Literature DB >> 8488721

The amino terminal sequence of VP60 from rabbit hemorrhagic disease virus supports its putative subgenomic origin.

F Parra1, J A Boga, M S Marin, R Casais.   

Abstract

Direct determination of the amino acid sequence of VP60 from rabbit hemorrhagic disease virus is impeded by the presence of a blocked N-terminus. Chemical cleavage of VP60 using cyanogen bromide allowed the identification and purification of two oligopeptides showing identical amino acid composition, one of which had its amino terminus blocked. Automated sequential degradation of the unblocked CNBr- peptide yielded the amino acid sequence EGKARTAPQGEAA. This sequence is identical to the deduced amino acid sequence following the first AUG codon found at position +10 at the 5'-end of the 2.4 kb subgenomic mRNA. These data favor the hypothesis that this viral polypeptide is mainly produced from the subgenomic mRNA and not from the genomic RNA by processing of the putative polyprotein generated from the major open reading frame.

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Year:  1993        PMID： 8488721     DOI： 10.1016/0168-1702(93)90034-k

Source DB:  PubMed          Journal:  Virus Res        ISSN： 0168-1702            Impact factor:   3.303


  22 in total

1.  Detection of viral proteins after infection of cultured hepatocytes with rabbit hemorrhagic disease virus.

Authors:  M König; H J Thiel; G Meyers
Journal:  J Virol       Date:  1998-05       Impact factor: 5.103

2.  Genetic map of the calicivirus rabbit hemorrhagic disease virus as deduced from in vitro translation studies.

Authors:  C Wirblich; H J Thiel; G Meyers
Journal:  J Virol       Date:  1996-11       Impact factor: 5.103

3.  Structural requirements for the assembly of Norwalk virus-like particles.

Authors:  Andrea Bertolotti-Ciarlet; Laura J White; Rong Chen; B V Venkataram Prasad; Mary K Estes
Journal:  J Virol       Date:  2002-04       Impact factor: 5.103

4.  Two independent pathways of expression lead to self-assembly of the rabbit hemorrhagic disease virus capsid protein.

Authors:  M Sibilia; M B Boniotti; P Angoscini; L Capucci; C Rossi
Journal:  J Virol       Date:  1995-09       Impact factor: 5.103

5.  Recombinant rabbit hemorrhagic disease virus capsid protein expressed in baculovirus self-assembles into viruslike particles and induces protection.

Authors:  S Laurent; J F Vautherot; M F Madelaine; G Le Gall; D Rasschaert
Journal:  J Virol       Date:  1994-10       Impact factor: 5.103

6.  Feline calicivirus VP2 is essential for the production of infectious virions.

Authors:  Stanislav V Sosnovtsev; Gaël Belliot; Kyeong-Ok Chang; Oge Onwudiwe; Kim Y Green
Journal:  J Virol       Date:  2005-04       Impact factor: 5.103

7.  Immunization with potato plants expressing VP60 protein protects against rabbit hemorrhagic disease virus.

Authors:  S Castañón; M S Marín; J M Martín-Alonso; J A Boga; R Casais; J M Humara; R J Ordás; F Parra
Journal:  J Virol       Date:  1999-05       Impact factor: 5.103

8.  3C-like protease of rabbit hemorrhagic disease virus: identification of cleavage sites in the ORF1 polyprotein and analysis of cleavage specificity.

Authors:  C Wirblich; M Sibilia; M B Boniotti; C Rossi; H J Thiel; G Meyers
Journal:  J Virol       Date:  1995-11       Impact factor: 5.103

9.  Self-assembly, antigenicity, and immunogenicity of the rabbit haemorrhagic disease virus (Czechoslovakian strain V-351) capsid protein expressed in baculovirus.

Authors:  H S Nagesha; L F Wang; A D Hyatt; C J Morrissy; C Lenghaus; H A Westbury
Journal:  Arch Virol       Date:  1995       Impact factor: 2.574

10.  Identification and characterization of a 3C-like protease from rabbit hemorrhagic disease virus, a calicivirus.

Authors:  B Boniotti; C Wirblich; M Sibilia; G Meyers; H J Thiel; C Rossi
Journal:  J Virol       Date:  1994-10       Impact factor: 5.103
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