Echovirus 1 interaction with the isolated VLA-2 I domain.
The isolated I domain of the integrin VLA-2, produced as a bacterial fusion protein, specifically bound echovirus 1 and prevented virus attachment to cells. These results demonstrate that the receptor structures critical for virus attachment are contained solely within the VLA-2 I domain and that soluble receptor fragments are capable of preventing infection.
King
S L
SL
Laboratory of Infectious Diseases, Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115, USA.
Cunningham
J A
JA
Finberg
R W
RW
Bergelson
J M
JM
D000818:Animals; D000911:Antibodies, Monoclonal; D015703:Antigens, CD / Q000378:metabolism*; D001665:Binding Sites / Q000235:genetics; D029822:Enterovirus B, Human / Q000235:genetics / Q000378:metabolism* / Q000472:pathogenicity; D005982:Glutathione Transferase / Q000235:genetics / Q000378:metabolism; D006367:HeLa Cells; D006801:Humans; D019012:Integrin beta1; D016023:Integrins / Q000378:metabolism*; D011991:Receptors, Virus / Q000235:genetics / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000378:metabolism
D000911:Antibodies, Monoclonal; D015703:Antigens, CD; D019012:Integrin beta1; D016023:Integrins; D011991:Receptors, Virus; D011993:Recombinant Fusion Proteins; D005982:Glutathione Transferase