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Calicivirin (EC, Camberwell virus processing peptidase, Chiba virus processing peptidase, Norwalk virus processing peptidase, Southampton virus processing peptidase, norovirus virus processing peptidase, calicivirus trypsin-like cysteine protease, calicivirus TCP, calicivirus 3C-like protease, calicivirus endopeptidase, rabbit hemorrhagic disease virus 3C endopeptidase) is an enzyme.[1][2][3][4][5] This enzyme catalyses the following chemical reaction

Endopeptidase with a preference for cleavage when the P1 position is occupied by Glu- and the P1- position is occupied by Gly-

Viruses that are members of the genus Norovirus (family Caliciviridae) are a major cause of epidemic acute viral gastroenteritis.


  1. ^ Meyers G, Rossi C, Thiel HJ (2004). "Calicivirus endopeptidases". In Barrett AJ, Rawlings ND, Woessner JF. Handbook of Proteolytic Enzymes (2nd ed.). London: Elsevier. pp. 1380–1382. 
  2. ^ Wirblich C, Sibilia M, Boniotti MB, Rossi C, Thiel HJ, Meyers G (November 1995). "3C-like protease of rabbit hemorrhagic disease virus: identification of cleavage sites in the ORF1 polyprotein and analysis of cleavage specificity". Journal of Virology. 69 (11): 7159–68. PMC 189637Freely accessible. PMID 7474137. 
  3. ^ Martín Alonso JM, Casais R, Boga JA, Parra F (February 1996). "Processing of rabbit hemorrhagic disease virus polyprotein". Journal of Virology. 70 (2): 1261–5. PMC 189940Freely accessible. PMID 8551592. 
  4. ^ Liu B, Clarke IN, Lambden PR (April 1996). "Polyprotein processing in Southampton virus: identification of 3C-like protease cleavage sites by in vitro mutagenesis". Journal of Virology. 70 (4): 2605–10. PMC 190109Freely accessible. PMID 8642693. 
  5. ^ Liu BL, Viljoen GJ, Clarke IN, Lambden PR (February 1999). "Identification of further proteolytic cleavage sites in the Southampton calicivirus polyprotein by expression of the viral protease in E. coli". The Journal of General Virology. 80 ( Pt 2): 291–6. doi:10.1099/0022-1317-80-2-291. PMID 10073687. 

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