Processing in the pestivirus E2-NS2 region: identification of proteins p7 and E2p7.
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.
Elbers
K
K
Federal Research Center for Virus Diseases of Animals, Tübingen, Germany.
Tautz
N
N
Becher
P
P
Stoll
D
D
Rümenapf
T
T
Thiel
H J
HJ
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D001908:Diarrhea Viruses, Bovine Viral / Q000737:chemistry / Q000235:genetics*; D008969:Molecular Sequence Data; D014759:Viral Envelope Proteins / Q000032:analysis / Q000737:chemistry / Q000235:genetics*; D017361:Viral Nonstructural Proteins / Q000032:analysis / Q000737:chemistry / Q000235:genetics*; D014771:Virion / Q000737:chemistry
D014759:Viral Envelope Proteins; D017361:Viral Nonstructural Proteins