The Membrane (M1) Protein of Influenza Virus Occurs in Two Forms and is a Phosphoprotein

Overview

Journal J Virol

Publisher American Society for Microbiology

Date 1984 Jan 1

PMID 6690712

Citations 11

Authors

A Gregoriades

T Christie

K Markarian

Affiliations

Soon will be listed here.

Abstract

The membrane (M1) protein of influenza virus was found to be heterogenous and to occur in two forms in the virus particle. The two forms of M1 were found in virus which was produced both early and late after infection and in infected cells. The two forms could be separated on polyacrylamide gels under specific conditions. The two components of M1 contained similar tryptic peptides. However, a small proteolytic difference between the two proteins could not be ruled out. Both M1 proteins were present in phosphorylated form in the virus particle. The phosphorylated M1 components were not readily distinguished from phosphorylated nonstructural protein (NS1) when cytoplasm of infected cells was analyzed on polyacrylamide gels. The two phosphorylated M1 components could, however, be detected in infected cells by immunoprecipitation. One M1 component contained only phosphoserine whereas the second contained phosphoserine and a small amount of phosphothreonine as well. In addition to the phosphorylated nucleoprotein and M1, a third phosphorylated protein was routinely detected in virus particles. It was a surface component of the virus, since it could be removed from whole virus with chymotrypsin and contained phosphate at serine residues. The identity of this component was not known.

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References

Zvonarjev A, Ghendon Y . Influence of membrane (M) protein on influenza A virus virion transcriptase activity in vitro and its susceptibility to rimantadine. J Virol. 1980; 33(2):583-6. PMC: 288582. DOI: 10.1128/JVI.33.2.583-586.1980. View

Gregoriades A . Interaction of influenza M protein with viral lipid and phosphatidylcholine vesicles. J Virol. 1980; 36(2):470-9. PMC: 353664. DOI: 10.1128/JVI.36.2.470-479.1980. View

Bucher D, Kharitonenkov I, Zakomirdin J, Grigoriev V, Klimenko S, Davis J . Incorporation of influenza virus M-protein into liposomes. J Virol. 1980; 36(2):586-90. PMC: 353677. DOI: 10.1128/JVI.36.2.586-590.1980. View

Winter G, Fields S . Cloning of influenza cDNA ino M13: the sequence of the RNA segment encoding the A/PR/8/34 matrix protein. Nucleic Acids Res. 1980; 8(9):1965-74. PMC: 324050. DOI: 10.1093/nar/8.9.1965. View

Allen H, McCauley J, Waterfield M, Gething M . Influenza virus RNA segment 7 has the coding capacity for two polypeptides. Virology. 1980; 107(2):548-51. DOI: 10.1016/0042-6822(80)90324-4. View

Clinton G, Huang A . Distribution of phosphoserine, phosphothreonine and phosphotyrosine in proteins of vesicular stomatitis virus. Virology. 1981; 108(2):510-4. DOI: 10.1016/0042-6822(81)90459-1. View

Zhirnov O, Bukrinskaya A . Two forms of influenza virus nucleoprotein in infected cells and virions. Virology. 1981; 109(1):174-9. DOI: 10.1016/0042-6822(81)90482-7. View

Privalsky M, Penhoet E . The structure and synthesis of influenza virus phosphoproteins. J Biol Chem. 1981; 256(11):5368-76. View

Lamb R, Choppin P . Identification of a second protein (M2) encoded by RNA segment 7 of influenza virus. Virology. 1981; 112(2):729-37. DOI: 10.1016/0042-6822(81)90317-2. View

10.

Zakowski J, Petri Jr W, Wagner R . Role of matrix protein in assembling the membrane of vesicular stomatitis virus: reconstitution of matrix protein with negatively charged phospholipid vesicles. Biochemistry. 1981; 20(13):3902-7. DOI: 10.1021/bi00516a037. View

11.

Rose J, Gallione C . Nucleotide sequences of the mRNA's encoding the vesicular stomatitis virus G and M proteins determined from cDNA clones containing the complete coding regions. J Virol. 1981; 39(2):519-28. PMC: 171362. DOI: 10.1128/JVI.39.2.519-528.1981. View

12.

Inglis S, Brown C . Spliced and unspliced RNAs encoded by virion RNA segment 7 of influenza virus. Nucleic Acids Res. 1981; 9(12):2727-40. PMC: 326888. DOI: 10.1093/nar/9.12.2727. View

13.

Gregoriades A, Frangione B . Insertion of influenza M protein into the viral lipid bilayer and localization of site of insertion. J Virol. 1981; 40(1):323-8. PMC: 256625. DOI: 10.1128/JVI.40.1.323-328.1981. View

14.

Kharitonenkov I, ElKaradahgi S, Bucher D, Zakomirdin J, Tverdislov V . Interaction of influenza virus proteins with planar lipid bilayers: a model for virion assembly. Biochem Biophys Res Commun. 1981; 102(1):308-14. DOI: 10.1016/0006-291x(81)91522-9. View

15.

Petri T, Dimmock N . Phosphorylation of influenza virus nucleoprotein in vivo. J Gen Virol. 1981; 57(Pt 1):185-90. DOI: 10.1099/0022-1317-57-1-185. View

16.

Shaw M, Lamon E, Compans R . Surface expression of a nonstructural antigen on influenza A virus-infected cells. Infect Immun. 1981; 34(3):1065-7. PMC: 350976. DOI: 10.1128/iai.34.3.1065-1067.1981. View

17.

Almond J, Felsenreich V . Phosphorylation of the nucleoprotein of an avian influenza virus. J Gen Virol. 1982; 60(Pt 2):295-305. DOI: 10.1099/0022-1317-60-2-295. View

18.

Gregoriades A, Markarian K . Anomalous electrophoretic behavior of the membrane (M) protein of influenza virus in polyacrylamide gels. Arch Virol. 1983; 76(3):263-7. DOI: 10.1007/BF01311110. View

19.

APOSTOLOV K, Flewett T . Further observations on the structure of influenza viruses A and C. J Gen Virol. 1969; 4(3):365-70. DOI: 10.1099/0022-1317-4-3-365. View

20.

Compans R, Klenk H, CALIGUIRI L, Choppin P . Influenza virus proteins. I. Analysis of polypeptides of the virion and identification of spike glycoproteins. Virology. 1970; 42(4):880-9. DOI: 10.1016/0042-6822(70)90337-5. View