Structural highlights
Publication Abstract from PubMed
The matrix proteins of orthomyxoviruses, including influenza virus, infectious salmon anemia virus and Thogoto virus, play crucial roles in essential processes of the viral life cycle. However, the mechanisms of the matrix proteins involved in these processes are not fully understood. Currently, only the structure and function of the matrix protein from influenza virus have been studied. Here, we present the crystal structures of the N-terminal domain of matrix protein from Thogoto virus at pH 7.0 and 4.5. By analyzing the structures, we identified the conformational changes of monomers and dimers in different pH conditions, mainly caused by two flexible loops, L3 and L5. We suggest these structural deviations would reflect the basis of viral capsid assembly or disassembly.
Conformational changes of matrix protein from Thogoto virus at different pH implicate the mechanism of viral assembly and uncoating.,Yang M, Feng F, Liu Y, Wang H, Yang Z, Hou W, Liang H J Gen Virol. 2016 Jul 13. doi: 10.1099/jgv.0.000551. PMID:27411929[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yang M, Feng F, Liu Y, Wang H, Yang Z, Hou W, Liang H. Conformational changes of matrix protein from Thogoto virus at different pH implicate the mechanism of viral assembly and uncoating. J Gen Virol. 2016 Jul 13. doi: 10.1099/jgv.0.000551. PMID:27411929 doi:http://dx.doi.org/10.1099/jgv.0.000551
