AVM

Protein name	Matrix Protein 1
Uniprot protein ID	C3W5X4
Protein length	252 amino acids
Protein description	The M1 protein is composed of nine a-helices (H1-H9). These α-helices are organized into two four-helix bundles: N-terminal domain (H1-H4) and C terminal domain (H6-H9) connected via another helix linker (H5). The M1 protein plays critical roles in virus replication, from virus entry and uncoating to assembly and budding of the virus particle. M1 binding to ribonucleocapsids (RNPs) in nucleus seems to inhibit viral transcription. Interaction of viral NEP with M1-RNP is thought to promote nuclear export of the complex, which is targeted to the virion assembly site at the apical plasma membrane in polarized epithelial cells. Interactions with NA and HA may bring M1, a non-raft-associated protein, into lipid rafts. Forms a continuous shell on the inner side of the lipid bilayer in virion, where it binds the RNP. During virus entry into cell, the M2 ion channel acidifies the internal virion core, inducing M1 dissociation from the RNP. M1-free RNPs are transported to the nucleus, where viral transcription and replication can take place.

Pubmed ID	12604801
Clinical information	No
Disease	-
Published year	2003
Journal	JOURNAL OF GENERAL VIROLOGY
Title	Reverse genetics studies on the filamentous morphology of influenza A virus
Author	Svetlana V. Bourmakina,Adolfo GarcIa-Sastre
Evidence	Effect of mutations in the M1 protein of Udorn virus on virion morphology. (A) Purified WSN, WSN-Mud, WSN-M1ud, Mchim1, Mchim2, M1udA41V, M1udR95K, M1udA167T, M1udT168A, M1udE204D, M1udV205I and M1udA218T viruses were visualized by electron microscopy.