Joisson C, Kuster F, Plaué S, Van Regenmortel M H
Laboratoire d'Immunochimie, Institut de Biologie Moléculaire et Cellulaire, Strasbourg, France.
Arch Virol. 1993;128(3-4):299-317. doi: 10.1007/BF01309441.
The antigenic structure of the comovirus bean pod mottle virus (BPMV) was studied using synthetic peptides selected on the basis of the exposed location of certain regions of the viral protein. Three regions of domain A, four regions of domain B and two regions of domain C of BPMV coat protein were studied. Each of four regions were synthesized in the form of linear and cyclized peptides while the others were synthesized as linear peptides only. The peptides were tested for their ability to be recognized by antibodies directed against BPMV. The peptides were also used for producing rabbit antisera, which were tested for their ability to react with various BPMV antigens as well as with the linear and cyclized peptides. All the peptides were found to correspond to epitopes of BPMV coat protein. Several of the antigenic sites of BPMV located on exposed loops of the coat protein occupy positions which correspond to known epitopes in the structurally related picornaviruses. Only in some cases did cyclization sufficiently improve the level of conformational mimicry between peptides and the viral protein to allow cross-reactions between them to be observed.
利用基于病毒蛋白特定区域暴露位置选择的合成肽,对豇豆花叶病毒(BPMV)的抗原结构进行了研究。研究了BPMV外壳蛋白A结构域的三个区域、B结构域的四个区域和C结构域的两个区域。四个区域中的每一个都以线性肽和环化肽的形式合成,而其他区域仅合成为线性肽。测试了这些肽被针对BPMV的抗体识别的能力。这些肽还用于制备兔抗血清,测试了它们与各种BPMV抗原以及线性和环化肽反应的能力。发现所有肽都对应于BPMV外壳蛋白的表位。BPMV位于外壳蛋白暴露环上的几个抗原位点占据的位置与结构相关的小RNA病毒中已知的表位相对应。只有在某些情况下,环化才足以提高肽与病毒蛋白之间的构象模拟水平,从而观察到它们之间的交叉反应。