Processing in the pestivirus E2-NS2 region: Identification of proteins p7 and E2p7

被引:122
|
作者
Elbers, K
Tautz, N
Becher, P
Stoll, D
Rumenapf, T
Thiel, HJ
机构
[1] UNIV GIESSEN, INST VIROL, FAC VET MED, D-35392 GIESSEN, GERMANY
[2] FED RES CTR VIRUS DIS ANIM, D-72076 TUBINGEN, GERMANY
[3] NMI, D-72762 REUTLINGEN, GERMANY
关键词
D O I
10.1128/JVI.70.6.4131-4135.1996
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The pestivirus genome encodes a single polyprotein which is subject to co- and posttranslational processing by cellular and viral proteases. The map positions of all virus-encoded proteins are known with the exception of a hypothetical peptide (p?) which interlinks the glycoprotein E2 and the nonstructural protein NS2-3 approximately between amino acid positions 1060 and 1130. Expression studies with recombinant vaccinia viruses bearing a set of C-terminally truncated E2-p?-NS2-encoding sequences derived from a bovine viral diarrhea virus (BVDV) strain led to the identification of a minor fraction of E2 which had an increased molecular mass due to a C-terminal extension. This larger form of E2 (E2p7) was specifically recognized by an antiserum raised against the amino acid sequence from 1065 to 1125. In addition, the antibodies revealed a BVDV-encoded 7-kDa protein (p7) in infected cells. By radiosequencing it was determined that Val-1067 was the N-terminal amino acid of in vitro-synthesized p7. Analyses of BVDV and classical swine fever virus virions suggest that neither p7 nor E2p7 is a major structural constituent.
引用
收藏
页码:4131 / 4135
页数:5
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