Yonsei Med J.  2003 Jun;44(3):371-378. 10.3349/ymj.2003.44.3.371.

Receptors for Treponema pallidum Attachment to the Surface and Matrix Proteins of Cultured Human Dermal Microvascular Endothelial Cells

• Lee JH
• Choi HJ
• Jung J
• Lee MG
• Lee JB
• Lee KH

• KMID: 720865
• DOI: http://doi.org/10.3349/ymj.2003.44.3.371

Abstract

Pathogenicity of Treponema pallidum may depend upon the binding of Treponema pallidum to matrix proteins, especially to fibronectin. Infectious organism or cell to matrix interactions are mediated by a family of adhesion molecule receptors known as integrins. Once in the host, the pathogenic Treponema pallidumdum adheres to the vascular endothelium and readily penetrates surrounding tissues. Fibronectin plays an important role in the mediation of the attachment of Treponema pallidum to host cells, including endothelial cells. We found that the binding of Treponema pallidum to human dermal microvascular endothelial cells and to a glass surface coated with fibronectin is inhibited by the presence of arginine-glycine- aspartic acid (RGD), and analysis of the surface receptor revealed an antigenic similarity to an integrin molecule, namely alpha5. This ability to adhere to host endothelium and fibronectin is quite unique to T. pallidum among the treponemes, and may be a key pathogenic factor.

Keyword

T. pallidum; RGD; alpha5 integrin

MeSH Terms

Carrier Proteins/*physiology
Cell Membrane/metabolism
Cells, Cultured
Endothelium, Vascular/cytology/*metabolism
Extracellular Matrix Proteins/*metabolism
Human
Microcirculation
Skin/*blood supply
Support, Non-U.S. Gov't
Treponema pallidum/*physiology