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Structural Basis of Oligosaccharide Receptor Recognition by Human Papillomavirus

The Journal of biological chemistry, 2011-01, Vol.286 (4), p.2617-2624 [Peer Reviewed Journal]

2011 © 2011 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;2011 by The American Society for Biochemistry and Molecular Biology, Inc. ;ISSN: 0021-9258 ;ISSN: 1083-351X ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M110.160184 ;PMID: 21115492

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Title:
Structural Basis of Oligosaccharide Receptor Recognition by Human Papillomavirus
Author: Dasgupta, Jhimli ; Bienkowska-Haba, Malgorzata ; Ortega, Marcos E. ; Patel, Hetalkumar D. ; Bodevin, Sabrina ; Spillmann, Dorothe ; Bishop, Brooke ; Sapp, Martin ; Chen, Xiaojiang S.
Subjects: Binding Sites ; Cell-surface Receptor ; Crystallography, X-Ray ; DNA Viruses ; Heparitin Sulfate - chemistry ; Heparitin Sulfate - genetics ; Heparitin Sulfate - metabolism ; Human papillomavirus ; Human papillomavirus 16 ; Human papillomavirus 16 - chemistry ; Human papillomavirus 16 - genetics ; Human papillomavirus 16 - metabolism ; Human papillomavirus 18 ; Human papillomavirus 18 - chemistry ; Human papillomavirus 18 - genetics ; Human papillomavirus 18 - metabolism ; Humans ; MEDICIN ; MEDICINE ; Microbiology ; Papillomavirus Infections - genetics ; Papillomavirus Infections - metabolism ; Structure-Activity Relationship ; Tumor Viruses ; Virus ; Virus Entry
Is Part Of: The Journal of biological chemistry, 2011-01, Vol.286 (4), p.2617-2624
Description: 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.
Publisher: United States: Elsevier Inc
Language: English
Identifier: ISSN: 0021-9258
ISSN: 1083-351X
EISSN: 1083-351X
DOI: 10.1074/jbc.M110.160184
PMID: 21115492
Source: Open Access: PubMed Central
MEDLINE
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Structural Basis of Oligosaccharide Receptor Recognition by Human Papillomavirus

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