DISSOCIATION OF PROGENY VACCINIA VIRUS FROM THE CELL-MEMBRANE IS REGULATED BY A VIRAL ENVELOPE GLYCOPROTEIN - EFFECT OF A POINT MUTATION IN THE LECTIN HOMOLOGY DOMAIN OF THE A34R GENE
DISSOCIATION OF PROGENY VACCINIA VIRUS FROM THE CELL-MEMBRANE IS REGULATED BY A VIRAL ENVELOPE GLYCOPROTEIN - EFFECT OF A POINT MUTATION IN THE LECTIN HOMOLOGY DOMAIN OF THE A34R GENE
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DOI：
10.1128/jvi.67.6.3319-3325.1993
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发表时间：
1993-06-01
影响因子：
5.4
通讯作者：
MOSS, B
中科院分区：
文献类型：
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作者：
BLASCO, R;SISLER, JR;MOSS, B
痘苗病毒株从受感染的细胞中释放的胞外被膜病毒(EEV)的量有很大差异。IHD-J株产生的EEV是相关WR株的40倍，因此在液体培养的敏感单层细胞中会产生细长的彗星状病毒空斑，而不是清晰界定的圆形空斑。EEV形成的差异是由于被包裹的WR病毒粒子保留在细胞表面(R.Blasco和B.Moss，J.Virol)。66：4170-4179,1992)。通过使用WR和IHD-J DNA片段进行标记转移，并通过彗星形成实验对后代病毒进行分析，我们确定了A34R基因和至少一个其他基因调控着细胞相关病毒粒子的释放。用来自IHD-J的相应基因替换WR的A34R基因使EEV的生成量增加了10倍，并赋予了形成独特的彗星状斑块的能力。基因A34R编码一种EEV特异性糖蛋白，与C型动物凝集素(S.A.Duncan和G.L.Smith，J.Virol)同源。66：1610-1621,1992)。WR株和IHD-J株A34R基因的核苷酸序列有6个差异，其中4个是沉默的。其中一个密码子突变(Lys-151-&Gt；Glu)位于假定的碳水化合物识别结构域，足以将彗星形成表型转移到WR病毒。这些数据表明，A34R编码的糖蛋白通过其凝集素同源结构域参与了后代病毒在亲本细胞表面的保留，并增加了该蛋白在病毒与未感染细胞的附着中发挥作用的可能性。
Vaccinia virus strains vary considerably in the amounts of extracellular enveloped virus (EEV) that they release from infected cells. The IHD-J strain produces up to 40 times more EEV than does the related WR strain and consequently generates elongated comet-shaped virus plaques instead of sharply defined round ones in susceptible monolayer cells under liquid medium. The difference in EEV formation is due to the retention of enveloped WR virions on the cell surface (R. Blasco and B. Moss, J. Virol. 66:4170-4179, 1992). By using WR and IHD-J DNA fragments for marker transfer and analyzing the progeny virus by the comet formation assay, we determined that gene A34R and at least one other gene regulate the release of cell-associated virions. Replacement of the A34R gene of WR with the corresponding gene from IHD-J increased the amount of EEV produced by 10-fold and conferred the ability to form distinctive comet-shaped plaques. Gene A34R encodes an EEV-specific glycoprotein with homology to C-type animal lectins (S. A. Duncan and G. L. Smith, J. Virol. 66:1610-1621, 1992). The nucleotide sequences of the A34R genes of WR and IHD-J strains differed in six positions, of which four were silent. One of the codon mutations (Lys-151-->Glu), which is located in the putative carbohydrate recognition domain, was sufficient to transfer a comet-forming phenotype to WR virus. These data indicate that the A34R-encoded glycoprotein is involved, through its lectin homology domain, in the retention of progeny virus on the surface of parental cells and raise the possibility that the protein also has a role in virus attachment to uninfected cells.