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副粘病毒猿猴病毒5融合蛋白胞质尾的缺失影响融合孔的扩大。

Deletion of the cytoplasmic tail of the fusion protein of the paramyxovirus simian virus 5 affects fusion pore enlargement.

作者信息

Dutch R E, Lamb R A

机构信息

Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 60208-3500, USA.

出版信息

J Virol. 2001 Jun;75(11):5363-9. doi: 10.1128/JVI.75.11.5363-5369.2001.

Abstract

The fusion (F) protein of the paramxyovirus simian parainfluenza virus 5 (SV5) promotes virus-cell and cell-cell membrane fusion. Previous work had indicated that removal of the SV5 F protein cytoplasmic tail (F Tail- or FDelta19) caused a block in fusion promotion at the hemifusion stage. Further examination has shown that although the F Tail- mutant is severely debilitated in promotion of fusion as measured by using two reporter gene assays and is debilitated in the formation of syncytia relative to the wild-type F protein, the F Tail- mutant is capable of promoting the transfer of small aqueous dyes. These data indicate that F Tail- is fully capable of promoting formation of small fusion pores. However, enlargement of fusion pores is debilitated, suggesting that either the cytoplasmic tail of the F protein plays a direct role in pore expansion or that it interacts with other components which control pore growth.

摘要

副粘病毒猴副流感病毒5(SV5)的融合(F)蛋白可促进病毒-细胞和细胞-细胞膜融合。先前的研究表明,去除SV5 F蛋白的细胞质尾巴(F Tail-或FDelta19)会导致在半融合阶段促进融合的过程受阻。进一步研究表明,尽管通过两种报告基因检测法测量,F Tail-突变体在促进融合方面严重受损,并且相对于野生型F蛋白,其在多核体形成方面也受损,但F Tail-突变体仍能够促进小水性染料的转移。这些数据表明,F Tail-完全能够促进小融合孔的形成。然而,融合孔的扩大受到损害,这表明要么F蛋白的细胞质尾巴在孔扩张中起直接作用,要么它与控制孔生长的其他成分相互作用。

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本文引用的文献

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