Sangar D V, Rowlands D J, Cavanagh D, Brown F
J Gen Virol. 1976 Apr;31(1):35-46. doi: 10.1099/0022-1317-31-1-35.
In addition to the four major polypeptides VP1 and VP4, foot-and-mouth disease virus particles contain two minor polypeptides, mol. wt. 40 X 10(3) (P40) and 52 X 10(3) (P52). Extensive purification procedures failed to remove these minor polypeptides from the virus particles. Polypeptide P40 co-electrophoresed in SDS-polyacrylamide gels with VP0, the probable precursor of VP2 and VP4 and was inaccessible to iodination in situ. The second minor polypeptide, P52, co-electrophoresed with the virus infection associated (VIA) antigen found in large amounts in harvests of the virus grown in BHK 21 cells. Polypeptide P52 was shown to be located near the surface of the virus particle by iodination experiments and by its removal on incubating the particles with trypsin or chymotrypsin. Pactamycin mapping showed that this polypeptide was not a precursor of the structural polypeptides. About one copy of P52 and 4 copies of P40 were found in the virus particles sedimenting at 146S. However a larger number of copies was found in those virus particles sedimenting faster than the 146S peak.
除了四种主要多肽VP1和VP4外，口蹄疫病毒颗粒还含有两种次要多肽，分子量分别为40×10³（P40）和52×10³（P52）。广泛的纯化程序未能从病毒颗粒中去除这些次要多肽。多肽P40在SDS-聚丙烯酰胺凝胶中与VP0共电泳，VP0可能是VP2和VP4的前体，且原位碘化时不可及。第二种次要多肽P52与在BHK 21细胞中生长的病毒收获物中大量存在的病毒感染相关（VIA）抗原共电泳。通过碘化实验以及用胰蛋白酶或胰凝乳蛋白酶孵育颗粒后其被去除的情况表明，多肽P52位于病毒颗粒表面附近。嘌呤霉素图谱显示该多肽不是结构多肽的前体。在沉降系数为146S的病毒颗粒中发现约一个拷贝的P52和4个拷贝的P40。然而，在沉降速度比146S峰更快的那些病毒颗粒中发现了更多的拷贝数。
