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.
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.
Stuart
Amanda D
AD
Division of Virology, Department of Pathology, University of Cambridge, Cambridge CB2 1QP, United Kingdom.
McKee
Thomas A
TA
Williams
Pamela A
PA
Harley
Chris
C
Shen
Shuo
S
Stuart
David I
DI
Brown
T David K
TD
Lea
Susan M
SM
D000818:Animals; D001665:Binding Sites; D018958:CD55 Antigens / Q000378:metabolism*; D002213:Capsid / Q000648:ultrastructure; D036022:Capsid Proteins; D002522:Chlorocebus aethiops; D018360:Crystallography, X-Ray; D029822:Enterovirus B, Human / Q000235:genetics / Q000378:metabolism / Q000472:pathogenicity* / Q000648:ultrastructure*; D019073:HT29 Cells; D006801:Humans; D009154:Mutation; D011991:Receptors, Virus / Q000378:metabolism*; D014709:Vero Cells; D014764:Viral Proteins / Q000648:ultrastructure; D014771:Virion / Q000648:ultrastructure
D018958:CD55 Antigens; D036022:Capsid Proteins; D011991:Receptors, Virus; C065897:VP1 protein, echovirus 11; D014764:Viral Proteins; C074958:echovirus 11 receptor