Involvement of lipids in the interaction of Sindbis virus with goose erythrocytes.
The chemical nature of Sindbis virus receptors on goose erythrocytes was investigated by means of two different experimental approaches: by testing the capacity of human serum lipoproteins (HDL, LDL, VLDL) to compete with erythrocytes for virus binding and by enzymatic and chemical modifications of the cell membrane. Each class of lipoproteins was separated into its protein and lipid components which were tested for hemagglutination and hemolysis inhibiting activity. Only the lipid moieties were able to inhibit binding and fusion activities of the virus. Enzymatic treatments of the erythrocyte surface showed that sialic acid and trypsin-sensitive proteins were not involved in Sindbis virus membrane receptor and that some phospholipids probably represent important components of the cellular binding site.
Mastromarino
P
P
Institute of Microbiology, School of Medicine, University of Rome La Sapienza, Italy.
Conti
C
C
Rieti
S
S
Orsi
N
N
D000818:Animals; D001667:Binding, Competitive; D004912:Erythrocytes / Q000378:metabolism*; D005260:Female; D005777:Geese / Q000097:blood; D006385:Hemagglutination Inhibition Tests; D006387:Hemagglutination, Viral; D006461:Hemolysis; D006801:Humans; D050356:Lipid Metabolism; D008055:Lipids / Q000032:analysis; D008074:Lipoproteins / Q000032:analysis / Q000378:metabolism*; D008297:Male; D011991:Receptors, Virus / Q000032:analysis*; D012845:Sindbis Virus / Q000378:metabolism*
D008055:Lipids; D008074:Lipoproteins; D011991:Receptors, Virus