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J Gen Virol 71 (1990), 1947-1955; DOI 10.1099/0022-1317-71-9-1947
© 1990 Society for General Microbiology
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Fusion of simian immunodeficiency virus with liposomes and erythrocyte ghost membranes: effects of lipid composition, pH and calcium

Charles E. Larsen1, Dennis R. Alford1,{dagger}, Lawrence J. T. Young3,{ddagger}>, Thomas P. McGraw3 and Nejat Düzgünes1,2,

1 Cancer Research Institute
and2 Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94143
and3 California Primate Research Center, University of California, Davis, California 95616, U.S.A.

Simian immunodeficiency virus from macaques (SIVmac) is closely related in its structure and biological activity to human immunodeficiency virus, and is the best animal model for the acquired immunodeficiency syndrome. We investigated the kinetics of membrane fusion between SIVmac and phospholipid vesicles and the effects of various parameters on this process. Purified SIVmac was labelled with octadecyl rhodamine B chloride, and fusion was continuously monitored as the dilution of the probe in target membranes. These studies show that SIVmac fusion is strongly dependent upon the liposome composition. Fusion with pure cardiolipin (CL) liposomes is significantly faster than with CL/dioleoylphosphatidylcholine (DOPC) (3:7), phosphatidylserine (PS) or disialoganglioside (GD1a)/DOPC (1.5:8.5) vesicles. SIVmac does not fuse appreciably with pure DOPC liposomes. Reduction of pH from 7.5 to 4.5 greatly enhances the rate of SIVmac fusion with CL, CL/DOPC and PS membranes, but does not affect fusion with DOPC or GD1a/DOPC membranes. Calcium stimulates viral fusion with CL liposomes, but not with CL/DOPC or DOPC liposomes. SIVmac fuses with human erythrocyte ghost membranes only slowly at reduced pH. Our results indicate that SIVmac can fuse with membranes lacking the known viral receptor, CD4. Although the mechanism of SIVmac fusion with model and biological membranes remains to be determined, the fusion activity of SIVmac shares similarities with other lipid-enveloped viruses such as Sendai and influenza viruses.

{dagger} Present address: Department of Bioscience and Biotechnology, Drexel University, Philadelphia, Pennsylvania 19104, U.S.A.

{ddagger}> Present address: Department of Pathology, University of California, Davis Medical Centre, Sacramento, California 95817, U.S.A.

Received 8 February 1990; accepted 22 May 1990.




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