Membrane fusion promoted by increasing surface densities of the paramyxovirus F and HN proteins: Comparison of fusion reactions mediated by simian virus 5 F, human parainfluenza virus type 3 F, and influenza virus HA

Membrane fusion promoted by increasing surface densities of the paramyxovirus F and HN proteins: Comparison of fusion reactions mediated by simian virus 5 F, human parainfluenza virus type 3 F, and influenza virus HA
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DOI:
10.1128/jvi.72.10.7745-7753.1998
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发表时间:
1998-10-01
影响因子:
5.4
通讯作者:
Lamb, RA
Lamb, RA
中科院分区:
医学2区
文献类型:
--
作者:
Dutch, RE;Joshi, SB;Lamb, RA

文献摘要

被引文献

相似文献

当F和HN的表面密度变化时,表征了由副粘病毒猿猴病毒5(SV 5)和人副流感病毒3型(HPN-3)融合(F)蛋白和血凝素-神经氨酸酶(HN)蛋白促进的膜融合反应。使用定量内容物混合测定,发现SV 5 F介导的融合的程度依赖于SV 5 F蛋白的表面密度,但不依赖于SV 5 HN蛋白的密度,表明HN在反应中仅起结合作用。然而,发现HPIV-3F蛋白促进融合反应的程度依赖于HPIV-3 HN蛋白的表面密度,表明HPIV-3 HN蛋白是融合反应的直接参与者。脂质混合的动力学分析表明,融合的初始速率和最终程度都随着SV 5 F蛋白表面密度的增加而增加,这表明在SV 5 F蛋白促进的膜融合期间,多个融合孔可以是活跃的。脂质混合的初始速率和程度也被发现随着流感病毒血凝素蛋白表面密度的增加而增加,这表明这两种病毒融合蛋白促进的融合机制之间存在相似之处。
The membrane fusion reaction promoted by the paramyxovirus simian virus 5 (SV5) and human parainfluenza virus type 3 (HPN-3) fusion (F) proteins and hemagglutinin-neuraminidase (HN) proteins was characterized when the surface densities of F and HN were varied. Using a quantitative content mixing assay, it was found that the extent of SV5 F-mediated fusion was dependent on the surface density of the SV5 F protein but independent of the density of SV5 HN protein, indicating that HN serves only a binding function in the reaction. However, the extent of HPIV-3 F protein promoted fusion reaction was found to be dependent on surface density of HPIV-3 HN protein, suggesting that the HPIV-3 HN protein is a direct participant in the fusion reaction. Analysis of the kinetics of lipid mixing demonstrated that both initial rates and final extents of fusion increased with rising SV5 F protein surface densities, suggesting that multiple fusion pores can be active during SV5 F protein-promoted membrane fusion. Initial rates and extent of lipid mixing were also found to increase with increasing influenza virus hemagglutinin protein surface density, suggesting parallels between the mechanism of fusion promoted by these two viral fusion proteins.