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Cloning, purification and preliminary crystallographic studies of the 2AB protein from hepatitis A virus

AuthorsGarriga, Damià; Vives-Adrián, Laia ; Buxaderas, Mònica ; Ferreira-da-Silva, Frederico; Almeida, Bruno; Macedo-Ribeiro, Sandra; Pereira, Pedro José Barbosa; Verdaguer, Núria
Issue Date2011
PublisherInternational Union of Crystallography
CitationActa Crystallographica Section F 67(10): 1224-1227 (2011)
AbstractThe 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 P41 or P43, with unit-cell parameters a = b = 90.42, c = 73.43 Å, and contained two molecules in the asymmetric unit. Native and selenomethionine-derivative crystals diffracted to 2.7 and 3.2 Å resolution, respectively. © 2011 International Union of Crystallography All rights reserved.
Publisher version (URL)http.//dx.doi.org/10.1107/S1744309111026261
Identifiersdoi: 10.1107/S1744309111026261
issn: 1744-3091
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