E. M. Abu-elzein and A. I. Afaleq, Rabbit haemorrhagic disease in Saudi Arabia, Vet Rec, vol.144, pp.480-481, 1999.

R. Aldabe, A. Irurzun, and L. Carrasco, Poliovirus protein 2BC increases cytosolic free calcium concentrations, J Virol, vol.71, pp.6214-6217, 1997.

M. Allaire, M. M. Chernaia, B. A. Malcolm, and M. N. James, Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases, Nature, vol.369, pp.72-76, 1994.

C. Alonso, J. M. Oviedo, J. M. Martin-alonso, E. Diaz, J. A. B-oga et al., Programmed cell death in the pathogenesis of rabbit hemorrhagic disease, Arch Virol, vol.143, pp.321-332, 1998.

A. Villares and J. L. , Viral haemorrhagic disease of rabbits: vaccination and immune response, Rev Sci Tech, vol.10, pp.459-480, 1991.

S. Asgari, J. R. Hardy, R. G. Sinclair, and B. D. Cooke, Field evidence for mechanical transmission of rabbit haemorrhagic disease virus (RHDV) by flies (Diptera:Calliphoridae) among wild rabbits in Australia, Virus Res, vol.54, pp.123-132, 1998.

J. M. Ball, D. Y. Graham, A. R. Opekun, M. A. Gilger, R. A. Guerrero et al., Recombinant Norwalk virus-like particles given orally to volunteers: phase I study, Gastroenterology, vol.117, pp.40-48, 1999.

A. Barco, E. Feduchi, and L. Carrasco, Poliovirus protease 3C(pro) kills cells by apoptosis, Virology, vol.266, pp.352-360, 2000.

R. Bartenschlager, L. Ahlborn-laake, J. Mous, and H. Jacobsen, Kinetic and structural analyses of hepatitis C virus polyprotein processing, J Virol, vol.68, pp.5045-5055, 1994.

J. F. Bazan and R. J. Fletterick, Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: structural and functional implications, Proc Natl Acad Sci U S A, vol.85, pp.7872-7876, 1988.

A. B. Becker and R. A. Roth, An unusual active site identified in a family of zinc metalloendopeptidases, Proc Natl Acad Sci U S A, vol.89, pp.3835-3839, 1992.

G. J. Belsham, G. M. Mcinerney, and N. Ross-smith, Foot-and-mouth disease virus 3C protease induces cleavage of translation initiation factors eIF4A and eIF4G within infected cells, J Virol, vol.74, pp.272-280, 2000.

T. Berke, B. Golding, X. Jiang, D. W. Cubitt, M. Wolfaardt et al., Phylogenetic analysis of the Caliciviruses, J Med Virol, vol.52, pp.419-424, 1997.

S. Bertagnoli, J. Gelfi, G. Le-gall, E. Boilletot, J. F. Vautherot et al., Protection against myxomatosis and rabbit viral hemorrhagic disease with recombinant myxoma viruses expressing rabbit hemorrhagic disease virus capsid protein, J Virol, vol.70, pp.5061-5066, 1996.
URL : https://hal.archives-ouvertes.fr/hal-02696622

W. S. Blair, X. Li, and B. L. Semler, A cellular cofactor facilitates efficient 3CD cleavage of the poliovirus P1 precursor, J Virol, vol.67, pp.2336-2343, 1993.

W. S. Blair and B. L. Semler, Role for the P4 amino acid residue in substrate utilization by the poliovirus 3CD proteinase, J Virol, vol.65, pp.6111-6123, 1991.

B. Boniotti, C. Wirblich, M. Sibilia, G. Meyers, H. J. Thiel et al., Identification and characterization of a 3C-like protease from rabbit hemorrhagic disease virus, a calicivirus, J Virol, vol.68, pp.6487-6495, 1994.

A. Bouslama, G. M. De-mia, S. Hammami, T. Aouina, H. Soussi et al., Identification of the virus of rabbit haemorrhagic disease in Tunisia, Vet Rec, vol.138, pp.108-110, 1996.

D. W. Bradley, Enterically-transmitted non-A, non-B hepatitis, Br Med Bull, vol.46, pp.442-461, 1990.

J. N. Burroughs and F. Brown, Presence of a covalently linked protein on calicivirus RNA, J Gen Virol, vol.41, pp.443-446, 1978.

J. N. Burroughs, T. R. Doel, C. J. Smale, and F. Brown, A model for vesicular exanthema virus, the prototype of the calicivirus group, J Gen Virol, vol.40, pp.161-174, 1978.

N. Burroughs, T. Doel, and F. Brown, Relationship of San Miguel sea lion virus to other members of the calicivirus group, Intervirology, vol.10, pp.51-59, 1978.

A. Cahour, B. Falgout, and C. J. Lai, Cleavage of the dengue virus polyprotein at the NS3/NS4A and NS4B/NS5 junctions is mediated by viral protease NS2B-NS3, whereas NS4A/NS4B may be processed by a cellular protease, J Virol, vol.66, pp.1535-1542, 1992.

F. M. Cancellotti and M. Renzi, Epidemiology and current situation of viral haemorrhagic disease of rabbits and the European brown hare syndrome in Italy, Rev Sci Tech, vol.10, pp.409-422, 1991.

L. Capucci, F. Fallacara, S. Grazioli, A. Lavazza, M. L. Pacciarini et al., A further step in the evolution of rabbit hemorrhagic disease virus: the appearance of the first consistent antigenic variant, Virus Res, vol.58, pp.115-126, 1998.

L. Capucci, P. Fusi, A. Lavazza, M. L. Pacciarini, and C. Rossi, Detection and preliminary characterization of a new rabbit calicivirus related to rabbit hemorrhagic disease virus but nonpathogenic, J Virol, vol.70, pp.8614-8623, 1996.

J. A. Carman, M. G. Garner, M. G. Catton, S. Thomas, H. A. Westbury et al., Viral haemorrhagic disease of rabbits and human health, Epidemiol Infect, vol.121, pp.409-418, 1998.

M. J. Carter, Transcription of feline calicivirus RNA, Arch Virol, vol.114, pp.143-152, 1990.

M. J. Carter, I. D. Milton, J. Meanger, M. Bennett, R. M. Gaskell et al., The complete nucleotide sequence of a feline calicivirus, Virology, vol.190, pp.443-448, 1992.

L. Casciola-rosen, A. Rosen, M. Petri, and M. Schlissel, Surface blebs on apoptotic cells are sites of enhanced procoagulant activity: implications for coagulation events and antigenic spread in systemic lupus erythematosus, Proc Natl Acad Sci, pp.1624-1629, 1996.

S. Castañon, M. S. Marín, J. M. Martín-alonso, J. A. Boga, R. Casais et al., Immunization with potato plants expressing VP60 protein protects against rabbit hemorrhagic disease virus, J Virol, vol.73, pp.4452-4455, 1999.

T. J. Chambers, A. Nestorowicz, S. M. Amberg, and C. M. Rice, Mutagenesis of the yellow fever virus NS2B protein: effects on proteolytic processing, NS2B-NS3 complex formation, and viral replication, J Virol, vol.67, pp.6797-6807, 1993.

I. N. Clarke and P. R. Lambden, The molecular biology of caliciviruses, J Gen Virol, vol.78, pp.291-301, 1997.

P. M. Collery, J. Mooney, M. O'conner, and N. Nowotny, Rabbit haemorrhagic disease in Ireland, Vet Rec, vol.137, p.547, 1995.

P. D. Cooper, V. I. Agol, H. L. Bachrach, F. Brown, Y. Ghendon et al., Picornaviridae: Second Report. Intervirology, vol.10, p.165, 1978.

W. D. Cubitt and A. D. Barrett, Propagation and preliminary characterization of a chicken candidate calicivirus, J Gen Virol, vol.66, pp.1431-1438, 1985.

S. Dawson, F. Mcardle, D. Bennett, S. D. Carter, M. Bennett et al., Investigation of vaccine reactions and breakdowns after feline calicivirus vaccination, 1993.

, Vet Rec, vol.132, pp.346-350

B. Delmas, D. Rasschaert, M. Godet, J. Gelfi, and H. Laude, Four major antigenic sites of the coronavirus transmissible gastroenteritis virus are located on the amino-terminal half of spike glycoprotein S, J Gen Virol, vol.71, pp.1313-1323, 1990.
URL : https://hal.archives-ouvertes.fr/hal-02709175

K. E. Dingle, P. R. Lambden, E. O. Caul, and I. N. Clarke, Human enteric Caliciviridae: the complete genome sequence and expression of virus-like particles from a genetic group II small round structured virus, J Gen Virol, vol.76, pp.2349-2355, 1995.

M. L. Donnelly, D. Gani, M. Flint, S. Monaghan, and M. D. Ryan, The cleavage activities of aphthovirus and cardiovirus 2A proteins, J Gen Virol, vol.78, pp.13-21, 1997.

W. G. Dougherty and B. L. Semler, Expression of virus-encoded proteinases: functional and structural similarities with cellular enzymes, Microbiol Rev, vol.57, pp.781-822, 1993.

W. J. Dower, J. F. Miller, and C. W. Ragsdale, High efficiency transformation of E. coli by high voltage electroporation, Nucleic Acids Res, vol.16, pp.6127-6145, 1988.

D. M. Dunham, X. Jiang, T. Berke, A. W. Smith, and D. O. Matson, Genomic mapping of a calicivirus VPg, Arch Virol, vol.143, pp.2421-2430, 1998.

D. W. Ehresmann and F. L. Schaffer, RNA synthesized in calicivirus-infected cells is atypical of picornaviruses, J Virol, vol.22, pp.572-576, 1977.

D. W. Ehresmann and F. L. Schaffer, Calicivirus intracellular RNA: fractionation of 18-22 s RNA and lack of typical 5'-methylated caps on 36 S and 22 S San Miguel sea lion virus RNAs, Virology, vol.95, pp.251-255, 1979.

C. Failla, L. Tomei, and R. De-francesco, Both NS3 and NS4A are required for proteolytic processing of hepatitis C virus nonstructural proteins, J Virol, vol.68, pp.3753-3760, 1994.

C. Failla, L. Tomei, and R. De-francesco, An amino-terminal domain of the hepatitis C virus NS3 protease is essential for interaction with NS4A, J Virol, vol.69, pp.1769-1777, 1995.

B. Falgout and L. Markoff, Evidence that flavivirus NS1-NS2A cleavage is mediated by a membrane-bound host protease in the endoplasmic reticulum, J Virol, vol.69, pp.7232-7243, 1995.

B. Falgout, R. H. Miller, and C. J. Lai, Deletion analysis of dengue virus type 4 nonstructural protein NS2B: identification of a domain required for NS2B-NS3 protease activity, J Virol, vol.67, pp.2034-2042, 1993.

B. Falgout, M. Pethel, Y. M. Zhang, and C. J. Lai, Both nonstructural proteins NS2B and NS3 are required for the proteolytic processing of dengue virus nonstructural proteins, J Virol, vol.65, pp.2467-2475, 1991.

M. M. Falk, F. Sobrino, and E. Beck, VPg gene amplification correlates with infective particle formation in foot-and-mouth disease virus, J Virol, vol.66, pp.2251-2260, 1992.

L. B. Fastier, A new feline virus isolated in tissue culture, Am J Vet Res, vol.18, pp.382-389, 1957.

F. Fenner, Classification and nomenclature of viruses, Intervirology, vol.7, pp.1-116, 1976.

W. T. Flynn, L. J. Saif, and P. D. Moorhead, Pathogenesis of porcine enteric calicivirus-like virus in four-day-old gnotobiotic pigs, Am J Vet Res, vol.49, pp.819-825, 1988.

M. Fretz and F. L. Schaffer, Calicivirus proteins in infected cells: evidence for a capsid polypeptide precursor, Virology, vol.89, pp.318-321, 1978.

K. Frolich, F. Klima, and J. Dedek, Antibodies against rabbit hemorrhagic disease virus in free-ranging red foxes from Germany, J Wildl Dis, vol.34, pp.436-442, 1998.

T. R. Fuerst, E. G. Niles, F. W. Studier, and B. Moss, Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase, Proc Natl Acad Sci U S A, vol.83, pp.8122-8126, 1986.

H. E. Fuller, D. Chasey, M. H. Lucas, and J. C. Gibbens, Rabbit haemorrhagic disease in the United Kingdom, Vet Rec, vol.133, pp.611-613, 1993.

A. V. Gamarnik and R. Andino, Switch from translation to RNA replication in a positivestranded RNA virus, Genes Dev, vol.12, pp.2293-2304, 1998.

C. J. Gaskell, Feline Medicine and Therapeutics, pp.257-270, 1985.

K. Geissler, C. R. Parrish, K. Schneider, and U. Truyen, Feline calicivirus capsid protein expression and self-assembly in cultured feline cells, 1999.

, Vet Microbiol, vol.69, pp.63-66

A. E. Gorbalenya, A. P. Donchenko, V. M. Blinov, and E. V. Koonin, Cysteine proteases of positive strand RNA viruses and chymotrypsin-like serine proteases. A distinct protein superfamily with a common structural fold, 1989.

, FEBS Lett, vol.243, pp.103-114

A. E. Gorbalenya, A. P. Donchenko, E. V. Koonin, and V. M. Blinov, N-terminal domains of putative helicases of flavi-and pestiviruses may be serine proteases, Nucleic Acids Res, vol.17, pp.3889-3897, 1989.

R. Gosert, G. Dollenmaier, and M. Weitz, Identification of active-site residues in protease 3C of hepatitis A virus by site-directed mutagenesis, J Virol, vol.71, pp.3062-3068, 1997.

A. Grakoui, D. W. Mccourt, C. Wychowski, S. M. Feinstone, and C. M. Rice, Characterization of the hepatitis C virus-encoded serine proteinase: determination of proteinase-dependent polyprotein cleavage sites, J Virol, vol.67, pp.2832-2843, 1993.

A. Grakoui, D. W. Mccourt, C. Wychowski, S. M. Feinstone, and C. M. Rice, A second hepatitis C virus-encoded proteinase, Proc Natl Acad Sci U S A, vol.90, pp.10583-10587, 1993.

C. W. Grassmann, O. Isken, and S. E. Behrens, Assignment of the multifunctional NS3 protein of bovine viral diarrhea virus during RNA replication: an in vivo and in vitro study, J Virol, vol.73, pp.9196-9205, 1999.

E. W. Greeno, R. R. Bach, and C. F. Moldow, Apoptosis is associated with increased cell surface tissue factor procoagulant activity, Lab Invest, vol.75, pp.281-289, 1996.

M. J. Grubman, M. Zellner, G. Bablanian, P. W. Mason, and M. E. Piccone, Identification of the active-site residues of the 3C proteinase of foot-and-mouth disease virus, Virology, vol.213, pp.581-589, 1995.

A. Guarne, J. Tormo, R. Kirchweger, D. Pfistermueller, I. Fita et al., Structure of the foot-and-mouth disease virus leader protease: a papain-like fold adapted for selfprocessing and eIF4G recognition, Embo J, vol.17, pp.7469-7479, 1998.

C. Guittre, N. Ruvoen-clouet, L. Barraud, Y. Cherel, I. Baginski et al., Early stages of rabbit haemorrhagic disease virus infection monitored by polymerase chain reaction, vol.1, pp.109-118

M. Guo, K. O. Chang, M. E. Hardy, Q. Zhang, A. V. Parwani et al., Molecular characterization of a porcine enteric calicivirus genetically related to sapporo-like human caliciviruses, 1999.

, J Virol, vol.73, pp.9625-9631

H. Hahn and A. C. Palmenberg, Mutational analysis of the encephalomyocarditis virus primary cleavage, J Virol, vol.70, pp.6870-6875, 1996.

D. J. Hall and A. C. Palmenberg, Mengo virus 3C proteinase: recombinant expression, intergenus substrate cleavage and localization in vivo, Virus Genes, vol.13, pp.99-110, 1996.

D. A. Harbour, P. E. Howard, and R. M. Gaskell, Isolation of feline calicivirus and feline herpesvirus from domestic cats 1980 to 1989, Vet Rec, vol.128, pp.77-80, 1991.

K. S. Harris, S. R. Reddigari, M. J. Nicklin, T. Hammerle, and E. Wimmer, Purification and characterization of poliovirus polypeptide 3CD, a proteinase and a precursor for RNA polymerase, J Virol, vol.66, pp.7481-7489, 1992.

K. S. Harris, W. Xiang, L. Alexander, W. S. Lane, A. V. Paul et al., Interaction of poliovirus polypeptide 3CDpro with the 5' and 3' termini of the poliovirus genome. Identification of viral and cellular cofactors needed for efficient binding, J Biol Chem, vol.269, pp.27004-27014, 1994.

M. Hashimoto, F. Roerink, Y. Tohya, and M. Mochizuki, Genetic analysis of the RNA polymerase gene of caliciviruses from dogs and cats, J Vet Med Sci, vol.61, pp.603-608, 1999.

A. Heneidi-zeckua, C. Zepeda-sein, A. Mateos-poumian, and G. Velazquez, , 1997.

, Rev Sci Tech, vol.16, pp.91-103

T. P. Herbert, I. Brierley, and T. D. Brown, Detection of the ORF3 polypeptide of feline calicivirus in infected cells and evidence for its expression from a single, functionally bicistronic, subgenomic mRNA, J Gen Virol, vol.77, pp.123-127, 1996.

T. P. Herbert, I. Brierley, and T. D. Brown, Identification of a protein linked to the genomic and subgenomic mRNAs of feline calicivirus and its role in translation, J Gen Virol, vol.78, pp.1033-1040, 1997.

M. Hijikata, N. Kato, Y. Ootsuyama, M. Nakagawa, and K. Shimotohno, Gene mapping of the putative structural region of the hepatitis C virus genome by in vitro processing analysis, Proc Natl Acad Sci U S A, vol.88, pp.5547-5551, 1991.

M. Hijikata, H. Mizushima, T. Akagi, S. Mori, N. Kakiuchi et al., Two distinct proteinase activities required for the processing of a putative nonstructural precursor protein of hepatitis C virus, J Virol, vol.67, pp.4665-4675, 1993.

T. Hohdatsu, K. Sato, T. Tajima, and H. Koyama, Neutralizing feature of commercially available feline calicivirus (FCV) vaccine immune sera against FCV field isolates, J Vet Med Sci, vol.61, pp.299-301, 1999.

C. Holden, Rabbit biocontrol project in disarray, Science, vol.270, p.1123, 1995.

E. A. Hoover and D. E. Kahn, Experimentally induced feline calicivirus infection: clinical signs and lesions, J Am Vet Med Assoc, vol.166, pp.463-468, 1975.

H. B. Huang, Vaccination against and immune response to viral haemorrhagic disease of rabbits: a review of research in the People's Republic of China, Rev Sci Tech, vol.10, pp.481-498, 1991.

L. R. Jan, C. S. Yang, D. W. Trent, B. Falgout, and C. J. Lai, Processing of Japanese encephalitis virus non-structural proteins: NS2B-NS3 complex and heterologous proteases, J Gen Virol, vol.76, pp.573-580, 1995.

X. Y. Jia, D. F. Summers, and E. Ehrenfeld, Primary cleavage of the HAV capsid protein precursor in the middle of the proposed 2A coding region, Virology, vol.193, pp.515-519, 1993.

X. Jiang, W. D. Cubitt, T. Berke, W. Zhong, X. Dai et al., Sapporo-like human caliciviruses are genetically and antigenically diverse, Arch Virol, vol.142, pp.1813-1827, 1997.

X. Jiang, D. O. Matson, G. M. Ruiz-palacios, J. Hu, J. Treanor et al., Expression, self-assembly, and antigenicity of a snow mountain agent-like calicivirus capsid protein, J Clin Microbiol, vol.33, pp.1452-1455, 1995.

X. Jiang, M. Wang, K. Wang, and M. K. Estes, Sequence and genomic organization of Norwalk virus, Virology, vol.195, pp.51-61, 1993.

M. Joachims, K. S. Harris, and D. Etchison, Poliovirus protease 3C mediates cleavage of microtubule-associated protein 4, Virology, vol.211, pp.451-461, 1995.

J. Jore, B. De-geus, R. J. Jackson, P. H. Pouwels, and B. E. Enger-valk, Poliovirus protein 3CD is the active protease for processing of the precursor protein P1 in vitro, J Gen Virol, vol.69, pp.1627-1636, 1988.

K. Kadoi, M. Kiryu, M. Iwabuchi, H. Kamata, M. Yukawa et al., A strain of calicivirus isolated from lions with vesicular lesions on tongue and snout, New Microbiol, vol.20, pp.141-148, 1997.

T. Kawaguchi, K. Nomura, Y. Hirayama, and T. Kitagawa, Establishment and characterization of a chicken hepatocellular carcinoma cell line, LMH, Cancer Res, vol.47, pp.4460-4464, 1987.

K. M. Kean, M. T. Howell, S. Grunert, M. Girard, and R. J. Jackson, Substitution mutations at the putative catalytic triad of the poliovirus 3C protease have differential effects on cleavage at different sites, Virology, vol.194, pp.360-364, 1993.

R. Kirchweger, E. Ziegler, B. J. Lamphear, D. Waters, H. D. Liebig et al., Foot-and-mouth disease virus leader proteinase: purification of the Lb form and determination of its cleavage site on eIF-4 gamma, J Virol, vol.68, pp.5677-5684, 1994.

M. König, H. J. Thiel, and G. Meyers, Detection of viral proteins after infection of cultured hepatocytes with rabbit hemorrhagic disease virus, J Virol, vol.72, pp.4492-4497, 1998.

E. V. Koonin, A. E. Gorbalenya, M. A. Purdy, M. N. Rozanov, G. R. Reyes et al., Computer-assisted assignment of functional domains in the nonstructural polyprotein of hepatitis E virus: delineation of an additional group of positive-strand RNA plant and animal viruses, Proc Natl Acad Sci U S A, vol.89, pp.8259-8263, 1992.

M. Kpodekon and T. Alogninouwa, Control of rabbit viral haemorrhagic disease in Benin by vaccination, Vet Rec, vol.143, pp.693-694, 1998.

L. C. Kreutz and B. S. Seal, The pathway of feline calicivirus entry, Virus Res, vol.35, pp.63-70, 1995.

L. C. Kreutz, B. S. Seal, and W. L. Mengeling, Early interaction of feline calicivirus with cells in culture, Arch Virol, vol.136, pp.19-34, 1994.

Y. Kusov and V. Gauss-muller, Improving proteolytic cleavage at the 3A/3B site of the hepatitis A virus polyprotein impairs processing and particle formation, and the impairment can be complemented in trans by 3AB and 3ABC, J Virol, vol.73, pp.9867-9878, 1999.

U. K. Laemmli, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature, vol.227, pp.680-685, 1970.

P. R. Lambden, E. O. Caul, C. R. Ashley, and I. N. Clarke, Sequence and genome organization of a human small round-structured (Norwalk-like) virus, Science, vol.259, pp.516-519, 1993.

P. R. Lambden, B. Liu, and I. N. Clarke, A conserved sequence motif at the 5' terminus of the Southampton virus genome is characteristic of the Caliciviridae, Virus Genes, vol.10, pp.149-152, 1995.

S. Laurent, J. F. Vautherot, L. Gall, G. Madelaine, M. F. Rasschaert et al., Structural, antigenic and immunogenic relationships between European brown hare syndrome virus and rabbit haemorrhagic disease virus, J Gen Virol, vol.78, pp.2803-2811, 1997.
URL : https://hal.archives-ouvertes.fr/hal-02695175

S. Laurent, J. F. Vautherot, M. F. Madelaine, L. Gall, G. Rasschaert et al., Recombinant rabbit hemorrhagic disease virus capsid protein expressed in baculovirus self-assembles into viruslike particles and induces protection, J Virol, vol.68, pp.6794-6798, 1994.
URL : https://hal.archives-ouvertes.fr/hal-02710464

A. Lavazza, M. T. Scicluna, and L. Capucci, Susceptibility of hares and rabbits to the European brown hare syndrome virus (EBHSV) and rabbit haemorrhagic disease virus (RHDV) under experimental conditions, vol.43, pp.401-410, 1996.

M. A. Lawson and B. L. Semler, Picornavirus protein processing--enzymes, substrates, and genetic regulation, Curr Top Microbiol Immunol, vol.161, pp.49-87, 1990.

L. Gall, G. Arnauld, C. Boilletot, E. Morisse, J. P. Rasschaert et al., Molecular epidemiology of rabbit haemorrhagic disease virus outbreaks in France during 1988 to 1995, J Gen Virol, vol.79, pp.11-16, 1998.
URL : https://hal.archives-ouvertes.fr/hal-02689092

L. Gall, G. Huguet, S. Vende, P. Vautherot, J. F. Rasschaert et al., European brown hare syndrome virus: molecular cloning and sequencing of the genome, J Gen Virol, vol.77, pp.1693-1697, 1996.
URL : https://hal.archives-ouvertes.fr/hal-02686455

A. M. Lesk and W. D. Fordham, Conservation and variability in the structures of serine proteinases of the chymotrypsin family, J Mol Biol, vol.258, pp.501-537, 1996.

H. Li, S. Clum, S. You, K. E. Ebner, and R. Padmanabhan, The serine protease and RNAstimulated nucleoside triphosphatase and RNA helicase functional domains of dengue virus type 2 NS3 converge within a region of 20 amino acids, J Virol, vol.73, pp.3108-3116, 1999.

C. Lin, T. J. Chambers, and C. M. Rice, Mutagenesis of conserved residues at the yellow fever virus 3/4A and 4B/5 dibasic cleavage sites: effects on cleavage efficiency and polyprotein processing, Virology, vol.192, pp.596-604, 1993.

B. Liu, I. N. Clarke, E. O. Caul, and P. R. Lambden, The genomic 5' terminus of Manchester calicivirus, Virus Genes, vol.15, pp.25-28, 1997.

B. Liu, I. N. Clarke, and P. R. Lambden, Polyprotein processing in Southampton virus: identification of 3C-like protease cleavage sites by in vitro mutagenesis, J Virol, vol.70, pp.2605-2610, 1996.

B. L. Liu, I. N. Clarke, E. O. Caul, and P. R. Lambden, Human enteric caliciviruses have a unique genome structure and are distinct from the Norwalk-like viruses, Arch Virol, vol.140, pp.1345-1356, 1995.

B. L. Liu, P. R. Lambden, H. Gunther, P. Otto, M. Elschner et al., Molecular characterization of a bovine enteric calicivirus: relationship to the Norwalk-like viruses, J Virol, vol.73, pp.819-825, 1999.

B. L. Liu, G. J. Viljoen, I. N. Clarke, and P. R. Lambden, Identification of further proteolytic cleavage sites in the Southampton calicivirus polyprotein by expression of the viral protease in E. coli, J Gen Virol, vol.80, pp.291-296, 1999.

S. J. Liu, H. P. Xue, B. Q. Pu, and N. H. Qian, A new viral disease in rabbits, Anim. Husb. Vet. Med, vol.16, pp.253-255, 1984.

M. Lobigs, Proteolytic processing of a Murray Valley encephalitis virus non-structural polyprotein segment containing the viral proteinase: accumulation of a NS3-4A precursor which requires mature NS3 for efficient processing, J Gen Virol, vol.73, pp.2305-2312, 1992.

G. G. Long, J. F. Evermann, and J. R. Gorham, Naturally occurring picornavirus infection of domestic mink, Can J Comp Med, vol.44, pp.412-417, 1980.

I. W. Lugton, A cross-sectional study of risk factors affecting the outcome of rabbit haemorrhagic disease virus releases in New South Wales, Aust Vet J, vol.77, pp.322-328, 1999.

M. Alonso, J. M. Casais, R. Boga, J. A. Parra, and F. , Processing of rabbit hemorrhagic disease virus polyprotein, J Virol, vol.70, pp.1261-1265, 1996.

D. O. Matson, T. Berke, M. B. Dinulos, E. Poet, W. M. Zhong et al., Partial characterization of the genome of nine animal caliciviruses, Arch Virol, vol.141, pp.2443-2456, 1996.

D. O. Matson, W. M. Zhong, S. Nakata, K. Numata, X. Jiang et al., Molecular characterization of a human calicivirus with sequence relationships closer to animal caliciviruses than other known human caliciviruses, J Med Virol, vol.45, pp.215-222, 1995.

Y. Matsuura, Y. Tohya, M. Onuma, F. Roerink, M. Mochizuki et al., Expression and processing of the canine calicivirus capsid precursor, J Gen Virol, vol.81, pp.195-199, 2000.

D. A. Matthews, W. W. Smith, R. A. Ferre, B. Condon, G. Budahazi et al., Structure of human rhinovirus 3C protease reveals a trypsin-like polypeptide fold, RNA-binding site, and means for cleaving precursor polyprotein, Cell, vol.77, pp.761-771, 1994.

M. Medina, E. Domingo, J. K. Brangwyn, and G. J. Belsham, The two species of the footand-mouth disease virus leader protein, expressed individually, exhibit the same activities, Virology, vol.194, pp.355-359, 1993.

R. Menard, C. Plouffe, P. Laflamme, T. Vernet, D. C. Tessier et al., Modification of the electrostatic environment is tolerated in the oxyanion hole of the cysteine protease papain, Biochemistry, vol.34, pp.464-471, 1995.

G. Meyers, C. Wirblich, and H. J. Thiel, Genomic and subgenomic RNAs of rabbit hemorrhagic disease virus are both protein-linked and packaged into particles, Virology, vol.184, pp.677-686, 1991.

G. Meyers, C. Wirblich, and H. J. Thiel, Rabbit hemorrhagic disease virus--molecular cloning and nucleotide sequencing of a calicivirus genome, Virology, vol.184, pp.664-676, 1991.

O. Mikami, J. H. Park, T. Kimura, K. Ochiai, and C. Itakura, Hepatic lesions in young rabbits experimentally infected with rabbit haemorrhagic disease virus, Res Vet Sci, vol.66, pp.237-242, 1999.

M. Mochizuki, A. Kawanishi, H. Sakamoto, S. Tashiro, R. Fujimoto et al., A calicivirus isolated from a dog with fatal diarrhoea, Vet Rec, vol.132, pp.221-222, 1993.

A. Molla, K. S. Harris, A. V. Paul, S. H. Shin, J. Mugavero et al., Stimulation of poliovirus proteinase 3Cpro-related proteolysis by the genome-linked protein VPg and its precursor 3AB, J Biol Chem, vol.269, pp.27015-27020, 1994.

J. P. Morisse, L. Gall, G. Boilletot, and E. , Hepatitis of viral origin in Leporidae: introduction and aetiological hypotheses, Rev Sci Tech, vol.10, pp.269-310, 1991.

S. C. Mosimann, M. M. Cherney, S. Sia, S. Plotch, and M. N. James, Refined X-ray crystallographic structure of the poliovirus 3C gene product, J Mol Biol, vol.273, pp.1032-1047, 1997.

H. M. Murthy, S. Clum, and R. Padmanabhan, Dengue virus NS3 serine protease. Crystal structure and insights into interaction of the active site with substrates by molecular modeling and structural analysis of mutational effects, J Biol Chem, vol.274, pp.5573-5580, 1999.

J. D. Neill, R. F. Meyer, and B. S. Seal, Genetic relatedness of the caliciviruses: San Miguel sea lion and vesicular exanthema of swine viruses constitute a single genotype within the Caliciviridae, J Virol, vol.69, pp.4484-4488, 1995.

J. D. Neill and B. S. Seal, Development of PCR primers for specific amplification of two distinct regions of the genomes of San Miguel sea-lion and vesicular exanthema of swine viruses, Mol Cell Probes, vol.9, pp.33-37, 1995.

V. T. Nguyen, M. Morange, and O. Bensaude, Firefly luciferase luminescence assays using scintillation counters for quantitation in transfected mammalian cells, Anal Biochem, vol.171, pp.404-408, 1988.

A. Nomoto, N. Kitamura, F. Golini, and E. Wimmer, The 5'-terminal structures of poliovirion RNA and poliovirus mRNA differ only in the genome-linked protein VPg, Proc Natl Acad Sci U S A, vol.74, pp.5345-5349, 1977.

G. D. Norsworthy, Questions efficacy of vaccinating cats at 3-year intervals, Am J Vet Res, vol.60, pp.918-919, 1999.

T. Nowak, P. M. Farber, and G. Wengler, Analyses of the terminal sequences of West Nile virus structural proteins and of the in vitro translation of these proteins allow the proposal of a complete scheme of the proteolytic cleavages involved in their synthesis, Virology, vol.169, pp.365-376, 1989.

N. Nowotny, C. R. Bascunana, A. Ballagi-pordany, D. Gavier-widen, M. Uhlen et al., Phylogenetic analysis of rabbit haemorrhagic disease and European brown hare syndrome viruses by comparison of sequences from the capsid protein gene, Arch Virol, vol.142, pp.657-673, 1997.

V. F. Ohlinger and H. J. Thiel, Identification of the viral haemorrhagic disease virus of rabbits as a calicivirus, Rev Sci Tech, vol.10, pp.311-323, 1991.

J. S. O'keefe, J. E. Tempero, M. X. Motha, M. F. Hansen, and P. H. Atkinsona, Serology of rabbit haemorrhagic disease virus in wild rabbits before and after release of the virus in New Zealand, Vet Microbiol, vol.66, pp.29-40, 1999.

A. C. Palmenberg, Proteolytic processing of picornaviral polyprotein, Annu Rev Microbiol, vol.44, pp.603-623, 1990.

A. C. Palmenberg, G. D. Parks, D. J. Hall, R. H. Ingraham, T. W. Seng et al., Proteolytic processing of the cardioviral P2 region: primary 2A/2B cleavage in clone-derived precursors, Virology, vol.190, pp.754-762, 1992.

J. H. Park, K. Ochiai, and C. Itakura, Detection of rabbit haemorrhagic disease virus particles in the rabbit liver tissues, J Comp Pathol, vol.107, pp.329-340, 1992.

N. Y. Park, C. J. Chong, J. H. Kim, S. M. Cho, Y. H. Cha et al., An outbreak of viral haemorrhagic pneumonia (tentative name) of rabbits in Korea, J Korean Vet Med Assoc, vol.23, pp.603-610, 1987.

F. Parra, J. A. Boga, M. S. Marin, and R. Casais, The amino terminal sequence of VP60 from rabbit hemorrhagic disease virus supports its putative subgenomic origin, Virus Res, vol.27, pp.219-228, 1993.

F. Parra and M. Prieto, Purification and characterization of a calicivirus as the causative agent of a lethal hemorrhagic disease in rabbits, J Virol, vol.64, pp.4013-4015, 1990.

T. B. Parsley, C. T. Cornell, and B. L. Semler, Modulation of the RNA binding and protein processing activities of poliovirus polypeptide 3CD by the viral RNA polymerase domain, J Biol Chem, vol.274, pp.12867-12876, 1999.

L. Pearl and T. Blundell, The active site of aspartic proteinases, FEBS Lett, vol.174, pp.96-101, 1984.

M. E. Piccone, M. Zellner, T. F. Kumosinski, P. W. Mason, and M. J. Grubman, Identification of the active-site residues of the L proteinase of foot-and-mouth disease virus, J Virol, vol.69, pp.4950-4956, 1995.

S. E. Poet, D. E. Skilling, J. L. Megyesl, W. G. Gilmartin, and A. W. Smith, Detection of a non-cultivatable calicivirus from the white tern (Gygis alba rothschildi), J Wildl Dis, vol.32, pp.461-467, 1996.

A. Poli, M. Nigro, D. Gallazzi, G. Sironi, A. Lavazza et al., Acute hepatosis in the European brown hare (Lepus europaeus) in Italy, J Wildl Dis, vol.27, pp.621-629, 1991.

B. V. Prasad, R. Rothnagel, X. Jiang, and M. K. Estes, Three-dimensional structure of baculovirus-expressed Norwalk virus capsids, J Virol, vol.68, pp.5117-5125, 1994.

B. V. Prasad, M. E. Hardy, T. Dokland, J. Bella, M. G. Rossmann et al., Xray Crystallographic Structure of the Norwalk Virus Capsid, Science, vol.286, pp.287-290, 1999.

C. R. Pringle, Virus taxonomy at the XIth international congress of virology, Arch Virol, vol.144, pp.2065-2070, 1999.

C. Probst, M. Jecht, and V. Gauss-muller, Processing of proteinase precursors and their effect on hepatitis A virus particle formation, J Virol, vol.72, pp.8013-8020, 1998.

F. Ramiro-ibanez, J. M. Martin-alonso, P. Garcia-palencia, F. Parra, and C. Alonso, Macrophage tropism of rabbit hemorrhagic disease virus is associated with vascular pathology, Virus Res, vol.60, pp.21-28, 1999.

D. Rasschaert, S. Huguet, M. F. Madelaine, and J. F. Vautherot, Sequence and genomic organization of a rabbit hemorrhagic disease virus isolated from a wild rabbit, Virus Genes, vol.9, pp.121-132, 1995.
URL : https://hal.archives-ouvertes.fr/hal-02709676

J. E. Rinehart-kim, W. M. Zhong, X. Jiang, A. W. Smith, and D. O. Matson, Complete nucleotide sequence and genomic organization of a primate calicivirus, Pan-1, Arch Virol, vol.144, pp.199-208, 1999.

P. J. Roberts and G. J. Belsham, Identification of critical amino acids within the foot-andmouth disease virus leader protein, a cysteine protease, Virology, vol.213, pp.140-146, 1995.

L. Rodak, M. Granatova, L. Valicek, B. Smid, T. Vesely et al., Monoclonal antibodies to rabbit haemorrhagic disease virus and their use in the diagnosis of infection, J Gen Virol, vol.71, pp.2593-2598, 1990.

L. Rodak, B. Smid, and L. Valicek, Application of control measures against viral haemorrhagic disease of rabbits in the Czech and Slovak Federal Republic, Rev Sci Tech, vol.10, pp.513-524, 1991.

T. Rumenapf, R. Stark, M. Heimann, and H. J. Thiel, N-terminal protease of pestiviruses: identification of putative catalytic residues by site-directed mutagenesis, J Virol, vol.72, pp.2544-2547, 1998.

N. Ruvoen-clouet, D. Blanchard, G. Andre-fontaine, and J. P. Ganiere, Partial characterization of the human erythrocyte receptor for rabbit haemorrhagic disease virus, Res Virol, vol.146, pp.33-41, 1995.

M. D. Ryan and M. Flint, Virus-encoded proteinases of the picornavirus super-group, J Gen Virol, vol.78, pp.699-723, 1997.

M. D. Ryan, A. M. King, and G. P. Thomas, Cleavage of foot-and-mouth disease virus polyprotein is mediated by residues located within a 19 amino acid sequence, J Gen Virol, vol.72, pp.2727-2732, 1991.

M. D. Ryan, S. Monaghan, and M. Flint, Virus-encoded proteinases of the Flaviviridae, J Gen Virol, vol.79, pp.947-959, 1998.

F. L. Schaffer, H. L. Bachrach, F. Brown, J. H. Gillespie, J. N. Burroughs et al., Caliciviridae. Intervirology, vol.14, pp.1-6, 1980.

F. L. Schaffer, D. W. Ehresmann, M. K. Fretz, and M. I. Soergel, A protein, VPg, covalently linked to 36S calicivirus RNA, J Gen Virol, vol.47, pp.215-220, 1980.

I. Schechter and A. Berger, The Schechter and Berger nomenclature for the description of protease subsites, Biochem Biophys Res Com, vol.27, pp.157-162, 1967.

H. Schirrmeier, I. Reimann, B. Kollner, and H. Granzow, Pathogenic, antigenic and molecular properties of rabbit haemorrhagic disease virus (RHDV) isolated from vaccinated rabbits: detection and characterization of antigenic variants, Arch Virol, vol.144, pp.719-735, 1999.

E. L. Seah, I. C. Gunesekere, J. A. Marshall, and P. J. Wright, Variation in ORF3 of genogroup 2 Norwalk-like viruses, Arch Virol, vol.144, pp.1007-1014, 1999.

E. L. Seah, J. A. Marshall, and P. J. Wright, Open reading frame 1 of the Norwalk-like virus Camberwell: completion of sequence and expression in mammalian cells, J Virol, vol.73, pp.10531-10535, 1999.

B. S. Seal, C. Lutze-wallace, L. C. Kreutz, T. Sapp, G. C. Dulac et al., Isolation of caliciviruses from skunks that are antigenically and genotypically related to San Miguel sea lion virus, Virus Res, vol.37, pp.1-12, 1995.

J. Seipelt, A. Guarne, E. Bergmann, M. James, W. Sommergruber et al., The structures of picornaviral proteinases, Virus Res, vol.62, pp.159-168, 1999.

Y. Shen, M. Igo, P. Yalamanchili, A. J. Berk, and A. Dasgupta, DNA binding domain and subunit interactions of transcription factor IIIC revealed by dissection with poliovirus 3C protease, Mol Cell Biol, vol.16, pp.4163-4171, 1996.

M. Sibilia, M. B. Boniotti, P. Angoscini, L. Capucci, and C. Rossi, Two independent pathways of expression lead to self-assembly of the rabbit hemorrhagic disease virus capsid protein, J Virol, vol.69, pp.5812-5815, 1995.

M. C. Simon, R. Muguruza, J. L. Alonso, J. L. Muzquiz, O. Girones et al., Recherche du virus de la maladie hémorragique virale du lapin (RHD) chez le renard et rôle des canidés domestiques dans la transmission de la maladie, vol.170, pp.841-845, 1994.

A. W. Smith and T. G. Akers, Vesicular exanthema of swine, J Am Vet Med Assoc, vol.169, pp.700-703, 1976.

A. W. Smith, T. G. Akers, S. H. Madin, and N. A. Vedros, San Miguel sea lion virus isolation, peliminary characterization and relationship to vesicular exanthema of swine virus, Nature, vol.244, pp.108-110, 1973.

A. W. Smith, M. P. Anderson, D. E. Skilling, J. E. Barlough, and P. K. Ensley, First isolation of calicivirus from reptiles and amphibians, Am J Vet Res, vol.47, pp.1718-1721, 1986.

A. W. Smith and P. M. Boyt, Caliciviruses of ocean origin: a review, J Zoo Wildl Med, vol.21, pp.3-23, 1990.

A. W. Smith, D. E. Skilling, N. Cherry, J. H. Mead, and D. O. Matson, Calicivirus emergence from ocean reservoirs: zoonotic and interspecies movements, 1998.

, Emerg Infect Dis, vol.4, pp.13-20

A. W. Smith, D. E. Skilling, P. K. Ensley, K. Benirschke, and T. L. Lester, Calicivirus isolation and persistence in a pygmy chimpanzee, Science, vol.221, pp.79-81, 1983.

A. W. Smith, D. E. Skilling, and S. Ridgway, Calicivirus-induced vesicular disease in cetaceans and probable interspecies transmission, J Am Vet Med Assoc, vol.183, pp.1223-1225, 1983.

W. Sommergruber, G. Casari, F. Fessl, J. Seipelt, and T. Skern, The 2A proteinase of human rhinovirus is a zinc containing enzyme, Virology, vol.204, pp.815-818, 1994.

W. Sommergruber, J. Seipelt, F. Fessl, T. Skern, H. D. Liebig et al., Mutational analyses support a model for the HRV2 2A proteinase, Virology, vol.234, pp.203-214, 1997.

S. Sosnovtsev and K. Y. Green, RNA transcripts derived from a cloned full-length copy of the feline calicivirus genome do not require VpG for infectivity, Virology, vol.210, pp.383-390, 1995.

S. V. Sosnovtsev, S. A. Sosnovtseva, and K. Y. Green, Cleavage of the feline calicivirus capsid precursor is mediated by a virus-encoded proteinase, J Virol, vol.72, pp.3051-3059, 1998.

S. A. Sosnovtseva, S. V. Sosnovtsev, and K. Y. Green, Mapping of the feline calicivirus proteinase responsible for autocatalytic p rocessing of the nonstructural polyprotein and identification of a stable proteinase-polymerase precursor protein, J Virol, vol.73, pp.6626-6633, 1999.

R. Stark, G. Meyers, T. Rumenapf, and H. J. Thiel, Processing of pestivirus polyprotein: cleavage site between autoprotease and nucleocapsid protein of classical swine fever virus, J Virol, vol.67, pp.7088-7095, 1993.

T. A. Steitz and R. G. Shulman, Crystallographic and NMR studies of the serine proteases, Annu Rev Biophys Bioeng, vol.11, pp.419-444, 1982.

M. J. Studdert, Caliciviruses. Brief review, Arch Virol, vol.58, pp.157-191, 1978.

D. Sung and H. Kang, The N-terminal amino acid sequences of the firefly luciferase are important for the stability of the enzyme, Photochem Photobiol, vol.68, pp.749-753, 1998.

T. Takegami, D. Sakamuro, and T. Furukawa, Japanese encephalitis virus nonstructural protein NS3 has RNA binding and ATPase activities, Virus Genes, vol.9, pp.105-112, 1994.

A. W. Tam, M. M. Smith, M. E. Guerra, C. C. Huang, D. W. Bradley et al., Hepatitis E virus (HEV): molecular cloning and sequencing of the full-length viral genome, Virology, vol.185, pp.120-131, 1991.

N. Tautz, K. Elbers, D. Stoll, G. Meyers, and H. J. Thiel, Serine protease of pestiviruses: determination of cleavage sites, J Virol, vol.71, pp.5415-5422, 1997.

H. J. Thiel and M. König, Caliciviruses: an overview, Vet Microbiol, vol.69, pp.55-62, 1999.

E. Thouvenin, S. Laurent, M. F. Madelaine, D. Rasschaert, J. F. Vautherot et al., Bivalent binding of a neutralising antibody to a calicivirus involves the torsional flexibility of the antibody hinge, J Mol Biol, vol.270, pp.238-246, 1997.

L. Tomei, C. Failla, E. Santolini, R. De-francesco, and N. La-monica, NS3 is a serine protease required for processing of hepatitis C virus polyprotein, J Virol, vol.67, pp.4017-4026, 1993.

H. Toyoda, M. J. Nicklin, M. G. Murray, C. W. Anderson, J. J. Dunn et al., A second virus-encoded proteinase involved in proteolytic processing of poliovirus polyprotein, Cell, vol.45, pp.761-770, 1986.

A. L. Vazquez, J. M. Martin-alonso, R. Casais, J. A. Boga, and F. Parra, Expression of enzymatically active rabbit hemorrhagic disease virus RNA-dependent RNA polymerase in Escherichia coli, J Virol, vol.72, pp.2999-3004, 1998.

T. Vernet, D. C. Tessier, J. Chatellier, C. Plouffe, T. S. Lee et al., Structural and functional roles of asparagine 175 in the cysteine protease papain, J Biol Chem, vol.270, pp.16645-16652, 1995.

R. Villafuerte, C. Calvete, C. Gortazar, and S. Moreno, First epizootic of rabbit hemorrhagic disease in free living populations of Oryctolagus cuniculus at Donana National Park, Spain, J Wildl Dis, vol.30, pp.176-179, 1994.

A. D. Wardell, W. Errington, G. Ciaramella, J. Merson, and M. J. Mcgarvey, Characterization and mutational analysis of the helicase and NTPase activities of hepatitis C virus full-length NS3 protein, J Gen Virol, vol.80, pp.701-709, 1999.

A. Warshel, G. Naray-szabo, F. Sussman, and J. K. Hwang, How do serine proteases really work?, Biochemistry, vol.28, pp.3629-3637, 1989.

P. Wattre, Ann Biol Clin, vol.52, issue.11, p.750, 1994.

, Ann Biol Clin, vol.52, pp.507-513

L. J. White, J. M. Ball, M. E. Hardy, T. N. Tanaka, N. Kitamoto et al., Attachment and entry of recombinant Norwalk virus capsids to cultured human and animal cell lines, J Virol, vol.70, pp.6589-6597, 1996.

C. Wirblich, G. Meyers, V. F. Ohlinger, L. Capucci, U. Eskens et al., European brown hare syndrome virus: relationship to rabbit hemorrhagic disease virus and other caliciviruses, J Virol, vol.68, pp.5164-5173, 1994.

C. Wirblich, M. Sibilia, M. B. Boniotti, C. Rossi, H. J. Thiel et al., 3C-like protease of rabbit hemorrhagic disease virus: identification of cleavage sites in the ORF1 polyprotein and analysis of cleavage specificity, J Virol, vol.69, pp.7159-7168, 1995.

C. Wirblich, H. J. Thiel, and G. Meyers, Genetic map of the calicivirus rabbit hemorrhagic disease virus as deduced from in vitro translation studies, J Virol, vol.70, pp.7974-7983, 1996.

Z. Wu, N. Yao, H. V. Le, and P. C. Weber, Mechanism of autoproteolysis at the NS2-NS3 junction of the hepatitis C virus polyprotein, Trends Biochem Sci, vol.23, pp.92-94, 1998.

J. Xu, E. Mendez, P. R. Caron, C. Lin, M. A. Murcko et al., Bovine viral diarrhea virus NS3 serine proteinase: polyprotein cleavage sites, cofactor requirements, and molecular model of an enzyme essential for pestivirus replication, J Virol, vol.71, pp.5312-5322, 1997.

W. Y. Xu, Viral haemorrhagic disease of rabbits in the People's Republic of China: epidemiology and virus characterisation, Rev Sci Tech, vol.10, pp.393-408, 1991.

P. Yalamanchili, K. Weidman, and A. Dasgupta, Cleavage of transcriptional activator Oct-1 by poliovirus encoded protease 3Cpro, Virology, vol.239, pp.176-185, 1997.

M. F. Ypma-wong, P. G. Dewalt, V. H. Johnson, J. G. Lamb, and B. L. Semler, Protein 3CD is the major poliovirus proteinase responsible for cleavage of the P1 capsid precursor, Virology, vol.166, pp.265-270, 1988.

M. F. Ypma-wong, D. J. Filman, J. M. Hogle, and B. L. Semler, Structural domains of the poliovirus polyprotein are major determinants for proteolytic cleavage at Gln-Gly pairs, J Biol Chem, vol.263, pp.17846-17856, 1988.