Detection of the ORF3 polypeptide of feline calicivirus in infected cells and evidence for its expression from a single, functionally bicistronic, subgenomic mRNA

Herbert, Terence P.; Brierley, Ian; Brown, T. D. K.

doi:10.1099/0022-1317-77-1-123

Cited by 73 publications

(66 citation statements)

References 22 publications

(24 reference statements)

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“…The ORF3 product identified in this study had a similar molecular mass of 10 kD to that of 8 kD reported by Herbert et al [6]. ORF3 as a small ORF found in the extreme 3' end of the genome is common to all caliciviruses [3].…”

Section: Discussionsupporting

confidence: 54%

“…Antibody responses to the fusion proteins in an FCV-infected cat were different. The low antibody response to the ORF3 product may be a result of the expression level of ORF3, which suggested to be approximately 10% of ORF2 [6]. In contrast to the ORF3 product, the GST-PUR fusion protein showed relatively high immunogenicity in FCV-infected cats, suggesting that the fusion protein has a potential to be an antigen for a diagnostic test of FCV infection.…”

Section: Discussionmentioning

confidence: 88%

“…It was suggested that ORF2 and ORF3 are expressed from the 2.4 kb subgenomic RNA [6]. Antibody responses to the fusion proteins in an FCV-infected cat were different.…”

Section: Discussionmentioning

confidence: 99%

“…ORF1 was suggested to encode the non-structural proteins including an RNA-dependent RNA polymerase and a cysteine proteinase [8]. ORF2 encodes the capsid precursor protein [10,18] and ORF3 encodes a small protein of which function is unknown [6]. The capsid precursor protein with a molecular mass of 76 kilodaltons (kD) is processed to capsid protein (62 kD) immediately after translation [1].…”

mentioning

confidence: 99%

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Analysis of the N-Terminal Polypeptide of the Capsid Precursor Protein and the ORF3 Product of Feline Calicivirus.

Tohya

Shinchi

Matsuura

et al. 1999

The Journal of Veterinary Medical Science

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ABSTRACT. The N-terminal unique polypeptide region of the capsid precursor protein of feline calicivirus (FCV) and the protein encoded by ORF3 of FCV were expressed as fusion proteins with glutathione S-transferase to analyze the expressed products in FCV-infected cells. Immunoblot analysis using a serum from a cat experimentally infected with FCV indicated relatively high immunogenicity of the Nterminal polypeptide in FCV-infected cats, as compared with the ORF3 protein. Specific antisera were prepared by immunization to mice with the fused proteins and used in immunoblot analysis. A 14 kD product corresponding to the N-terminal polypeptide and a 10 kD polypeptide of the ORF3 product were identified in the FCV-infected cells but not detected in the purified particles. No neutralization activity against FCV was detected in these antisera. The proteins identified as polypeptides of 14 kD and 10 kD in this study may have functions as non-structural proteins.-KEY WORDS: capsid precursor protein, expression, feline calicivirus, glutathione S-transferase, immunogenicity.

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Section: Discussionsupporting

confidence: 54%

Section: Discussionmentioning

confidence: 88%

“…It was suggested that ORF2 and ORF3 are expressed from the 2.4 kb subgenomic RNA [6]. Antibody responses to the fusion proteins in an FCV-infected cat were different.…”

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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Analysis of the N-Terminal Polypeptide of the Capsid Precursor Protein and the ORF3 Product of Feline Calicivirus.

Tohya

Shinchi

Matsuura

et al. 1999

The Journal of Veterinary Medical Science

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“…ORF2 encodes a 705-residue protein (Mr. 78,701), a precursor of the mature capsid protein as deduced from the observed 67 kDa molecular mass of the major structural protein found in purified virions. ORF3 encodes a 110-residue protein possibly corresponding to a minor structural component of the virion as described for Feline calicivirus (FCV) (Herbert et al, 1996;Sosnovtsev and Green, 2000), Rabbit hemorrhagic disease virus (RHDV) (Wirblich et al, 1996) and Norwalk virus (Glass et al, 2000). A distinctive feature of the vesiviruses is the presence of a protease-polymerase bifunctional 3CD-like protein, which is not further processed to 3C-and 3D-like mature products (Sosnovtseva et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

Structural and functional analysis of virus factories purified from Rabbit vesivirus-infected Vero cells

et al. 2008

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a b s t r a c tRabbit vesivirus infection induces membrane modifications and accumulation of vesicular structures in the cytoplasm of infected Vero cells. Crude RaV replication complexes (RCs) have been purified and their structural and functional properties have been characterized. We show that calnexin, an ER-resident protein, RaV non-structural proteins 2AB-, 2C-, 3A-, 3B-and 3CD-like as well as viral RNAs co-localize within membranous structures which are able to replicate the endogenous RNA templates. The purified virus factories protected their viral RNA contents from microccocal nuclease degradation and were inaccessible to exogenously added synthetic transcripts. In addition, we have shown that RCs can be used to investigate uridylylation of native endogenous VPg. In contrast to the observation that the virus factories were inaccessible to RNAs, RCs were accessible to added recombinant VPg which was subsequently nucleotidylylated. Nevertheless no elongation of an RNA chain attached to native or recombinant VPg could be demonstrated.

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Structure and Molecular Virology

Anderson

Cheng

2005

Viral Hepatitis

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Detection of the ORF3 polypeptide of feline calicivirus in infected cells and evidence for its expression from a single, functionally bicistronic, subgenomic mRNA

Cited by 73 publications

References 22 publications

Analysis of the N-Terminal Polypeptide of the Capsid Precursor Protein and the ORF3 Product of Feline Calicivirus.

Analysis of the N-Terminal Polypeptide of the Capsid Precursor Protein and the ORF3 Product of Feline Calicivirus.

Structural and functional analysis of virus factories purified from Rabbit vesivirus-infected Vero cells

Structure and Molecular Virology

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