Determination of the Structure of a Decay Accelerating Factor-Binding Clinical Isolate of Echovirus 11 Allows Mapping of Mutants with Altered Receptor Requirements for Infection
| Autor: | T. D. K. Brown, David I. Stuart, Susan M. Lea, Pamela A. Williams, T. A. McKee, C. Harley, Shuo Shen, Amanda D. Stuart |
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| Rok vydání: | 2002 |
| Předmět: |
Echovirus
viruses Immunology Mutant Biology Crystallography X-Ray medicine.disease_cause Microbiology Viral Proteins Capsid Virology Chlorocebus aethiops medicine Animals Humans Binding site Receptor Vero Cells Decay-accelerating factor chemistry.chemical_classification Mutation Binding Sites CD55 Antigens Virion biochemical phenomena metabolism and nutrition Molecular biology Enterovirus B Human Virus-Cell Interactions Amino acid Cell biology chemistry Insect Science Receptors Virus Capsid Proteins HT29 Cells |
| Zdroj: | Journal of Virology. 76:7694-7704 |
| ISSN: | 1098-5514 0022-538X |
| DOI: | 10.1128/jvi.76.15.7694-7704.2002 |
| Popis: | We have used X-ray crystallography to determine the structure of a decay accelerating factor (DAF)-binding, clinic-derived isolate of echovirus 11 (EV11-207). The structures of the capsid proteins closely resemble those of capsid proteins of other picornaviruses. The structure allows us to interpret a series of amino acid changes produced by passaging EV11-207 in different cell lines as highlighting the locations of multiple receptor-binding sites on the virion surface. We suggest that a DAF-binding site is located at the fivefold axes of the virion, while the binding site for a distinct but as yet unidentified receptor is located within the canyon surrounding the virion fivefold axes. |
| Databáze: | OpenAIRE |
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