Macejak D G, Luftig R B
Department of Microbiology, Immunology and Parasitology, Louisiana State University Medical Center, New Orleans 70112-1393.
Virology. 1991 Jan;180(1):120-5. doi: 10.1016/0042-6822(91)90015-4.
Although maximal synthesis of HSP70 is induced early (6-12 hr) after adenovirus type 5 (Ad5) infection of HEp-2 or HeLa cells, the total amount of HSP70 appears to be increased at late times of infection (18-24 hr). Since virion structural proteins also accumulate at these times, we investigated the possible interaction between Ad5 structural proteins and HSP70 by immunoprecipitation of infected cell extracts with antibodies to either ATP-affinity-purified HSP70 or to CsCl-gradient-purified Ad5 virions. We found that HSP70 and a 62-kDa Ad-specific protein coimmunoprecipitated from infected cell extracts. Antibody which recognizes one of these two proteins does not cross-react with the other. Thus, the association between HSP70 and the 62-kDa protein appears specific. Using different antisera to specific adenovirus structural proteins, we have identified the 62-kDa protein as the Ad5 fiber protein.
虽然在5型腺病毒（Ad5）感染人喉表皮样癌细胞（HEp-2）或人宫颈癌上皮细胞（HeLa）后的早期（6 - 12小时）就可诱导热休克蛋白70（HSP70）的最大合成，但在感染后期（18 - 24小时）HSP70的总量似乎会增加。由于病毒粒子结构蛋白在这些时候也会积累，我们通过用针对ATP亲和纯化的HSP70或氯化铯梯度纯化的Ad5病毒粒子的抗体对感染细胞提取物进行免疫沉淀，研究了Ad5结构蛋白与HSP70之间可能的相互作用。我们发现HSP70和一种62 kDa的腺病毒特异性蛋白能从感染细胞提取物中共免疫沉淀。识别这两种蛋白之一的抗体不会与另一种蛋白发生交叉反应。因此，HSP70与62 kDa蛋白之间的关联似乎具有特异性。使用针对特定腺病毒结构蛋白的不同抗血清，我们已将62 kDa蛋白鉴定为Ad5纤维蛋白。
