Buchmeier M J, Gee S R, Rawls W E
J Virol. 1977 Apr;22(1):175-86. doi: 10.1128/JVI.22.1.175-186.1977.
Antigens detected by the complement-fixation (CF) test were prepared from BHK-21 cells infected with Pichinde virus. The preparations contained two antigens demonstrable by immunodiffusion. The antigen present in abundance was heat stable, Pronase resistant, and had a molecular weight of 20,000 to 30,000 as estimated by gel filtration. Polyacrylamide gel electrophoresis of purified antigen demonstrated two low-molecular-weight polypeptides. An identical antigenic determinant was found by disrupting purified virus with Nonidet P-40; however, none of the viral polypeptides co-migrated with the polypeptides derived from purified CF antigen. Pronase digestion of disrupted virus did not alter antigenicity but degraded the viral peptides to sizes similar to those associated with the major CF antigen. These observations suggest that the major CF antigen of Pichnide virus is a cleavage product of the structural proteins of the virus.
补体结合(CF)试验检测的抗原是用感染皮钦德病毒的BHK - 21细胞制备的。这些制剂含有两种可通过免疫扩散证明的抗原。大量存在的抗原对热稳定,对链霉蛋白酶有抗性,通过凝胶过滤估计其分子量为20,000至30,000。纯化抗原的聚丙烯酰胺凝胶电泳显示出两条低分子量多肽。用诺乃洗涤剂P - 40破坏纯化病毒后发现了相同的抗原决定簇;然而,没有一种病毒多肽与纯化的CF抗原衍生的多肽共迁移。对破坏的病毒进行链霉蛋白酶消化不会改变抗原性,但会将病毒肽降解到与主要CF抗原相关的大小。这些观察结果表明,皮钦德病毒的主要CF抗原是病毒结构蛋白的裂解产物。