TY - JOUR
T1 - La Crosse virus G1 glycoprotein undergoes a conformational change at the pH of fusion
AU - Gonzalez-Scarano, Francisco
N1 - Funding Information:
Supported in part by USPHS Grant NS 29994 and US RDC contract 17-82-C2994. The author is supported by Teacher Investigator Award NS 9971’7 and a Harry Weaver Neuroscience Fellowship from the National Multiple Sclerosis Society. I appreciate the helpful suggestions provided by Neal Nathanson, John Skehel, and Jon Gentsch.
PY - 1985/1/30
Y1 - 1985/1/30
N2 - La Crosse virus, a member of the family Bunyaviridae, can mediate cell-to-cell fusion after mild acidification. Either of its two envelope glycoproteins could potentially be responsible for this function. The large glycoprotein (Gl) undergoes a conformational change at the pH of activation of the fusion function, resulting in both an alteration in the cleavage pattern produced by amino-acid-specific proteases, and in a change in its antigenicity, as defined by altered binding of monoclonal antibodies.
AB - La Crosse virus, a member of the family Bunyaviridae, can mediate cell-to-cell fusion after mild acidification. Either of its two envelope glycoproteins could potentially be responsible for this function. The large glycoprotein (Gl) undergoes a conformational change at the pH of activation of the fusion function, resulting in both an alteration in the cleavage pattern produced by amino-acid-specific proteases, and in a change in its antigenicity, as defined by altered binding of monoclonal antibodies.
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U2 - 10.1016/0042-6822(85)90359-9
DO - 10.1016/0042-6822(85)90359-9
M3 - Article
C2 - 3881876
AN - SCOPUS:0021932202
SN - 0042-6822
VL - 140
SP - 209
EP - 216
JO - Virology
JF - Virology
IS - 2
ER -