Influenza virus hemagglutinin and neuraminidase glycoproteins stimulate the membrane association of the matrix protein
Influenza virus hemagglutinin and neuraminidase glycoproteins stimulate the membrane association of the matrix protein
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DOI：
10.1128/jvi.70.10.6653-6657.1996
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发表时间：
1996-10-01
影响因子：
5.4
通讯作者：
Enami, K
中科院分区：
文献类型：
--
作者：
Enami, M;Enami, K
我们分析了在甲型流感病毒装配过程中基质（M1）蛋白与细胞膜结合的机制，通过使用野生型和转染流感病毒以及表达M1蛋白、HA或NA的重组牛痘病毒，广泛分析了M1蛋白与病毒血凝素（HA）和神经氨酸酶（NA）糖蛋白的相互作用。M1蛋白的膜结合在病毒感染的后期被显著刺激。使用重组牛痘病毒，我们发现在没有其他病毒蛋白的情况下，相对小部分（20 - 40%）的细胞质M1蛋白与细胞膜结合，而HA和NA的共表达刺激M1蛋白的膜结合，NA的刺激作用（>90%）是显著的并且高于HA的刺激作用（>60%）。同时，HA可以补充NA的缺陷，促进NA/TAIL（-）转染细胞中病毒的组装。总之，HA和NA的高度保守的胞质尾在病毒组装中起重要作用。
We have analyzed the mechanism by which the matrix (M1) protein associates with cellular membranes during influenza A virus assembly, Interaction of the M1 protein with the viral hemagglutinin (HA) br neuraminidase (NA) glycoprotein was extensively analyzed by using wild-type and transfectant influenza viruses as well as recombinant vaccinia viruses expressing the M1 protein, HA, or NA. Membrane binding of the M1 protein was significantly stimulated at the late stage of virus infection. Using recombinant vaccinia viruses, we found that a relatively small fraction (20 to 40%) of the cytoplasmic M1 protein associated with cellular membranes in the absence of other viral proteins, while coexpression of the HA and the NA stimulated membrane binding of the M1 protein, The stimulatory effect of the NA (>90%) was significant and higher than that of the HA (>60%). Introduction of mutations into the cytoplasmic tail of the NA interfered with its stimulatory effect, Meanwhile, the HA may complement the defective NA and facilitate virus assembly in cells infected with the NA/TAIL(-) transfectant. In conclusion, the highly conserved cytoplasmic tails of the HA and NA play an important role in virus assembly.