Hepatitis A virus polyprotein processing by Escherichia coli proteases

Journal of General Virology

Volumn 83, Issue 2, 2002, Pages 359-368

  Pintó, Rosa M ^a   Guix, Susana ^a   González Dankaart, Juan F ^a   Caballero, Santiago ^a   Sánchez, Gloria ^a   Guo, Ke Jian ^a   Ribes, Enric ^a   Bosch, Albert ^a  

^a UNIVERSITY OF BARCELONA   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; CAPSID PROTEIN; MUTANT PROTEIN; POLYPROTEIN; PROTEINASE;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ESCHERICHIA COLI; GENETIC CODE; HEPATITIS A VIRUS; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN PROCESSING; TEMPERATURE DEPENDENCE; VIRUS CAPSID; VIRUS PARTICLE; WILD TYPE;

ANIMALIA; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; HEPATITIS A VIRUS; NEGIBACTERIA; RNA VIRUSES;

EID: 0036169263     PISSN: 00221317     EISSN: None     Source Type: Journal    
DOI: 10.1099/0022-1317-83-2-359     Document Type: Article

References (31)

1. The refined crystal structure of the 3C gene product from hepatitis A virus: Specific proteinase activity and RNA recognition
2. Identification and characterization of a 3C-like protease from rabbit hemorrhagic disease virus, a calicivirus
3. Synthesis and assembly of hepatitis A virus-specific proteins in BS-C-1 cells
4. Recombinant hepatitis A virus polyprotein expressed in E. coli assembles in subviral structures
5. Complete nucleotide sequence of wild-type hepatitis A virus: Comparison with different strains of hepatitis A virus and other picornaviruses
6. Development of a plaque assay for a cytopathogenic, rapidly replicating isolate of a hepatitis A virus
7. Expression of virus-encoded proteinases: Functional and structural similarities with cellular enzymes
8. Auto-proteolytic cleavage of recombinant 3C proteinase of hepatitis A virus
9. Identification of active-site residues in protease 3C of hepatitis A virus by site-directed mutagenesis
10. Hepatitis A virus capsid protein VP1 has a heterogeneous C terminus
11. Polyprotein processing in cis and in trans by hepatitis A virus 3C protease cloned and expressed in Escherichia coli
12. Automated statistical analysis of microbial enumeration by dilution series
13. Proteolytic activity of hepatitis A virus 3C protein
14. Translation of hepatitis A virus RNA in vitro: Aberrant internal initiations influenced by 5′ noncoding region
15. 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
16. Current perspectives in the virology and molecular biology of hepatitis A virus
17. Expression, processing, and assembly of foot-and-mouth disease virus capsid structures in heterologous systems: Induction of a neutralizing antibody response in guinea pigs
18. Identification of further proteolytic cleavage sites in the Southampton calicivirus polyprotein by expression of the viral protease in E. coli
19. Expression and characterization of recombinant hepatitis A virus 3C proteinase
20. pro proteinase
21. Proteolytic processing of picornaviral polyprotein
22. Use of the colonic carcinoma cell line CaCo-2 for in vivo amplification and detection of enteric viruses
23. Proteinase 3C-mediated processing of VP1-2A of two hepatitis A virus strains: In vivo evidence for cleavage at amino acid position 273/274 of VP1
24. Processing of proteinase precursors and their effect on hepatitis A virus particle formation
25. Synthesis of immunogenic hepatitis A virus particles by recombinant baculoviruses
26. Cleavage of the feline calicivirus capsid precursor is mediated by a virus-encoded proteinase
27. Detection of hepatitis A virus capsid proteins in insect cells infected with recombinant baculoviruses encoding the entire hepatitis A virus open reading frame
28. Antigenic and immunogenic properties of recombinant hepatitis A virus 14S and 70S subviral particles
29. The hepatitis A virus polyprotein expressed by a recombinant vaccinia virus undergoes proteolytic processing and assembly into viruslike particles
30. 3C-like protease of rabbit hemorrhagic disease virus: Identification of cleavage sites in the ORF1 polyprotein and analysis of cleavage specificity