scholarly journals Single Amino Acid Differences Are Sufficient for CD4+ T-Cell Recognition of a Heterologous Virus by Cattle Persistently Infected with Bovine Viral Diarrhea Virus

Virology ◽  
2000 ◽  
Vol 276 (1) ◽  
pp. 70-82 ◽  
Author(s):  
Trevor Collen ◽  
Alastair J. Douglas ◽  
David J. Paton ◽  
Gang Zhang ◽  
W.Ivan Morrison
Keyword(s):  
Amino Acid ◽  
Cd4 T Cell ◽  
Single Amino Acid ◽  
Bovine Viral Diarrhea ◽  
Cell Recognition ◽  
Diarrhea Virus ◽  
Viral Diarrhea ◽  
T Cell Recognition ◽  
Heterologous Virus ◽  
Viral Diarrhea Virus

scholarly journals Specific Inhibition of Bovine Viral Diarrhea Virus Replicase

2003 ◽  
Vol 77 (12) ◽  
pp. 6753-6760 ◽  
Author(s):  
Jin-Hua Sun ◽  
Julie A. Lemm ◽  
Donald R. O'Boyle ◽  
Jason Racela ◽  
Richard Colonno ◽  
...  
Keyword(s):  
Bovine Viral Diarrhea Virus ◽  
Single Amino Acid ◽  
Bovine Viral Diarrhea ◽  
Cdna Clones ◽  
Single Mutation ◽  
Resistant Virus ◽  
Replication Efficiency ◽  
Diarrhea Virus ◽  
Viral Diarrhea ◽  
Viral Diarrhea Virus

ABSTRACT Compound-1453 was identified and characterized as a specific inhibitor of bovine viral diarrhea virus (BVDV). The concentration of compound-1453 which results in 50% protection from virus-induced cytopathic effect is ∼2.2 μM, with a therapeutic index of 60, and it is not active against a panel of RNA and DNA viruses. A time-of-addition experiment suggested that compound-1453 targets a stage of the viral life cycle after viral entry. To determine the target of compound-1453, resistant virus was generated. Resistant variants grew efficiently in the presence or absence of 33 μM compound-1453 and exhibited replication efficiency in the presence of compound-1453 approximately 1,000-fold higher than that of the wild-type (wt) virus. Functional mapping and sequence analysis of resistant cDNAs revealed a single amino acid substitution (Glu to Gly) at residue 291 in the NS5B polymerase in all eight independently generated cDNA clones. Recombinant virus containing this single mutation retained the resistance phenotype and a replication efficiency similar to that of the original isolated resistant virus. Since compound-1453 did not inhibit BVDV polymerase activity in vitro (50% inhibitory concentration > 300 μM), we developed a membrane-based assay that consisted of a BVDV RNA replicase complex isolated from virus-infected cells. Compound-1453 inhibited the activity of the wt, but not the drug-resistant, replicase in the membrane assay at concentrations similar to those observed in the viral infection assay. This work presents a novel inhibitor of a viral RNA-dependent RNA replicase.

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.

scholarly journals A CRISPR/Cas9 Generated Bovine CD46-knockout Cell Line—A Tool to Elucidate the Adaptability of Bovine Viral Diarrhea Viruses (BVDV)

Viruses ◽  
2020 ◽  
Vol 12 (8) ◽  
pp. 859 ◽  
Author(s):  
Kevin P. Szillat ◽  
Susanne Koethe ◽  
Kerstin Wernike ◽  
Dirk Höper ◽  
Martin Beer
Keyword(s):  
Amino Acid ◽  
Cell Line ◽  
Receptor Interaction ◽  
Bovine Viral Diarrhea ◽  
Viral Glycoprotein ◽  
Diarrhea Virus ◽  
Viral Diarrhea ◽  
Dependent Cell ◽  
Viral Diarrhea Virus

Bovine viral diarrhea virus (BVDV) entry into a host cell is mediated by the interaction of the viral glycoprotein E2 with the cellular transmembrane CD46 receptor. In this study, we generated a stable Madin–Darby Bovine Kidney (MDBK) CD46-knockout cell line to study the ability of different pestivirus A and B species (BVDV-1 and -2) to escape CD46-dependent cell entry. Four different BVDV-1/2 isolates showed a clearly reduced infection rate after inoculation of the knockout cells. However, after further passaging starting from the remaining virus foci on the knockout cell line, all tested virus isolates were able to escape CD46-dependency and grew despite the lack of the entry receptor. Whole-genome sequencing of the escape-isolates suggests that the genetic basis for the observed shift in infectivity is an amino acid substitution of an uncharged (glycine/asparagine) for a charged amino acid (arginine/lysine) at position 479 in the ERNS in three of the four isolates tested. In the fourth isolate, the exchange of a cysteine at position 441 in the ERNS resulted in a loss of ERNS dimerization that is likely to influence viral cell-to-cell spread. In general, the CD46-knockout cell line is a useful tool to analyze the role of CD46 for pestivirus replication and the virus–receptor interaction.

scholarly journals Genetic analysis of NS5B gene from bovine viral diarrhea virus-infected cattle in Central and East Java, Indonesia

2019 ◽  
Vol 12 (7) ◽  
pp. 1108-1115 ◽  
Author(s):  
S. H. Irianingsih ◽  
H. Wuryastuty ◽  
R. Wasito ◽  
H. Wibawa ◽  
F. S. Tjatur Rasa ◽  
...  
Keyword(s):  
Amino Acid ◽  
Genetic Variability ◽  
Binding Pocket ◽  
Bovine Viral Diarrhea ◽  
Infected Cattle ◽  
Amino Acid Residues ◽  
Diarrhea Virus ◽  
Viral Diarrhea ◽  
Central Java ◽  
Viral Diarrhea Virus

Background and Aim: A previous study divided Indonesian bovine viral diarrhea virus (BVDV)-1 into subgenotypes BVDV-1a to BVDV-1d based on the partial NS5B gene using strain Bega as reference for BVDV-1a. In fact, it is clustered into BVDV-1c with strain Bega-like Australia. BVDV genotyping has been done on isolates from Jakarta, West and Central Java, but East Java isolates have not been genotyped. This study aimed to analyze genetic variability and amino acid residues in the nucleotide-binding pocket of the NS5B gene from infected cattle. Materials and Methods: Samples were obtained from the Sera Bank originating from active and passive surveillance of cattle that had been tested for BVDV antigen from 2013 to 2017. Detection of the p80 antibody and BVDV genotyping was carried out using ELISA and nested-multiplex-polymerase chain reaction (PCR), respectively. We defined 15 nested PCR products for partial sequencing of NS5B. Those field samples were selected from each location and year using proportional calculation as a representative sample. Homological and phylogenetic analyses of the partial NS5B gene were performed using BLAST and MEGA version 6. Results: Based on the phylogenetic tree analysis using 360 nucleotides as the partial NS5B gene, Indonesian BVDV-1 isolates from Central and East Java were subdivided to BVDV-1a (n=9), BVDV-1b (n=1), and BVDV-1c (n=5). In the present study, the homology of BVDV subgenotype -1a, -1b, and -1c was compared to the BVDV GenBank data and found 90-93%, 93%, and 92-95% respectively with the average pairwise distance of 0.207. A point mutation was shown at R283K of all BVDV isolates based on the sequence of three amino acid residues R283, R285, and I287 in the nucleotide-binding pocket as a part of the encoded RNA-dependent RNA polymerase. Conclusion: This study revealed the genetic variability of BVDV infecting cattle in Central Java and East Java, Indonesia, the subtypes BVDV-1a, BVDV-1b, BVDV-1c, and a point mutation at the R283K residue.

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