Title Cloning, purification and preliminary crystallographic studies of the 2AB protein from hepatitis A virus.
Author Garriga, Damia; Vives-Adrian, Laia; Buxaderas, Monica; Ferreira-da-Silva, Frederico; Almeida, Bruno; Macedo-Ribeiro, Sandra; Pereira, Pedro Jose Barbosa; Verdaguer, Nuria
Journal Acta Crystallogr Sect F Struct Biol Cryst Commun Publication Year/Month 2011-Oct
PMID 22102033 PMCID PMC3212368
Affiliation 1.Institut de Biologia Molecular de Barcelona, CSIC, Parc Cientific de Barcelona, Baldiri i Reixac 10, 08028 Barcelona, Spain.

The Picornaviridae family contains a large number of human pathogens such as rhinovirus, poliovirus and hepatitis A virus (HAV). Hepatitis A is an infectious disease that causes liver inflammation. It is highly endemic in developing countries with poor sanitation, where infections often occur in children. As in other picornaviruses, the genome of HAV contains one open reading frame encoding a single polyprotein that is subsequently processed by viral proteinases to originate mature viral proteins during and after the translation process. In the polyprotein, the N-terminal P1 region generates the four capsid proteins, while the C-terminal P2 and P3 regions contain the enzymes, precursors and accessory proteins essential for polyprotein processing and virus replication. Here, the first crystals of protein 2AB of HAV are reported. The crystals belonged to space group P4(1) or P4(3), with unit-cell parameters a = b = 90.42, c = 73.43 A, and contained two molecules in the asymmetric unit. Native and selenomethionine-derivative crystals diffracted to 2.7 and 3.2 A resolution, respectively.

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