Hog cholera virus: molecular composition of virions from a pestivirus

Thiel, Heinz-Jürgen; Stark, Robert; Weiland, Emilie; Rümenapf, Till; Meyers, Gregor

doi:10.1128/jvi.65.9.4705-4712.1991

Cited by 328 publications

(176 citation statements)

References 29 publications

Supporting

Mentioning

170

Contrasting

Unclassified

Order By: Relevance

“…The SD sequences integrated between the LD elements in the genomes of BVDV Pe515CP and CP6 are derived from a region of the viral RNA which has been shown to code for ~20, the first protein of the BVDV ORF (Collett et a/., 1988b;Thiel et al, 1991). Because of the rapid liberation of this polypeptide during translation which can also be observed in vitro, it has been proposed, that p20 represents an autoprotease (Wiskerchen eta/., 1991;Thiel eta/., 1991).…”

Section: (A) Extracts From Mdbk Cells Infected With Bvdvmentioning

confidence: 99%

Rearrangement of viral sequences in cytopathogenic pestiviruses

et al. 1992

View full text Add to dashboard Cite

Two cytopathogenic isolates of bovine viral diarrhea virus (cpBVDV) have been analyzed. For both viruses two regions of their genomic RNAs were found to be duplicated and rearranged. The viral genomes contain a small duplicated element (SD) derived from the genomic 5' end far downstream of its original context. This sequence is followed by a larger duplication which encompasses the region coding for the protein p80(LD), a molecular marker for cpBVDV. The SD element codes for the viral protease p20. In the case of the viruses analyzed here the aminoterminus of p80 is generated by autoproteolytic removal of the preceding SD-encoded protease. For one of the cpBVDV isolates a specific fusion protein (p28) could be identified which is composed of p20 and part of p10, another viral protein. Molecular characterization of the respective noncytopathogenic counterpart revealed that duplication and rearrangement of sequences as well as the expression of p28 and p80 are specific for the cytopathogenic virus.

show abstract

Section: (A) Extracts From Mdbk Cells Infected With Bvdvmentioning

confidence: 99%

Rearrangement of viral sequences in cytopathogenic pestiviruses

et al. 1992

View full text Add to dashboard Cite

show abstract

“…CSFV is a small, enveloped virus with a single-stranded, positive-sense RNA genome, which is classified in the genus Pestivirus within the family Flaviviridae, along with bovine viral diarrhea virus 1 (BVDV-1), BVDV-2, and border disease virus (BDV) (Becher et al, 2003). The 12.5-kb CSFV genome contains a single open reading frame that encodes a 3898-amino-acid polyprotein and yields 12 final cleavage products: NH2-N pro -C-E rns -E1-E2-p7-NS2-NS3-NS4ANS4B-NS5A-NS5B-COOH through co-and post-translational processing of the polyprotein by cellular and viral proteases (Meyers et al, 1989;Meyers and Thiel, 1996;Thiel et al, 1991). The virion consists of four structural proteins, the capsid (C) protein and the glycoproteins E rns , E1, and E2 (Thiel et al, 1991).…”

Section: Introductionmentioning

confidence: 99%

“…The C protein of CSFV is located between the N-terminal protease N pro and the glycoprotein E rns in the polyprotein. The C protein is a small protein and rich in basic amino acids (lysine and arginine) (Meyers et al, 1989;Thiel et al, 1991). Mature C protein has 86 amino acids and its apparent molecular weight (MW) is 14 kDa (Heimann et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

“…The C protein acts as a transcriptional regulator and plays an important role in the CSFV virion maturation (Liu et al, 1998a). Formation of a C protein-RNA complex inside the virion suggests a protective function of the C protein (Meyers and Thiel, 1996;Thiel et al, 1991). Furthermore, C proteins may function in RNA structural rearrangements taking place during virus replication (Ivanyi-Nagy et al, 2008) and RNA packaging and virion morphogenesis (Murray et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Identification of a linear epitope on the capsid protein of classical swine fever virus

Zhang

Xu²,

Sun

et al. 2011

Virus Research

View full text Add to dashboard Cite

The capsid (C) protein of Classical swine fever virus (CSFV) is proposed to play an essential role in the replication and translation of the viral RNA. In this study, a monoclonal antibody (mAb) directed against the C protein was generated with the recombinant C protein expressed in Escherichia coli as immunogen. IFA and IPMA analysis showed that the native C protein of CSFV virions was reactive to the mAb. By truncating the C protein, we identified a linear epitope recognized by the mAb, corresponding to amino acids (61)TQDGLYHNKN(70) of the CSFV C protein, which is well conserved among pestiviruses. Laser confocal analysis showed that the C protein mainly locates in the cellular nucleoplasm and nucleolus of PK-15 cells. The results have implications for further study of CSFV replication.

show abstract

“…The etiological agent, classical swine fever virus (CSFV), is a member of the genus Pestivirus, which belongs to the family Flaviviridae [1,2]. CSFV is a small, enveloped virus with a 12.5-kb positive, single-stranded RNA genome containing a single large open reading frame encoding a polyprotein precursor, which is cleaved co-and post-translationally by cellular and viral proteases into structural and nonstructural proteins [3]. Both ends of the genome are flanked by 5 0 and 3 0 untranslated regions (UTR), which are highly conserved among all of the virus isolates [4][5][6][7].…”

Section: Introductionmentioning

confidence: 99%

Rapid pre-clinical detection of classical swine fever by reverse transcription loop-mediated isothermal amplification

Chen¹,

Zhang²,

Ma³

et al. 2009

Molecular and Cellular Probes

View full text Add to dashboard Cite

The usefulness of reverse transcription loop-mediated isothermal amplification (RT-LAMP) for rapid pre-clinical detection of classical swine fever virus (CSFV) infection was evaluated. The RT-LAMP reaction could be finished in 60 min under isothermal condition at 65 degrees C by employing a set of four primers targeting the 5' untranslated region of CSFV. The RT-LAMP assay of CSFV showed higher sensitivities than that of RT-PCR, with a detection limit of 5 copies per reaction. No cross-reactivity was observed from the samples of other related viruses including porcine circovirus type 2, porcine parvovirus, porcine pseudorabies virus, Japanese encephalitis virus, and porcine reproductive and respiratory syndrome virus. The detection rates of CSFV RT-LAMP, RT-PCR and virus isolation for samples including blood, tonsil, nasal and rectal swabs from uninoculated pigs without any clear clinical symptom were 89%, 78% and 71%, respectively. Furthermore, all of the assays showed higher sensitivity for blood and tonsil swabs samples than nasal and rectal swabs. These results indicate that the CSFV RT-LAMP assay is a valuable tool for its rapid, cost-effective detection and has potential usefulness for rapid pre-clinical detection and surveillance of classical swine fever in developing countries.

show abstract

Hog cholera virus: molecular composition of virions from a pestivirus

Cited by 328 publications

References 29 publications

Rearrangement of viral sequences in cytopathogenic pestiviruses

Rearrangement of viral sequences in cytopathogenic pestiviruses

Identification of a linear epitope on the capsid protein of classical swine fever virus

Rapid pre-clinical detection of classical swine fever by reverse transcription loop-mediated isothermal amplification

Contact Info

Product

Resources

About