title: Hepatitis A virus polyprotein processing by Escherichia coli proteases.
abstract: Hepatitis A virus (HAV) encodes a single polyprotein, which is post-translationally processed. This processing represents an essential step in capsid formation. The virus possesses only one protease, 3C, responsible for all cleavages, except for that at the VP1/2A junction region, which is processed by cellular proteases. In this study, data demonstrates that HAV polyprotein processing by Escherichia coli protease(s) leads to the formation of particulate structures. P3 polyprotein processing in E. coli is not dependent on an active 3C protease: the same processing pattern is observed with wild-type 3C or with several 3C mutants. However, this processing pattern is temperature-dependent, since it differs at 37 or 42 degrees C. The bacterial protease(s) cleave scissile bonds other than those of HAV; this contributes to the low efficiency of particle formation.
authors.affiliation: Department of Microbiology1 and Department of Animal and Plant Cell Biology2, University of Barcelona, Av. Diagonal 645, 08028 Barcelona, Spain.
authors.forename: Rosa M
authors.initials: RM
authors.lastname: Pintó
authors.affiliation: Department of Microbiology1 and Department of Animal and Plant Cell Biology2, University of Barcelona, Av. Diagonal 645, 08028 Barcelona, Spain.
authors.forename: Susana
authors.initials: S
authors.lastname: Guix
authors.affiliation: Department of Microbiology1 and Department of Animal and Plant Cell Biology2, University of Barcelona, Av. Diagonal 645, 08028 Barcelona, Spain.
authors.forename: Juan F
authors.initials: JF
authors.lastname: González-Dankaart
authors.affiliation: Department of Microbiology1 and Department of Animal and Plant Cell Biology2, University of Barcelona, Av. Diagonal 645, 08028 Barcelona, Spain.
authors.forename: Santiago
authors.initials: S
authors.lastname: Caballero
authors.affiliation: Department of Microbiology1 and Department of Animal and Plant Cell Biology2, University of Barcelona, Av. Diagonal 645, 08028 Barcelona, Spain.
authors.forename: Gloria
authors.initials: G
authors.lastname: Sánchez
authors.affiliation: Department of Microbiology1 and Department of Animal and Plant Cell Biology2, University of Barcelona, Av. Diagonal 645, 08028 Barcelona, Spain.
authors.forename: Ke-Jian
authors.initials: KJ
authors.lastname: Guo
authors.affiliation: Department of Microbiology1 and Department of Animal and Plant Cell Biology2, University of Barcelona, Av. Diagonal 645, 08028 Barcelona, Spain.
authors.forename: Enric
authors.initials: E
authors.lastname: Ribes
authors.affiliation: Department of Microbiology1 and Department of Animal and Plant Cell Biology2, University of Barcelona, Av. Diagonal 645, 08028 Barcelona, Spain.
authors.forename: Albert
authors.initials: A
authors.lastname: Bosch
mesh_terms: D000086042:3C Viral Proteases; D002213:Capsid / Q000378:metabolism*; D002460:Cell Line; D003546:Cysteine Endopeptidases / Q000235:genetics* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics*; D030041:Hepatitis A virus / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D015151:Immunoblotting; D016297:Mutagenesis, Site-Directed; D010957:Plasmids / Q000235:genetics; D016133:Polymerase Chain Reaction; D011498:Protein Precursors / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D014764:Viral Proteins / Q000235:genetics* / Q000378:metabolism; D014771:Virion / Q000378:metabolism / Q000648:ultrastructure
chemical_list: D011498:Protein Precursors; D014764:Viral Proteins; D003546:Cysteine Endopeptidases; D000086042:3C Viral Proteases