TY - JOUR
T1 - Sendai virus envelope glycoproteins become laterally mobile on the surface of human erythrocytes following fusion
AU - Henis, Yoav I.
AU - Gutman, Orit
AU - Loyter, Abraham
N1 - Funding Information:
Y. I. H. is a recipient of the Bat-Sheva de Rotschild Fellowship. This research was supported by grants from The Fund for Basic Research (administeredb y The Israel Academy of Sciences and Humanities) and from the United States-Israel Binational Science Foundation (BSF, Jerusalem, Israel; grant No. 3149/84t)o Y. I. H.
PY - 1985/10
Y1 - 1985/10
N2 - Fluorescence photobleaching recovery has been employed to study the lateral mobility of the Sendai virus envelope glycoproteins (HN, neuraminidase/hemagglutinin protein (HN) fusion protein (F)) on the surface of human erythrocytes. Our results indicate that the two viral glycoproteins are laterally immobile on the cell surface prior to fusion, and become mobile during the fusion process. The two fused glycoproteins are mobilized to the same extent (diffusion coefficients of 3.1-3.3 × 10-10 cm2/sec with mobile fractions of 53-57 for both HN and F). Their mobilization is blocked under conditions that allow virus adsorption and hemagglutination, but not virus-cell or cell-cell fusion. These findings suggest a possible role for the lateral diffusion of the viral glycoproteins in the mechanism of cell-cell fusion, enabling them to perturb the membranes of adjacent cells and lead to cell-cell fusion.
AB - Fluorescence photobleaching recovery has been employed to study the lateral mobility of the Sendai virus envelope glycoproteins (HN, neuraminidase/hemagglutinin protein (HN) fusion protein (F)) on the surface of human erythrocytes. Our results indicate that the two viral glycoproteins are laterally immobile on the cell surface prior to fusion, and become mobile during the fusion process. The two fused glycoproteins are mobilized to the same extent (diffusion coefficients of 3.1-3.3 × 10-10 cm2/sec with mobile fractions of 53-57 for both HN and F). Their mobilization is blocked under conditions that allow virus adsorption and hemagglutination, but not virus-cell or cell-cell fusion. These findings suggest a possible role for the lateral diffusion of the viral glycoproteins in the mechanism of cell-cell fusion, enabling them to perturb the membranes of adjacent cells and lead to cell-cell fusion.
UR - http://www.scopus.com/inward/record.url?scp=0022178999&partnerID=8YFLogxK
U2 - 10.1016/0014-4827(85)90198-3
DO - 10.1016/0014-4827(85)90198-3
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AN - SCOPUS:0022178999
SN - 0014-4827
VL - 160
SP - 514
EP - 526
JO - Experimental Cell Research
JF - Experimental Cell Research
IS - 2
ER -