SYNTHESIS OF MUMPS-VIRUS POLYPEPTIDES IN INFECTED VERO CELLS
SYNTHESIS OF MUMPS-VIRUS POLYPEPTIDES IN INFECTED VERO CELLS
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DOI:
10.1016/0042-6822(82)90102-7
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发表时间:
1982-01-01
期刊:
影响因子:
3.7
通讯作者:
COMPANS, RW
中科院分区:
文献类型:
--
作者:
HERRLER, G;COMPANS, RW
Mumps virus was adapted to growth in African green monkey kidney Vero cells, which yielded virus of high infectivity titers. The structural polypeptides of purified virions grown in Vero cells were similar to those described previously for egg-grown mumps virus: L (200K), HN (79K), NP (72K), F1 (61K), P (45K), M (40K) and F2 (16K). The synthesis of viral polypeptides in Vero cells was analyzed by pulse labeling with radioactive amino acid precursors. The nucleoprotein (NP) was the first to be detected intracellularly above the cellular protein background at 6 hours post-infection (h.p.i.). By 12 h.p.i., all viral polypeptides were observed except for the glycoproteins F1 and F2, which are derived from a precursor designated F0 (74K). Two low-MW polypeptides not present in purified virions were also detected in infected cells. They are designated pI (28K) and pII (19K). Peptide mapping revealed that these 2 polypeptides share regions of their amino acid sequence and that they are also related to the structural protein P. Polypeptides pI and pII were found in several cell types (Vero, chicken embryo fibroblast, Madin-Darby bovine kidney MDBK cells) infected with mumps virus. Infection of Vero cells with other paramyxoviruses (simian virus 5 and Sendai virus) did not induce the synthesis of proteins comparable to PI and PII; in mumps virus-infected cells no counterpart to the nonstructural C protein of Sendai virus was detected. Pulse-chase experiments suggest that pI and pII may not be derived from P by proteolytic cleavage.