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Structural Basis of Oligosaccharide Receptor Recognition by Human Papillomavirus
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2011 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 286, no 4, 2617-2624 p.Article in journal (Refereed) Published
Abstract [en]

High risk human papillomavirus types 16 (HPV16) and 18 (HPV18) can cause cervical cancer. Efficient infection by HPV16 and HPV18 pseudovirions requires interactions of particles with cell-surface receptor heparan sulfate oligosaccharide. To understand the virus-receptor interactions for HPV infection, we determined the crystal structures of HPV16 and HPV18 capsids bound to the oligosaccharide receptor fragment using oligomeric heparin. The HPV-heparin structures revealed multiple binding sites for the highly negatively charged oligosaccharide fragment on the capsid surface, which is different from previously reported virus-receptor interactions in which a single type of binding pocket is present for a particular receptor. We performed structure-guided mutagenesis to generate mutant viruses, and cell binding and infectivity assays demonstrated the functional role of viral residues involved in heparin binding. These results provide a basis for understanding virus-heparan sulfate receptor interactions critical for HPV infection and for the potential development of inhibitors against HPV infection.

Place, publisher, year, edition, pages
2011. Vol. 286, no 4, 2617-2624 p.
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Medical and Health Sciences
URN: urn:nbn:se:uu:diva-148608DOI: 10.1074/jbc.M110.160184ISI: 000286464300027PubMedID: 21115492OAI: oai:DiVA.org:uu-148608DiVA: diva2:402486
Available from: 2011-03-08 Created: 2011-03-08 Last updated: 2011-06-28Bibliographically approved

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Spillmann, Dorothe
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Department of Medical Biochemistry and Microbiology
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