Point mutations in glycoprotein gene of vesicular stomatitis virus (New Jersey serotype) selected by resistance to neutralization by epitope-specific monoclonal antibodies.
Point mutations in glycoprotein gene of vesicular stomatitis virus (New Jersey serotype) selected by resistance to neutralization by epitope-specific monoclonal antibodies.
复制标题
水疱性口炎病毒（新泽西血清型）糖蛋白基因的点突变通过表位特异性单克隆抗体的中和抗性进行选择。
DOI：
10.1016/0042-6822(88)90274-7
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发表时间：
1988
期刊：
影响因子：
3.7
通讯作者：
Wagner,RR
中科院分区：
文献类型：
--
作者：
Luo,LH;Li,Y;Snyder,RM;Wagner,RR
Antigenic variants of the New Jersey serotype of vesicular stomatitis virus (VSV-NJ) were isolated and cloned by selecting virus plaques resistant to neutralization by high-titered monoclonal antibodies (MAbs) directed to glycoprotein (G) epitopes V, VI, VII, or VIII. The G proteins of each neutralization-resistant virus variant also exhibited markedly reduced antigenic reactivity with each corresponding epitope-specific MAb as determined by enzyme-linked immuno-absorbent assay and by Western blot analysis. Loss of antigenic reactivity of certain mutant G proteins to a MAb other than the one used to select the mutant virus suggested close antigenic proximity, particularly for epitopes VI and VII. The virion RNAs coding for the entire G gene of the wild-type virus and 10 MAb-induced mutants were sequenced by primer DNA extension using the dideoxy method. Each mutant G gene exhibited only a single nucleotide change, leading in each case to a single amino acid substitution, as follows: Glu210→ Lys for all three mutants selected by MAbl4 (epitope VII); Pro266→ Thr for one mutant selected by MAb12 (epitope VI); Ser277→ Leu for all three mutants selected by MAW 5 (epitope VIII); and Glu364→ Lys for all three mutants selected by MAb11 (epitope V). These neutralizing MAb-selected mutations are clustered in the middle third of the 517-amino acid VSV-NJ G protein, presumably resulting in conformational changes that alter recognition of one or more antigenic determinants by a specific monoclonal antibody.
