2024-03-29T02:06:48Zhttp://digital.csic.es/dspace-oai/requestoai:digital.csic.es:10261/1240982021-11-22T13:10:09Zcom_10261_25com_10261_1com_10261_41col_10261_278col_10261_294
00925njm 22002777a 4500
dc
Vives-Adrián, Laia
author
Garriga, Damià
author
Buxaderas, Mònica
author
Fraga, Joana
author
Pereira, Pedro José Barbosa
author
Macedo-Ribeiro, Sandra
author
Verdaguer, Núria
author
2015-01-14
© 2015, American Society for Microbiology. The complexity of viral RNA synthesis and the numerous participating factors require a mechanism to topologically coordinate and concentrate these multiple viral and cellular components, ensuring a concerted function. Similarly to all other positivestrand RNA viruses, picornaviruses induce rearrangements of host intracellular membranes to create structures that act as functional scaffolds for genome replication. The membrane-targeting proteins 2B and 2C, their precursor 2BC, and protein 3A appear to be primarily involved in membrane remodeling. Little is known about the structure of these proteins and the mechanisms by which they induce massive membrane remodeling. Here we report the crystal structure of the soluble region of hepatitis A virus (HAV) protein 2B, consisting of two domains: a C-terminal helical bundle preceded by an N-terminally curved five-stranded antiparallel β-sheet that displays striking structural similarity to the β-barrel domain of enteroviral 2A proteins. Moreover, the helicoidal arrangement of the protein molecules in the crystal provides a model for 2B-induced host membrane remodeling during HAV infection.
Journal of Virology 89(7): 3648-3658 (2015)
http://hdl.handle.net/10261/124098
10.1128/JVI.02881-14
http://dx.doi.org/10.13039/501100004837
http://dx.doi.org/10.13039/501100001871
http://dx.doi.org/10.13039/501100000780
25589659
Structural basis for host membrane remodeling induced by protein 2B of hepatitis A virus