Kantrong S, Saunal H, Briand J P, Sako N
Laboratory of Plant Pathology, Faculty of Agriculture, Saga University, Japan.
Arch Virol. 1995;140(3):453-67. doi: 10.1007/BF01718423.
The antigenic activity of the N-terminal region of coat protein of turnip mosaic virus (TuMV) aphid transmissible strain 1 and non-transmissible strain 31 was examined by using a panel of monoclonal antibodies (MAbs) raised against the two virus strains as well as antisera raised against several synthetic peptides from the N-terminal region of the protein. The reactivity of these antibodies was tested in ELISA and in a biosensor system (BIAcore Pharmacia) using virus particles, dissociated coat protein and synthetic peptides as antigens. Substitution of a single amino acid at position 8 in the coat protein of TuMV strain 1 abolished any cross-reactivity between MAbs to strain 1 and the substituted peptide (strain 31) in ELISA although some cross-reactivity was apparent in BIAcore inhibition experiments. In reciprocal tests with MAbs to strain 31 no cross-reactivity with the heterologous peptide was detected in either type of assay. The amino acid residue present at position 8 appears to play a critical role in the binding capacity of MAbs specific for the N-terminal region of TuMV. Antiserum to a synthetic peptide corresponding to residues 1-14 of the protein of TuMV strain 1 was found to react strongly with dissociated coat protein and intact virus particles and was able to inhibit the aphid transmission of the virus. Antiserum to the corresponding peptide of strain 31 did not have this capacity.
利用一组针对芜菁花叶病毒（TuMV）蚜虫传播株系1和非传播株系31产生的单克隆抗体（MAb）以及针对该蛋白N端区域几种合成肽产生的抗血清，检测了这两种病毒株系外壳蛋白N端区域的抗原活性。在酶联免疫吸附测定（ELISA）和生物传感器系统（BIAcore Pharmacia）中，以病毒颗粒、解离的外壳蛋白和合成肽作为抗原，检测了这些抗体的反应性。在ELISA中，TuMV株系1外壳蛋白第8位的单个氨基酸替换消除了针对株系1的MAb与替换肽（株系31）之间的任何交叉反应，尽管在BIAcore抑制实验中仍有一些交叉反应明显。在用针对株系31的MAb进行的反向试验中，在任何一种检测中均未检测到与异源肽的交叉反应。第8位存在的氨基酸残基似乎在对TuMV N端区域具有特异性的MAb的结合能力中起关键作用。发现针对TuMV株系1蛋白第1 - 14位残基的合成肽的抗血清与解离的外壳蛋白和完整病毒颗粒强烈反应，并能够抑制该病毒的蚜虫传播。针对株系31相应肽的抗血清没有这种能力。
