expressed by using the expression vector pQE30. Recombinant Msp TL (rMsp TL) protein was purified and functionally characterized. Msp TL was one of several T. lecithinolyticum surface proteins that bound to cultured human gingival fibroblasts (HGFs). As well, it strongly induced IL-6 production by HGFs. These observations suggest that MspTL contributes to pathogenesis of periodontitis by adhesion to host cells and by induction of the proinflammatory cytokine IL-6.

Keyword

Periodontitis; Treponema lecithinolyticum; Major surface protein

MeSH Terms

Clone Cells
Fibroblasts
Humans
Interleukin-6
Membrane Proteins*
Membranes*
Periodontitis
Treponema*
Interleukin-6
Membrane Proteins
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