tetano
Editor, Senior Moderator
FEBS Lett
. 2021 Sep 21.
doi: 10.1002/1873-3468.14194. Online ahead of print.
New structural insights into the multi-functional influenza A matrix protein 1
Julia Peukes[SUP] 1 2 [/SUP], Xiaoli Xiong[SUP] 1 3 [/SUP], John A G Briggs[SUP] 1 4 [/SUP]
Affiliations
Abstract
Influenza A virus matrix protein 1 (M1) is the most abundant protein within virions and functions at multiple steps of the virus life cycle, including nuclear RNA export, virus particle assembly, and virus disassembly. Two recent publications have presented the first structures of full-length M1, and show that it assembles filaments in vitro via an interface between the N- and C- terminal domains of adjacent monomers. These filaments were found to be similar to those that form the endoskeleton of assembled virions. The structures provide a molecular basis to understand the functions of M1 during the virus life cycle. Here we compare and discuss the two structures, and explore their implications for the mechanisms by which the multifunctional M1 protein can mediate virus assembly, interact with viral ribonucleoproteins and act during infection of a new cell.
Keywords: Influenza virus; M1; cryo-electron tomography; enveloped virus; helical reconstruction; matrix proteins; protein oligomerization; subtomogram averaging; virus assembly.
. 2021 Sep 21.
doi: 10.1002/1873-3468.14194. Online ahead of print.
New structural insights into the multi-functional influenza A matrix protein 1
Julia Peukes[SUP] 1 2 [/SUP], Xiaoli Xiong[SUP] 1 3 [/SUP], John A G Briggs[SUP] 1 4 [/SUP]
Affiliations
- PMID: 34547821
- DOI: 10.1002/1873-3468.14194
Abstract
Influenza A virus matrix protein 1 (M1) is the most abundant protein within virions and functions at multiple steps of the virus life cycle, including nuclear RNA export, virus particle assembly, and virus disassembly. Two recent publications have presented the first structures of full-length M1, and show that it assembles filaments in vitro via an interface between the N- and C- terminal domains of adjacent monomers. These filaments were found to be similar to those that form the endoskeleton of assembled virions. The structures provide a molecular basis to understand the functions of M1 during the virus life cycle. Here we compare and discuss the two structures, and explore their implications for the mechanisms by which the multifunctional M1 protein can mediate virus assembly, interact with viral ribonucleoproteins and act during infection of a new cell.
Keywords: Influenza virus; M1; cryo-electron tomography; enveloped virus; helical reconstruction; matrix proteins; protein oligomerization; subtomogram averaging; virus assembly.