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Hepatitis A virus polyprotein processing by Escherichia coli proteases

Department of Microbiology¹ and Department of Animal and Plant Cell Biology², University of Barcelona, Av. Diagonal 645, 08028 Barcelona, Spain

Author for correspondence: Albert Bosch. Fax +34 934034629. e-mail albert{at}porthos.bio.ub.es

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-dependant, since it differs at 37 or 42 °C. The bacterial protease(s) cleave scissile bonds other than those of HAV; this contributes to the low efficiency of particle formation.

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