Integrin-Using Rotaviruses Bind α2β1 Integrin α2 I Domain via VP4 DGE Sequence and Recognize αXβ2 and αVβ3 by Using VP7 during Cell Entry
0301 basic medicine
03 medical and health sciences
3. Good health
DOI:
10.1128/jvi.77.18.9969-9978.2003
Publication Date:
2003-08-26T22:54:06Z
AUTHORS (8)
ABSTRACT
Integrins alpha2beta1, alphaXbeta2, and alphaVbeta3 have been implicated in rotavirus cell attachment entry. The virus spike protein VP4 contains the alpha2beta1 ligand sequence DGE at amino acid positions 308 to 310, outer capsid VP7 alphaXbeta2 GPR. To determine viral proteins sequences involved define roles of alphaVbeta3, we analyzed ability rotaviruses their reassortants use these integrins for binding infection effect peptides DGEA GPRP on events. Many laboratory-adapted human, monkey, bovine viruses used integrins, whereas all porcine were integrin independent. integrin-using strains each interacted with three integrins. Integrin usage related serotype independently sialic usage. Analysis assays infectivity integrin-transfected cells showed that bound a postbinding stage. inhibited infectivity, but not binding. truncated VP5* subunit VP4, expressed as glutathione S-transferase fusion protein, alpha2 I domain. Alanine mutagenesis D308 G309 eliminated In novel process, bind domain via interact (via GPR) by using facilitate entry infection.
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