Foamy virus particle formation

被引:94
作者
Fischer, N
Heinkelein, M
Lindemann, D
Enssle, J
Baum, C
Werder, E
Zentgraf, H
Müller, JG
Rethwilm, A
机构
[1] Univ Wurzburg, Inst Virol & Immunbiol, D-97078 Wurzburg, Germany
[2] Univ Wurzburg, Inst Pathol, D-97078 Wurzburg, Germany
[3] Univ Hamburg, Heinrich Pette Inst Expt Virol & Immunol, D-2000 Hamburg, Germany
[4] Deutsch Krebsforschungszentrum, D-6900 Heidelberg, Germany
关键词
D O I
10.1128/JVI.72.2.1610-1615.1998
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Subgenomic expression plasmids for the so-called human foamy, virus (HFV) structural gag, gag/pol, and env genes were constructed and used to analyze foamy virus particle formation by electron microscopy. Expression of an R-US-gag-pol construct under control of the human cytomegalovirus immediate-early enhancer-promoter resulted in the formation of viral cores with a homogeneous size of approximately 50 nm located in the cytoplasm. Upon coexpression of an envelope construct, particles were observed budding into cytoplasmic vesicles and from the plasma membrane, Expression of the Gag protein precursor pr74 alone led to aberrantly formed viral particles of heterogeneous size and with open cores, Normal-shaped cores were seen after transfection of a construct expressing the p70(gag) cleavage product, indicating that p70(gag) is able to assemble into capsids, Coexpression of p70(gag) and Env resulted in budding virions, ruling out a requirement of the reverse transcriptase for capsid or virion formation, In sharp contrast to other retroviruses, the HFV cores did not spontaneously bud from cellular membranes. Radiochemical labeling followed by protein gel electrophoresis also revealed the intracellular retention of Env-deprived HFV capsids.
引用
收藏
页码:1610 / 1615
页数:6
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