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J Biomol Struct Dyn. 2018 Feb 1:1-46. doi: 10.1080/07391102.2018.1436089. [Epub ahead of print]
Matrix proteins of enveloped viruses: a case study of Influenza A virus M1 protein.
Kordyukova LV1, Shtykova EV2,3, Baratova LA1, Svergun DI4, Batishchev OV5,6.
Author information
Abstract
Influenza A virus, a member of the Orthomyxoviridae family of enveloped viruses, is one of the human and animal top killers, and its structure and components are therefore extensively studied during the last decades. The most abundant component, M1 matrix protein, forms a matrix layer (scaffold) under the viral lipid envelope, and the functional roles as well as structural peculiarities of the M1 protein are still under heavy debate. Despite multiple attempts of crystallization, no high resolution structure is available for the full length M1 of Influenza A virus. The likely reason for the difficulties lies in the intrinsic disorder of the M1 C-terminal part preventing diffraction quality crystals to be grown. Alternative structural methods including synchrotron small-angle X-ray scattering (SAXS), atomic force microscopy (AFM), cryo-electron microscopy (CEM)/tomography (CET) are therefore widely applied to understand the structure of M1, its self-association and interactions with the lipid membrane and the viral nucleocapsid. These methods reveal striking similarities in the behaviour of M1 and matrix proteins of other enveloped RNA viruses, with the differences accompanied by the specific features of the viral lifecycles, thus suggesting common interaction principles and, possibly, common evolutional ancestors. The structural information on the Influenza A virus M1 protein obtained to the date strongly suggests that the intrinsic disorder in the C-terminal domain has important functional implications.
KEYWORDS:
M1 matrix protein; M1 self-association; M1-lipid interactions; enveloped viruses; influenza A virus; intrinsically disordered proteins; matrix scaffold
PMID: 29388479 DOI: 10.1080/07391102.2018.1436089
Matrix proteins of enveloped viruses: a case study of Influenza A virus M1 protein.
Kordyukova LV1, Shtykova EV2,3, Baratova LA1, Svergun DI4, Batishchev OV5,6.
Author information
Abstract
Influenza A virus, a member of the Orthomyxoviridae family of enveloped viruses, is one of the human and animal top killers, and its structure and components are therefore extensively studied during the last decades. The most abundant component, M1 matrix protein, forms a matrix layer (scaffold) under the viral lipid envelope, and the functional roles as well as structural peculiarities of the M1 protein are still under heavy debate. Despite multiple attempts of crystallization, no high resolution structure is available for the full length M1 of Influenza A virus. The likely reason for the difficulties lies in the intrinsic disorder of the M1 C-terminal part preventing diffraction quality crystals to be grown. Alternative structural methods including synchrotron small-angle X-ray scattering (SAXS), atomic force microscopy (AFM), cryo-electron microscopy (CEM)/tomography (CET) are therefore widely applied to understand the structure of M1, its self-association and interactions with the lipid membrane and the viral nucleocapsid. These methods reveal striking similarities in the behaviour of M1 and matrix proteins of other enveloped RNA viruses, with the differences accompanied by the specific features of the viral lifecycles, thus suggesting common interaction principles and, possibly, common evolutional ancestors. The structural information on the Influenza A virus M1 protein obtained to the date strongly suggests that the intrinsic disorder in the C-terminal domain has important functional implications.
KEYWORDS:
M1 matrix protein; M1 self-association; M1-lipid interactions; enveloped viruses; influenza A virus; intrinsically disordered proteins; matrix scaffold
PMID: 29388479 DOI: 10.1080/07391102.2018.1436089