Identification and sequence determination of the capsid protein gene of feline calicivirus

Carter, M. J.; Milton, Ian D.; Turner, Philip C.; Meanger, Jayesh; Bennett, Malcolm J.; Gaskell, Rosalind M.

doi:10.1007/bf01317185

Cited by 78 publications

(50 citation statements)

References 20 publications

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“…The gene has also been expressed as a fl-galactosidase fusion protein in Escherichia coli. The purified protein is immunogenic in mice, and reacts with feline antisera (Carter et al, 1992). We have also reported the production of two MAbs specific for the virus capsid .…”

confidence: 92%

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Location of monoclonal antibody binding sites in the capsid protein of feline calicivirus

Milton¹,

Turner

Teelan³

et al. 1992

Journal of General Virology

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confidence: 92%

“…prepared as a PstI-EcoRI fragment from clone pFC42. The derivation and sequencing of this clone have been described (Carter, t990;Carter et al, 1992). This fragment does not contain the entire gene for the protein precursor, but does include all sequences expressed in the mature protein (Carter et al, 1992).…”

confidence: 99%

Location of monoclonal antibody binding sites in the capsid protein of feline calicivirus

Milton¹,

Turner

Teelan³

et al. 1992

Journal of General Virology

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“…Variable region E is known to contain the major B-cell epitopes [32,86,110] and its variability has been used as the basis of sequence-based methods to differentiate between strains [84,105]. Region A is cleaved to produce the mature capsid protein [10,102]. ORF 3 encodes for a minor structural protein [103].…”

Section: Aetiologymentioning

confidence: 99%

Feline calicivirus

et al. 2007

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-Feline calicivirus (FCV) is an important and highly prevalent pathogen of cats. It belongs to the family Caliciviridae which includes other significant pathogens of man and animals. As an RNA virus, high polymerase error rates convey upon FCV a high genome plasticity, and allow the virus to respond rapidly to environmental selection pressures. This makes the virus very adaptable and has important implications for clinical disease and its control. Being genetically diverse, FCV is associated with a range of clinical syndromes from inapparent infections to relatively mild oral and upper respiratory tract disease with or without acute lameness. More recently, highly virulent forms of the virus have emerged associated with a systemic infection that is frequently fatal. A proportion of FCV infected cats that recover from acute disease, remain persistently infected. In such cats, virus evolution is believed to help the virus to evade the host immune response. Such longterm carriers may only represent a minority of the feline population but are likely to be crucial to the epidemiology of the virus. Vaccination against FCV has been available for many years and has effectively reduced the incidence of clinical disease. However, the vaccines do not prevent infection and vaccinated cats can still become persistently infected. In addition, FCV strain variability means that not all strains are protected against equally. Much progress has been made in understanding the biology and pathogenesis of this important feline virus. Challenges for the future will necessarily focus on how to control the variability of this virus particularly in relation to emerging virulent strains and vaccination.

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“…A genetic feature unique to members of the genus Vesivirus is expression of the major capsid protein from ORF2 as a precursor protein (5,(18)(19)(20). This precursor is processed in trans by the viral protease to release two proteins: the leader of the capsid (LC) and the mature capsid protein (VP1) (5,19,21,22). The function of the LC protein is not clear, but cleavage of the precursor to release LC and VP1 is essential for the recovery of infectious virions (5).…”

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confidence: 99%

“…The genomic RNA serves as a template for translation of the ORF1 polyprotein that is proteolytically cleaved by the viral protease to release the nonstructural proteins (16,17), and an ϳ2.2-to 2.6-kb subgenomic bicistronic RNA template is used for the translation of VP1 and VP2 (7,18). A genetic feature unique to members of the genus Vesivirus is expression of the major capsid protein from ORF2 as a precursor protein (5,(18)(19)(20). This precursor is processed in trans by the viral protease to release two proteins: the leader of the capsid (LC) and the mature capsid protein (VP1) (5,19,21,22).…”

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confidence: 99%

The Feline Calicivirus Leader of the Capsid Protein Is Associated with Cytopathic Effect

Abente

Sosnovtsev

Sandoval-Jaime

et al. 2013

J Virol

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Open reading frame 2 (ORF2) of the feline calicivirus (FCV) genome encodes a capsid precursor that is posttranslationally processed to release the mature capsid protein (VP1) and a small protein of 124 amino acids, designated the leader of the capsid (LC). To investigate the role of the LC protein in the virus life cycle, mutations and deletions were introduced into the LC coding region of an infectious FCV cDNA clone. Three cysteine residues that are conserved among all vesivirus LC sequences were found to be critical for the recovery of FCV with a characteristic cytopathic effect in feline kidney cells. A cell-rounding phenotype associated with the transient expression of wild-type and mutagenized forms of the LC correlated with the cytopathic and growth properties of the corresponding engineered viruses. The host cellular protein annexin A2 was identified as a binding partner of the LC protein, consistent with a role for the LC in mediating host cell interactions that alter the integrity of the cell and enable virus spread.M embers of the family Caliciviridae are small nonenveloped viruses that contain a positive-sense single-stranded RNA genome. Feline calicivirus (FCV) is in the genus Vesivirus of the family and has been an important model for studying calicivirus replication because it grows efficiently in cell culture and has a reverse genetics system (1-5). The RNA genomes of caliciviruses range in size from ϳ6.7 to 8.5 kb and typically encode 8 or 9 viral proteins from two (Sapovirus, Nebovirus, and Lagovirus) or three (Norovirus and Vesivirus) open reading frames (ORFs). A unique ORF4 in the murine norovirus genome that encodes a protein reported to downregulate the innate immune response has been identified (6). The 5= end of the viral RNA genome is covalently linked to a VPg protein; the 3= end of the genome is polyadenylated (2, 7-9). The infectious virion is composed of 180 copies of the major capsid protein VP1 and 1 to 10 copies of the minor structural protein VP2, which together form a capsid around the VPg-linked genome (10-15). The genomic RNA serves as a template for translation of the ORF1 polyprotein that is proteolytically cleaved by the viral protease to release the nonstructural proteins (16,17), and an ϳ2.2-to 2.6-kb subgenomic bicistronic RNA template is used for the translation of VP1 and VP2 (7, 18). A genetic feature unique to members of the genus Vesivirus is expression of the major capsid protein from ORF2 as a precursor protein (5,(18)(19)(20). This precursor is processed in trans by the viral protease to release two proteins: the leader of the capsid (LC) and the mature capsid protein (VP1) (5,19,21,22). The function of the LC protein is not clear, but cleavage of the precursor to release LC and VP1 is essential for the recovery of infectious virions (5). Transient expression of the LC was reported to enhance replication of a human norovirus RNA replicon (23), and an increase in the level of mRNA for the low-density lipoprotein receptor (LDLR) was observed (24). We showed previo...

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Identification and sequence determination of the capsid protein gene of feline calicivirus

Cited by 78 publications

References 20 publications

Location of monoclonal antibody binding sites in the capsid protein of feline calicivirus

Location of monoclonal antibody binding sites in the capsid protein of feline calicivirus

Feline calicivirus

The Feline Calicivirus Leader of the Capsid Protein Is Associated with Cytopathic Effect

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