Analysis of the cell fusion activities of chimeric simian immunodeficiency virus murine leukemia virus envelope proteins: Inhibitory effects of the R peptide

被引:51
作者
Yang, CL
Compans, RW
机构
[1] EMORY UNIV,SCH MED,DEPT MICROBIOL & IMMUNOL,ATLANTA,GA 30322
[2] UNIV ALABAMA,DEPT BIOCHEM & MOLEC GENET,BIRMINGHAM,AL 35294
关键词
D O I
10.1128/JVI.70.1.248-254.1996
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
It was previously reported that truncation or proteolytic removal of the C-terminal 16 amino acids (the R peptide) from the cytoplasmic tail of the murine leukemia virus (MuLV) envelope protein greatly increases its fusion activity, In this study, to investigate the specificity of the effect of the R peptide on the fusion activity of viral envelope proteins, we expressed simian immunodeficiency virus (SN)-MuLV chimeric proteins in which the entire cytoplasmic tail of the SIV envelope protein was replaced by either the full-length MuLV cytoplasmic tail or a truncated MuLV cytoplasmic tail with the R peptide deleted. Extensive fusion of CD4-positive cells with the chimeric protein containing a truncated MuLV cytoplasmic tail was observed. In contrast, no cell fusion activity was found for the chimeric protein,vith a full-length MuLV cytoplasmic tail. We constructed another SIV-MuLV chimeric protein in which the MuLV R peptide was added to an SIV envelope protein cytoplasmic tail 17 amino acids from its membrane-spanning domain. No fusion activity was observed within this construct, while the corresponding truncated SIV envelope protein lacking the R peptide showed extensive fusion activity, No significant difference in the transport or surface expression was observed among the various SIV-MuLV chimeric proteins and the truncated SN envelope protein. Our results thus demonstrate that the MuLV R peptide has profound inhibitory effects on virus-induced cell fusion, not only with MuLV but also in a distantly related retroviral envelope protein which utilizes a different receptor and fuses different cell types.
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页码:248 / 254
页数:7
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