Herrler G, Compans R W
J Virol. 1983 Aug;47(2):354-62. doi: 10.1128/JVI.47.2.354-362.1983.
Analysis of the pronase-derived glycopeptides of isolated mumps virus glycoproteins revealed the presence of both complex and high-mannose-type oligosaccharides on the HN and F1 glycoproteins, whereas only high-mannose-type glycopeptides were detected on F2. Endoglycosidase F, a newly described glycosidase that cleaves N-linked high mannose as well as complex oligosaccharides, appeared to completely cleave the oligosaccharides linked to HN and F2, whereas F1 was resistant to the enzyme. Two distinct cleavage products of F2 were observed, suggesting the presence of two oligosaccharide side chains. Tunicamycin was found to reduce the infectious virus yield and inhibit mumps virus particle formation. The two glycoproteins, HN and F, were not found in the presence of the glycosylation inhibitor. However, two new polypeptides were detected, with molecular weights of 63,000 (HNT) and 53,000 (FT), respectively, which may represent nonglycosylated forms of the glycoproteins. Synthesis of the nonglycosylated virus-coded proteins (L, NP, P, M, pI, and pII) was not affected by tunicamycin. The formation of HN oligomers and the proteolytic cleavage of the F protein were found to occur with the same kinetics. Analysis of the time course of appearance of mumps virus glycoproteins on the cell surface suggested that dimerization of HN and cleavage of F occur immediately after their exposure on the plasma membrane.
对分离出的腮腺炎病毒糖蛋白中链霉蛋白酶衍生的糖肽进行分析，结果显示HN和F1糖蛋白上同时存在复合型和高甘露糖型寡糖，而在F2上仅检测到高甘露糖型糖肽。内切糖苷酶F是一种新描述的糖苷酶，可切割N - 连接的高甘露糖以及复合型寡糖，它似乎能完全切割与HN和F2相连的寡糖，而F1对该酶具有抗性。观察到F2有两种不同的切割产物，表明存在两条寡糖侧链。发现衣霉素可降低感染性病毒产量并抑制腮腺炎病毒颗粒形成。在存在糖基化抑制剂的情况下未检测到两种糖蛋白HN和F。然而，检测到两种新的多肽，分子量分别为63,000（HNT）和53,000（FT），它们可能代表糖蛋白的非糖基化形式。衣霉素不影响非糖基化病毒编码蛋白（L、NP、P.M、pI和pII）的合成。发现HN寡聚体的形成和F蛋白的蛋白水解切割具有相同的动力学。对腮腺炎病毒糖蛋白在细胞表面出现的时间进程分析表明，HN的二聚化和F的切割在它们暴露于质膜后立即发生。
