The M2 protein of influenza A virus is acylated.
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Thin-layer chromatographic fatty acid analysis of [3H]myristic and [ 3H]palmitic acid-labelled M2 protein shows that palmitic Acid is the predominant fatty acid linked to this polypeptide.Abstract:
The M2 protein of influenza A virus, a 97 amino acid integral membrane protein expressed on the surface of infected cells, is covalently modified with long chain fatty acids. The fatty acid bond is sensitive to treatment with neutral hydroxylamine and mercaptoethanol, which indicates a labile thioester type linkage. Thinlayer chromatographic fatty acid analysis of [3H]myristic and [3H]palmitic acid-labelled M2 protein shows that palmitic acid is the predominant fatty acid linked to this polypeptide. Palmitoylation of M2 occurs post-translationally and causes an upward shift in the SDS-PAGE mobility of the protein.read more
Citations
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Journal ArticleDOI
Influenza Virus Assembly and Lipid Raft Microdomains: a Role for the Cytoplasmic Tails of the Spike Glycoproteins
TL;DR: Examination of purified virions indicated reduced amounts of DIG-associated lipids in the envelope of HAt− and NAt− viruses, indicating that deletion of both the HA and NA cytoplasmic tails results in reduced DIG association and changes in both virus polypeptide and lipid composition.
Journal ArticleDOI
Activation of the M2 ion channel of influenza virus: a role for the transmembrane domain histidine residue
TL;DR: Results are consistent with protonation of histidine residue 37 as an essential step in the activation of the wild-type M2 ion channel.
Journal ArticleDOI
Proteolipid protein (PLP) of CNS myelin: positions of free, disulfide-bonded, and fatty acid thioester-linked cysteine residues and implications for the membrane topology of PLP
Thomas Weimbs,Wilhelm Stoffel +1 more
TL;DR: The structural data not only demand the revision of the concept of the membrane topology of PLP but will also promote more sophisticated studies on the mechanism of myelination and new functions ofPLP.
Book ChapterDOI
Modification of membrane permeability by animal viruses.
TL;DR: The infection of susceptible cells by animal viruses leads to profound changes in membrane permeability at two well defined moments of the infection cycle: early during infection when the virus enters the cells and at the beginning of the late phase before the onset of viral macromolecular synthesis.
Journal ArticleDOI
Influenza Virus M2 Ion Channel Protein Is Necessary for Filamentous Virion Formation
Jeremy S. Rossman,Xianghong Jing,Xianghong Jing,George P. Leser,Victoria Balannik,Lawrence H. Pinto,Robert A. Lamb +6 more
TL;DR: It is found that an amphipathic helix located within the M2 cytoplasmic tail is able to bind cholesterol, and it is speculated that M2 cholesterol binding is essential for both filament formation and the stability of existing viral filaments.
References
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Journal ArticleDOI
The biology and enzymology of eukaryotic protein acylation
TL;DR: The N-Myristoylated Protein s Have Diff erent Intracellular Destinations and the Importance of Sequ ence Context is illustrated.
Journal ArticleDOI
The molecular basis of the specific anti-influenza action of amantadine.
TL;DR: The data reported here demonstrate that the basis of these actions is similar and resides in the virus‐coded M2 membrane protein, the product of a spliced transcript of RNA segment 7.
Journal ArticleDOI
Influenza virus M2 protein is an integral membrane protein expressed on the infected-cell surface
TL;DR: The influenza A virus M 2 protein is expressed abundantly at the cell surface, and in addition to the hemagglutinin (HA) and neuraminidase (NA), is a third virus-specific membrane protein this paper.
Journal ArticleDOI
Influenza A virus M2 protein: monoclonal antibody restriction of virus growth and detection of M2 in virions.
Suzanne Zebedee,Robert A. Lamb +1 more
TL;DR: The monoclonal antibody, when included in a plaque assay overlay, considerably showed the growth of some influenza virus strains and is a specific effect for the M2 antibody as determined by an analysis of recombinants with defined genome composition and by the observation that competition by an N-terminal peptide prevents the antibody restriction of virus growth.
Book ChapterDOI
The molecular biology of influenza virus pathogenicity.
Hans-Dieter Klenk,Rudolf Rott +1 more
TL;DR: Evidence is steadily growing that a key role has to be assigned to hemagglutinin in the pathogenicity of influenza virus, and there is now evidence that it may also be relevant for the disease in humans because bacterial proteases have been found to promote the development of influenza pneumonia in mammals.
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