Receptors for Treponema pallidum attachment to the surface and matrix proteins of cultured human dermal microvascular endothelial cells

JuHee Lee, Hyun Joo Choi, Jeanne Jung, Mingeol Lee, Jung Bock Lee, Kwanghoon Lee

Research output: Contribution to journalArticle

12 Citations (Scopus)

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 α5. 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.

Original languageEnglish
Pages (from-to)371-378
Number of pages8
JournalYonsei medical journal
Volume44
Issue number3
DOIs
Publication statusPublished - 2003 Jun 30

Fingerprint

Treponema pallidum
Membrane Proteins
Fibronectins
Endothelial Cells
Skin
Integrins
Treponema
Vascular Endothelium
Aspartic Acid
Glycine
Endothelium
Glass
Virulence
Arginine
Proteins

All Science Journal Classification (ASJC) codes

  • Medicine(all)

Cite this

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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 α5. 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.",
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Receptors for Treponema pallidum attachment to the surface and matrix proteins of cultured human dermal microvascular endothelial cells. / Lee, JuHee; Choi, Hyun Joo; Jung, Jeanne; Lee, Mingeol; Lee, Jung Bock; Lee, Kwanghoon.

In: Yonsei medical journal, Vol. 44, No. 3, 30.06.2003, p. 371-378.

Research output: Contribution to journalArticle

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