Berencsi G, Lengyel A, Dyachenko N S, Nász I
Acta Microbiol Hung. 1983;30(3-4):189-97.
Two distinct CsCl-stable empty particle populations were characterized in human adenovirus type 1 infected cells. Different sensitivity to proteases and polypeptide composition indicate that empty capsids A and B are degradation products of two different assembly intermediates. Both empty particle populations react with antihexon antibodies similarly to complete virions. Thus the arrangement of exposed type-specific epitopes is suggested to be unchanged during virus assembly. Experimental evidence is presented that both antifibre and antihexon antibodies trigger structural changes of complete virions, which are initiating the specific loss of core protein V from antibody-aggregated virions.
在人1型腺病毒感染的细胞中鉴定出两种不同的CsCl稳定空颗粒群体。对蛋白酶的不同敏感性和多肽组成表明，空衣壳A和B是两种不同装配中间体的降解产物。两种空颗粒群体与抗六邻体抗体的反应与完整病毒粒子相似。因此，在病毒装配过程中，暴露的型特异性表位的排列被认为没有改变。实验证据表明，抗纤维抗体和抗六邻体抗体都会引发完整病毒粒子的结构变化，这会导致抗体聚集的病毒粒子中核心蛋白V的特异性丢失。
