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Binding of type-I collagen to Chlamydia trachomatis
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.
1994 (English)In: Microbial Pathogenesis, ISSN 0882-4010, E-ISSN 1096-1208, Vol. 17, no 4, 253-259 p.Article in journal (Refereed) Published
Abstract [en]

Denatured type-I collagen was found to bind to Chlamydia trachomatis elementary bodies (EBs) in a time-dependent and specific manner. Specificity was tested by having a large excess of other proteins present in the binding mixture. Only denatured type-I collagen efficiently competed for binding. Radiolabelled fibronectin did not bind under the test conditions used. The binding was temperature-dependent and the interaction increased at the melting temperature of the collagen. Evidence was found for two binding sites: one with high affinity (Kd 3.3 x 10(-9)) and one with low affinity (Kd 1.7 x 10(-7)), with an estimated number of binding sites per EB of 590 and 2900, respectively. The interaction between C. trachomatis and collagen may also be relevant in vivo, since 50% binding occurred at 37 degrees C. The binding to denatured collagen may be of importance for the development of sexually acquired reactive arthritis.

Place, publisher, year, edition, pages
1994. Vol. 17, no 4, 253-259 p.
National Category
Infectious Medicine
Identifiers
URN: urn:nbn:se:uu:diva-302053DOI: 10.1006/mpat.1994.1070PubMedID: 7715423OAI: oai:DiVA.org:uu-302053DiVA: diva2:956154
Available from: 2016-08-29 Created: 2016-08-29 Last updated: 2016-09-16Bibliographically approved

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