Determination of the structure of a decay accelerating factor-binding clinical isolate of echovirus 11 allows mapping of mutants with altered receptor requirements for infection1
Détails
ID Serval
serval:BIB_B27201027F3C
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Determination of the structure of a decay accelerating factor-binding clinical isolate of echovirus 11 allows mapping of mutants with altered receptor requirements for infection1
Périodique
Journal of Virology
ISSN
0022-538X (Print)
Statut éditorial
Publié
Date de publication
2002
Volume
76
Numéro
15
Pages
7694-7704
Notes
PT - Journal Article PT - Research Support, Non-U.S. Gov't
Résumé
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
Mots-clé
Animals/Antigens,CD55/metabolism/Binding Sites/Capsid/ultrastructure/Capsid Proteins/Cercopithecus aethiops/Crystallography,X-Ray/Enterovirus B,Human/genetics/pathogenicity/HT29 Cells/Humans/Mutation/Receptors,Virus/Vero Cells/Viral Proteins/Virion/Research
Pubmed
Web of science
Création de la notice
29/01/2008 19:34
Dernière modification de la notice
20/08/2019 16:21