Open AccessNew insights into processing of bovine viral diarrhea virus glycoproteins Erns and E1
Author(s) -
Anne Wegelt,
Ilona Reimann,
Johanna Marie Luise Zemke,
Martin Beer
Publication year - 2009
Publication title -
journal of general virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.55
H-Index - 167
eISSN - 1465-2099
pISSN - 0022-1317
DOI - 10.1099/vir.0.012559-0
Subject(s) - biology , virology , pestivirus , virus , ns2 3 protease , glycoprotein , cleavage (geology) , plasmid , complementary dna , viral replication , proteases , viral envelope , microbiology and biotechnology , flaviviridae , genetics , dna , hepatitis c virus , gene , biochemistry , paleontology , fracture (geology) , enzyme
Bovine viral diarrhea virus (BVDV) is a member of the genus Pestivirus within the family Flaviviridae . Its single-stranded RNA encodes a polyprotein that is cleaved co- and post-translationally by viral and cellular proteases. However, the cleavage between the envelope proteins E rns and E1 is still unexplained. In this study, an E rns –E1 protein could be identified and characterized with a new E1-specific antiserum. With bicistronic constructs bearing a deletion in the E rns -encoding region and expressing E rns or the E rns –E1 protein, it could be shown that this protein is not essential for virus replication. Furthermore, two putative cleavage sites were mutated in eukaryotic expression plasmids, as well as in full-length cDNA constructs. The mutation of position P3 of a potential signal peptide peptidase site abolished cleavage completely and no infectious virus progeny could be observed, indicating that cleavage of the E rns –E1 protein is indispensable for virus growth.