NEUTRALIZATION MAP OF THE HEMAGGLUTININ-NEURAMINIDASE GLYCOPROTEIN OF NEWCASTLE-DISEASE VIRUS - DOMAINS RECOGNIZED BY MONOCLONAL-ANTIBODIES THAT PREVENT RECEPTOR RECOGNITION
NEUTRALIZATION MAP OF THE HEMAGGLUTININ-NEURAMINIDASE GLYCOPROTEIN OF NEWCASTLE-DISEASE VIRUS - DOMAINS RECOGNIZED BY MONOCLONAL-ANTIBODIES THAT PREVENT RECEPTOR RECOGNITION
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DOI：
10.1128/jvi.65.9.4999-5006.1991
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发表时间：
1991-09-01
影响因子：
5.4
通讯作者：
RIEL, AM
中科院分区：
文献类型：
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作者：
IORIO, RM;SYDDALL, RJ;RIEL, AM
新城疫病毒血凝素-神经氨酸酶（HN）糖蛋白单克隆抗体（mab）在分子表面形成7个重叠的抗原位点。其中五个位点的抗体主要通过防止病毒粒子附着于细胞受体来中和病毒的传染性。通过鉴定逃避单克隆抗体对这5个抗原位点的中和的变异中的单氨基酸取代，构建了HN的中和图谱，鉴定了几个有助于单克隆抗体识别的表位的残基，这些表位阻断了分子的附着功能。这些表位至少部分由HN上的三个结构域定义：残基193 ~ 201；345至353（其中包括我们在HN中发现的唯一线性表位）；和由残基494、513至521和569组成的c端结构域。为了鉴定直接参与受体识别的HN残基，我们测试了每个变异的凝集高碘酸盐修饰的鸡红细胞的能力。在残基193上有一个单氨基酸取代的变异比野生型病毒对高碘酸盐处理红细胞的抵抗力高2.5至3倍，这表明该残基影响病毒与细胞表面含唾液酸受体的结合。
Monoclonal antibodies (MAbs) to the hemagglutinin-neuraminidase (HN) glycoprotein of Newcastle disease virus delineate seven overlapping antigenic sites which form a continuum on the surface of the molecule. Antibodies to five of these sites neutralize viral infectivity principally by preventing attachment of the virion to cellular receptors. Through the identification of single amino acid substitutions in variants which escape neutralization by MAbs to these five antigenic sites, a neutralization map of HN was constructed, identifying several residues that contribute to the epitopes recognized by MAbs which block the attachment function of the molecule. These epitopes are defined, at least in part, by three domains on HN: residues 193 to 201; 345 to 353 (which include the only linear epitope we have identified in HN); and a C-terminal domain composed of residues 494, 513 to 521, and 569. To identify HN residues directly involved in receptor recognition, each of the variants was tested for its ability to agglutinate periodate-modified chicken erythrocytes. One variant with a single amino acid substitution at residue 193 was 2.5- to 3-fold more resistant to periodate treatment of erythrocytes than the wild-type virus, suggesting that this residue influences the binding of virus to a sialic acid-containing receptor(s) on the cell surface.