The membrane protein of influenza virus: Extraction from virus and infected cell with acidic chloroform—Methanol

Gregoriades, Anastasia

doi:10.1016/0042-6822(73)90150-5

Cited by 75 publications

(46 citation statements)

References 40 publications

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“…Matrix protein 1 was purified from A/Dk/HN/303/ 2004(H5N1) by extraction with acidic chloroformmethanol, as described by Gregoriades [19]. Protein concentration was assayed by using the DC RC protein assay kit (Bio-Rad, Hercules, CA, USA) with BSA as a standard protein.…”

Section: Purification Of M1 Proteinmentioning

confidence: 99%

Identification of amino acid substitutions in avian influenza virus (H5N1) matrix protein 1 by using nanoelectrospray MS and MS/MS

Liu

Song

Lee

et al. 2009

J. Am. Soc. Mass Spectrom.

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Matrix protein 1 (M1), the major structural protein of the avian influenza virus, plays a critical role in regulation of viral RNA transcription via interaction with RNA and transportation of RNP cores. Mutations in M1 have been frequently observed in the highly virulent avian influenza H5N1 virus, which might be crucial to the pathogenic function. Here we report the characterization of mutated peptides in M1 purified from highly pathogenic avian influenza virus H5N1 by nanoelectrospray MS and MS/MS analyses on a quadrupole-time-of-flight mass spectrometer (Q-TOFMS). The specificity of tandem mass spectrometry allowed the identification of six amino acid (AA) substitutions in M1, including R95K, A166V, I168T, N207S, N224S, and R230K. Two commonly observed modifications such as oxidation and deamidation were accurately assigned in the protein. Bioinformatics analysis suggested some relationship between the amino acid substitution and structural property of M1 protein.Discussions on de novo sequencing of MS/MS spectra, especially in dealing with the AA substitutions, were provided. (J Am Soc Mass Spectrom 2009, 20, 312-320)

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Section: Purification Of M1 Proteinmentioning

confidence: 99%

Identification of amino acid substitutions in avian influenza virus (H5N1) matrix protein 1 by using nanoelectrospray MS and MS/MS

Liu

Song

Lee

et al. 2009

J. Am. Soc. Mass Spectrom.

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“…The method of Gregoriades (1973) was used. Purified virus was resuspended in NT buffer (0.1 M-NaCI, 0-01 i-Tris HCI pH 7-4).…”

Section: Virusesmentioning

confidence: 99%

“…For this purpose, 303 mg NaBr was added per ml plasma to give a final solution density of 1.21 g/ml. Then, 4 ml samples of plasma were placed into centrifuge tubes in a Beckman SW50 rotor, overlaid with 2 ml saline at a final density of 1.21 g/ml, and centrifuged at 40000 rev/min at 20 °C for 24 h. A lipoprotein fraction (a narrow yellow band on top of the gradient) was collected, and the proteins soluble in ACM were isolated as described by Gregoriades (1973).…”

Section: Virusesmentioning

confidence: 99%

“…According to reports in the literature, the M protein of vesicular stomatitis (VSV) and influenza viruses inhibits the RNP transcriptase activity of a homologous virus in experiments in vitro (Carroll & Wagner, 1979;Zvonarjov & Ghendon, 1980). The M protein isolated from the virions of negative strand viruses possesses some physical and chemical peculiarities; one of the most important of them is its solubility in chloroformmethanol mixture at acid pH (acidic chloroform-methanol, ACM) (Gregoriades, 1973). Proteins soluble in ACM (ACMS proteins) have been isolated not only from viruses, but from membrane structures of myelin, mitochondria and bacteria as well (Folch & Less, 1951 ;Gagnon et al, 1971 ;Sanderman & Strominger, 1971 ;Tzagaloff & Kawai, 1972).…”

Section: Introductionmentioning

confidence: 99%

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In vitro Inhibition of Negative Strand Virus Transcriptase Activity by Proteins Soluble in Acidic Chloroform-Methanol

Mikhejeva¹,

Ghendon²

1983

Journal of General Virology

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SUMMARYThe effect of proteins soluble in acidic chloroform-methanol (ACMS proteins) on the transcriptase activity of virus ribonucleoproteins (RNPs) in vitro has been studied. Experiments with ACMS membrane (M) proteins from type A and B orthomyxoviruses, as well as from vesicular stomatitis virus, showed that inhibition of the viral RNP transcriptase activity occurred when they interacted with M proteins isolated from viruses of a different serotype, or even of a different family. The presence of ACMS proteins capable of inhibiting the transcriptase activity of orthomyxovirus RNP in vitro was also detected in human blood plasma and among proteins produced by human leukocytes. Determination of the minimum concentration of M protein inhibiting the RNP transcriptase activity, and analysis of the fowl plague virus M protein-RNP complex formed in the in vitro system, showed that the M protein was capable of inhibiting RNP transcriptase activity at a M:RNP ratio of 0.1 to 0.2:1.

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“…The topography of M2 in the viral membrane is such that it would allow net proton flow into the virion interior. The rationale for this function of the virion M2 relates to certain characteristics of the matrix protein, in particular its tendency to be solubilized in the presence of detergent or organic solvents at low pH (Gregoriades, 1973;Ruigrok et al, 1989;Zhirnov, 1990) and observations that inhibition of M2 prevents the separation of matrix protein from the ribonucleoprotein (Bukrinskaya et al, 1982b;Martin & Helenius, 1991). Furthermore, the ability of mutations in the matrix protein to prevent the growth restriction caused by a monoclonal antibody directed against the N-terminal, external domain of M2 is a clear demonstration of the importance of either direct or indirect interactions between the two proteins (Zebedee & Lamb, 1989).…”

mentioning

confidence: 99%

Role of virion M2 protein in influenza virus uncoating: specific reduction in the rate of membrane fusion between virus and liposomes by amantadine

Wharton¹,

Belshe

Skehel³

et al. 1994

Journal of General Virology

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The anti-influenza virus drug amantadine was shown to reduce the rate of fusion of liposomes with influenza A viruses whose replication is inhibited by this drug. The fusion with amantadine-resistant viruses was unaffected. Experiments with reassortant and mutant viruses showed that this effect was linked to the M2 protein and not to the haemagglutinin of the virus. The proton ionophore monensin, on the other hand, substantially increased the rate of fusion of the viruses tested. These results indicate that the kinetics of virus-liposome fusion can be modulated by the virus M2 protein, the target of amantadine action, and it is postulated that the M2 ion channel functions by transporting protons into the virion interior and facilitating virus uncoating.

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The membrane protein of influenza virus: Extraction from virus and infected cell with acidic chloroform—Methanol

Cited by 75 publications

References 40 publications

Identification of amino acid substitutions in avian influenza virus (H5N1) matrix protein 1 by using nanoelectrospray MS and MS/MS

Identification of amino acid substitutions in avian influenza virus (H5N1) matrix protein 1 by using nanoelectrospray MS and MS/MS

In vitro Inhibition of Negative Strand Virus Transcriptase Activity by Proteins Soluble in Acidic Chloroform-Methanol

Role of virion M2 protein in influenza virus uncoating: specific reduction in the rate of membrane fusion between virus and liposomes by amantadine

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