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

Dami Garriga, Laia Vives-Adrián, Mnica Buxaderas, Frederico Ferreira-Da-Silva, Bruno Almeida, Sandra Macedo-Ribeiro, Pedro José Barbosa Pereira, Nria Verdaguer

Research output: Contribution to journalArticleResearchpeer-review

2 Citations (Scopus)

Abstract

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 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.

Original languageEnglish
Pages (from-to)1224-1227
Number of pages4
JournalActa Crystallographica Section F: Structural Biology Communications
Volume67
Issue number10
DOIs
Publication statusPublished - Oct 2011
Externally publishedYes

Keywords

  • 2A
  • 2B
  • hepatitis A virus
  • nonstructural P2 region
  • picornaviruses

Cite this