scholarly journals Identification of Conserved Amino Acid Substitutions During Serial Infection of Pregnant Cattle and Sheep With Bovine Viral Diarrhea Virus

2018 ◽  
Vol 9 ◽  
Author(s):  
Thibaud Kuca ◽  
Thomas Passler ◽  
Benjamin W. Newcomer ◽  
John D. Neill ◽  
Patricia K. Galik ◽  
...  
Keyword(s):  
Amino Acid ◽  
Bovine Viral Diarrhea Virus ◽  
Bovine Viral Diarrhea ◽  
Amino Acid Substitutions ◽  
Diarrhea Virus ◽  
Viral Diarrhea ◽  
Viral Diarrhea Virus ◽  
Cattle And Sheep

The analyses of relationships among nucleotide, synonymous codon and amino acid usages for E2 gene of bovine viral diarrhea virus

Gene ◽  
2018 ◽  
Vol 660 ◽  
pp. 62-67 ◽  
Author(s):  
Xiao-xia Ma ◽  
Peng Ma ◽  
Qiu-yan Chang ◽  
Lin-jie Li ◽  
Xiao-kai Zhou ◽  
...  
Keyword(s):  
Amino Acid ◽  
Bovine Viral Diarrhea Virus ◽  
Synonymous Codon ◽  
Bovine Viral Diarrhea ◽  
Diarrhea Virus ◽  
Viral Diarrhea ◽  
E2 Gene ◽  
Viral Diarrhea Virus

scholarly journals Formation of bovine viral diarrhea virus E1–E2 heterodimers is essential for virus entry and depends on charged residues in the transmembrane domains

2008 ◽  
Vol 89 (9) ◽  
pp. 2114-2121 ◽  
Author(s):  
Saskia Ronecker ◽  
Gert Zimmer ◽  
Georg Herrler ◽  
Irene Greiser-Wilke ◽  
Beatrice Grummer
Keyword(s):  
Amino Acid ◽  
Bovine Viral Diarrhea Virus ◽  
Transmembrane Domain ◽  
Virus Entry ◽  
Transmembrane Domains ◽  
Site Directed Mutagenesis ◽  
Bovine Viral Diarrhea ◽  
Diarrhea Virus ◽  
Viral Diarrhea ◽  
Viral Diarrhea Virus

The envelope of bovine viral diarrhea virus (BVDV) contains the glycoproteins Erns, E1 and E2. Complementation of a recombinant vesicular stomatitis virus (VSV) with BVDV glycoproteins resulted in infectious pseudotyped viruses. To elucidate the specific role of each of the single envelope glycoproteins during viral entry, pseudotypes were generated bearing the BVDV envelope proteins in different combinations. Pseudoviruses that contained E1 and E2 but not Erns were infectious, indicating that Erns is dispensable for virus entry. VSV/BVDV pseudotypes with chimeric proteins (the ectodomain of the BVDV glycoprotein and the transmembrane domain of the VSV-G protein) were not infectious. The fact that E1–E2 heterodimers were not detected if one of the proteins was chimeric indicated that the heterodimers are crucial for BVDV entry. It was shown by site-directed mutagenesis that the charged amino acids in the transmembrane domains of BVDV E1 (lysine and arginine) and the charged amino acid in the transmembrane domain of E2 (arginine) play a key role in heterodimer formation. Pseudoviruses bearing the mutation E2-R/A, where the charged amino acid was substituted by alanine, were not infectious, supporting the hypothesis that E1–E2 heterodimers are essential for BVDV entry.

Prevention and elimination of bovine viral diarrhea virus infections in fetal fibroblast cells

2004 ◽  
Vol 64 (2) ◽  
pp. 113-118 ◽  
Author(s):  
M GIVENS ◽  
D STRINGFELLOW ◽  
C DYKSTRA ◽  
K RIDDELL ◽  
P GALIK ◽  
...  
Keyword(s):  
Bovine Viral Diarrhea Virus ◽  
Bovine Viral Diarrhea ◽  
Fibroblast Cells ◽  
Virus Infections ◽  
Fetal Fibroblast ◽  
Diarrhea Virus ◽  
Viral Diarrhea ◽  
Viral Diarrhea Virus
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