Open AccessCloning, purification and preliminary crystallographic studies of the 2AB protein from hepatitis A virus
Author(s) -
Garriga Damià,
VivesAdrián Laia,
Buxaderas Mònica,
FerreiradaSilva Frederico,
Almeida Bruno,
MacedoRibeiro Sandra,
Pereira Pedro José Barbosa,
Verdaguer Núria
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111026261
Subject(s) - capsid , virology , poliovirus , biology , virus , open reading frame , genetics , peptide sequence , gene
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 P 4 1 or P 4 3 , 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.