Jaegle M, Briand J P, Burckard J, Van Regenmortel M H
Laboratoire d'Immunochimie, Institut de Biologie Moléculaire et Cellulaire du CNRS, Strasbourg, France.
Ann Inst Pasteur Virol. 1988 Jan-Mar;139(1):39-50. doi: 10.1016/s0769-2617(88)80004-2.
Three peptides corresponding to residues 28-40, 138-154 and 380-387 of the coat protein of tomato bushy stunt virus (TBSV) were synthesized by the solid phase method and used to raise specific antibodies. These antibodies were used to follow the conformational changes that occur when TBSV particles swell under slightly alkaline conditions. Peptides 28-40 and 380-387 were found to correspond to continuous epitopes in the dissociated viral protein as well as in both compact and swollen virions. The region 138-154, which is also a continuous epitope of the monomeric protein, became accessible to antibody binding in the virion only when the particles were in the swollen state.
通过固相法合成了与番茄丛矮病毒(TBSV)外壳蛋白的28 - 40、138 - 154和380 - 387位残基相对应的三种肽,并用于制备特异性抗体。这些抗体用于追踪TBSV颗粒在微碱性条件下膨胀时发生的构象变化。发现肽28 - 40和380 - 387对应于解离的病毒蛋白以及紧密和膨胀病毒粒子中的连续表位。区域138 - 154也是单体蛋白的连续表位,只有当颗粒处于膨胀状态时,该区域才会在病毒粒子中变得可被抗体结合。