The fusion glycoprotein of Sendai virus: sequence analysis of an epitope involved in fusion and virus neutralization.

The fusion glycoprotein of Sendai virus: sequence analysis of an epitope involved in fusion and virus neutralization.
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仙台病毒的融合糖蛋白:参与融合和病毒中和的表位的序列分析。

DOI:
10.1016/0042-6822(87)90301-1
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发表时间:
1987
期刊:
影响因子:
3.7
通讯作者:
Naeve,CW
Naeve,CW
中科院分区:
医学3区
文献类型:
--
作者:
Portner,A;Scroggs,RA;Naeve,CW

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为了定位F糖蛋白上参与仙台病毒融合和病毒中和的氨基酸残基,利用抑制这些功能的抗F单克隆抗体选择了3种抗原变异体。对这三个变体的整个F基因的序列分析确定了一个导致抗体结合丧失的单一突变。该突变是在399残基上的脯氨酸到谷氨酰胺的替换,位于初级序列中远离被认为直接参与融合的疏水f1 - nh2末端的位置。由突变区域的氨基酸序列组成的合成肽,与用于选择变异的抗体结合,表明突变位点也是抗体结合位点。这一信息表明,在F分子的三维结构中,脯氨酸399周围的氨基酸残基位于f1 - nh2末端附近,抗体结合直接抑制了融合。讨论了其他不太可能的替代方案。
To localize the amino acid residues on the F glycoprotein that are involved in Sendai virus fusion and virus neutralization, an anti-F monoclonal antibody which inhibits these functions was used to select three antigenic variants. Sequence analysis of the entire F gene of the three variants identified a single mutation that was responsible for the loss of antibody binding. The mutation, a proline to glutamine substitution at residue 399, was at a position in the primary sequence far removed from the hydrophobic F1-NH2terminus thought to be directly involved in fusion. A synthetic peptide, comprising amino acid sequences in the region of the mutation, bound to the antibody used to select the variants, suggesting that the site of mutation is also the site of antibody binding. This information suggests that in the three-dimensional structure of the F molecule the amino acid residues around proline 399 are located close to the F1-NH2terminus, and that fusion is directly inhibited by antibody binding. Other less likely alternatives are discussed.
人副流感病毒3型融合糖蛋白:基因核苷酸序列、切割激活位点的直接鉴定以及与其他副粘病毒的比较。
DOI: --
发表时间: 1986
期刊: Virology
影响因子: 3.7
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DOI: 10.1016/0042-6822(85)90226-0
发表时间: 1985
期刊: Virology
影响因子: 3.7
作者:
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DOI: --
发表时间: 1974
期刊: Virology
影响因子: 3.7
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