Receptors for Treponema pallidum Attachment to the Surface and Matrix Proteins of Cultured Human Dermal Microvascular Endothelial Cells.
10.3349/ymj.2003.44.3.371
- Author:
Ju Hee LEE
1
;
Hyun Joo CHOI
;
Jeanne JUNG
;
Min Geol LEE
;
Jung Bock LEE
;
Kwang Hoon LEE
Author Information
1. Department of Dermatology and Cutaneous Biology Research Institute, Yonsei University College of Medicine, 134 Shinchon-dong, Seodaemun-gu, Seoul 120-752, Korea. kwanglee@yumc.yonsei.ac.kr
- Publication Type:Original Article ; Research Support, Non-U.S. Gov't
- Keywords:
T. pallidum;
RGD;
alpha5 integrin
- MeSH:
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
- From:Yonsei Medical Journal
2003;44(3):371-378
- CountryRepublic of Korea
- Language:English
-
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.
