Cleavage of the Feline Calicivirus Capsid Precursor Is Mediated by a Virus-Encoded Proteinase

Sosnovtsev, Stanislav V.; Sosnovtseva, Svetlana A.; Green, Kim Y.

doi:10.1128/jvi.72.4.3051-3059.1998

Cited by 113 publications

(83 citation statements)

References 31 publications

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“…However, in another human pathogenic calicivirus, the sapovirus (SV), NS6 pro NS7 pol is the only protein detected in a cell-free system (Oka et al, 2005a,b). In the case of the pathogenic feline calicivirus (FCV), the NS6 pro NS7 pol precursor is detected in mammalian cells (Sosnovtsev et al, 2002(Sosnovtsev et al, , 1998Sosnovtseva et al, 1999). In accordance with our observations (Scheffler et al, 2007), evidence for autocatalytic cleavage of norovirus NS6 pro from the polyprotein precursor has been presented Liu et al, 1999;Seah et al, 1999;Sosnovtsev et al, 2006).…”

Section: The Viral Chymotrypsin-like Proteasesupporting

confidence: 87%

“…FCV has been used during the past two decades as a surrogate to investigate the replication strategy of the Caliciviridae. Many studies have brought insights into the replication of the vesivirus genome Green, 1995, 2000;Sosnovtsev et al, 2005Sosnovtsev et al, , 2003Sosnovtsev et al, , 1998Sosnovtseva et al, 1999). Lately, additional knowledge has been obtained from studies on the murine norovirus in RAW264.7 murine macrophages in vitro Wobus et al, 2004Wobus et al, , 2006.…”

Section: Multiplication Cycle Of the Caliciviridaementioning

confidence: 99%

“…In the noroviruses and vesiviruses, transcription of subgenomic RNA yields high amounts of structural proteins, the VP1 and VP2. In FCV, the VP1 is additionally cleaved by the viral protease releasing a leader protein (LC, leader of the capsid protein) and the capsid (Matsuura et al, 2000;Sosnovtsev et al, 1998). In the sapoviruses, lagoviruses and beco/naboviruses, the VP1 is released from the polyprotein precursor after processing by the viral protease.…”

Section: Multiplication Cycle Of the Caliciviridaementioning

confidence: 99%

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Antiviral strategies to control calicivirus infections

et al. 2010

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Caliciviridae are human or non-human pathogenic viruses with a high diversity. Some members of the Caliciviridae, i.e. human pathogenic norovirus or rabbit hemorrhagic disease virus (RHDV), are worldwide emerging pathogens. The norovirus is the major cause of viral gastroenteritis worldwide, accounting for about 85% of the outbreaks in Europe between 1995 and 2000. In the United States, 25 million cases of infection are reported each year. Since its emergence in 1984 as an agent of fatal hemorrhagic diseases in rabbits, RHDV has killed millions of rabbits and has been dispersed to all of the inhabitable continents. In view of their successful and apparently increasing emergence, the development of antiviral strategies to control infections due to these viral pathogens has now become an important issue in medicine and veterinary medicine. Antiviral strategies have to be based on an understanding of the epidemiology, transmission, clinical symptoms, viral replication and immunity to infection resulting from infection by these viruses. Here, we provide an overview of the mechanisms underlying calicivirus infection, focusing on the molecular aspects of replication in the host cell. Recent experimental data generated through an international collaboration on structural biology, virology and drug design within the European consortium VIZIER is also presented. Based on this analysis, we propose antiviral strategies that may significantly impact on the epidemiological characteristics of these highly successful viral pathogens.

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Section: The Viral Chymotrypsin-like Proteasesupporting

confidence: 87%

Section: Multiplication Cycle Of the Caliciviridaementioning

confidence: 99%

Section: Multiplication Cycle Of the Caliciviridaementioning

confidence: 99%

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Antiviral strategies to control calicivirus infections

et al. 2010

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“…Caliciviruses are small, non-enveloped viruses that are 27-38 nm in diameter and possess a single-stranded, plus-sense RNA genome of 7.3-8.3 kb in length and a major structural protein (Green et al, 2001;Sosnovtsev et al, 1998). The family Caliciviridae is classified into four genera: Norovirus (NoV), Sapovirus (SaV), Vesivirus and Lagovirus (Green et al, 2000) with a new proposed genus, Nebraska (NB)-like (Smiley et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

Molecular detection and characterization of unclassified bovine enteric caliciviruses in South Korea

Park¹,

Jeong²,

Park³

et al. 2008

Veterinary Microbiology

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The unclassified bovine enteric calicivirus (BEC) is a new bovine enteric calicivirus that is different from bovine norovirus, and causes diarrhea and pathologies in the small intestine of calves. This virus includes Nebraska (NB)- and Newbury agent 1 (NA1)-like strains. The prevalence of this BEC and its genetic characterization has only been reported in the UK and the USA. This study examined the prevalence and genetic diversity of these BECs in diarrheic calves in South Korea. Among a total of 645 diarrheic fecal specimens obtained from 629 cattle herds, these unclassified BECs were detected in 59 (9.1%) diarrheic fecal samples from 57 herds (9.3%) by either RT-PCR or nested PCR. Sequence and phylogenetic analyses of the partial RdRp gene showed that all the Korean BECs clustered together and were closely related to the NB-like viruses (80.9-88.1% nucleotide and 84.5-98.4% amino acid) but not to the NA1-like viruses (75.8-78.4% nucleotide and 79.7-82.8% amino acid). Although these viruses could not be classified into NA1- and NB-like viruses from the sequence and phylogenetic data of the entire capsid gene, all the Korean BECs clustered together on a branch separate from the other known BECs. These results show that these BEC infections are endemic in diarrheic calves in South Korea. The infecting strains are genetically closer to the NB-like viruses but have a distinct evolutionary pathway.

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“…The viral protease, encoded in ORF1, is initially synthesized as a part of the ORF1 polyprotein, and responsible for the cleavage among ORF1 proteins to generate functional non-structural proteins. This protease also functions to cleave an ORF2-encoded protein to generate the capsid protein VP1 (Clarke and Lambden, 2000;Sosnovtsev et al, 1998Sosnovtsev et al, , 2002. The FCV protease cleaves peptide bonds downstream of a specific glutamic acid (E) in the precursor protein (Green, 2007;Oka et al, 2009;Sosnovtsev et al, 1998Sosnovtsev et al, , 2002.…”

Section: Introductionmentioning

confidence: 99%

Bioluminescence technologies to detect calicivirus protease activity in cell-free system and in infected cells

et al. 2011

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Feline calicivirus (FCV) is an important veterinary pathogen and causes respiratory disease in cats. Because it grows well in cell culture, FCV is often used as a model virus of non-culturable caliciviruses. In this study, a cell-free and two cell culture-based biosensor assay systems were established to detect FCV protease activity. The assays utilize luciferase sensor technology or second-generation bioluminescence resonance energy transfer (BRET2). A luciferase sensor was designed to contain an FCV protease cleavage motif within the permutated luciferase (GloSensor). The BRET2-based probe contained the same cleavage motif flanked by a renilla luciferase and a variant of green fluorescent protein. To confirm the specificity of these assay systems, GloSensor or a BRET2-based probe containing a mutation in the cleavage motif was also constructed. In a cell-free assay, GloSensor showed increased luminescence in proportion to the amount of FCV protease, while no signal change was observed when the construct harboring the mutant cleavage motif was used. A feline cell line stably expressing GloSensor or the BRET2-based probe was established. Increased levels of GloSensor luminescence, and decreased levels of BRET2 signals were observed according to input FCV titers. In contrast, no significant signal change was observed in the cells stably expressing the mutant cleavage motif. GloSensor and the BRET2-based probe were capable of detecting the inhibitory activity of ribavirin in FCV-infected cells. Our results demonstrate that these biosensors are useful to detect FCV protease activity induced in infected cells, and well worth consideration for screening of anti-FCV protease compounds in cell-free system as well as anti-FCV compounds in cultured cells.

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Cleavage of the Feline Calicivirus Capsid Precursor Is Mediated by a Virus-Encoded Proteinase

Cited by 113 publications

References 31 publications

Antiviral strategies to control calicivirus infections

Antiviral strategies to control calicivirus infections

Molecular detection and characterization of unclassified bovine enteric caliciviruses in South Korea

Bioluminescence technologies to detect calicivirus protease activity in cell-free system and in infected cells

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