The polypeptides of influenza virus

Stanley, Pamela; Haslam, Elizabeth A.

doi:10.1016/0042-6822(71)90078-x

Cited by 85 publications

(9 citation statements)

References 15 publications

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“…The presence of N-acetylglucosamine and the absence of N-acetylgalactosamine and xylose suggests the carbohydrate is attached via N-glycosidic linkage to asparagine [24]. We find that the light chain carries about one-third as much N-acetylglucosamine as the heavy chain [9,20] but only traces of the other sugars. For a tool.…”

Section: Carbohydrate and Amino Acid Compositionsmentioning

confidence: 82%

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Size and chemical composition of influenza virus hemagglutinin chains

Ward

Dopheide

1976

FEBS Letters

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Section: Carbohydrate and Amino Acid Compositionsmentioning

confidence: 82%

“…wt. of the HA~ from Ao/Bel/42 has been reported as 65 000 when 5% gels were used [20], 58 000 when 7.5% gels were used [21] but only 47 000 when the mol. wt.…”

Section: Molecular Weightmentioning

confidence: 99%

Size and chemical composition of influenza virus hemagglutinin chains

Ward

Dopheide

1976

FEBS Letters

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Section: Introductionmentioning

confidence: 99%

“…The lactoperoxidase (iodide: hydrogen-peroxide oxidoreductase, EC 1.11.1.8) catalyzed iodination procedure (6) is a technique by which tyrosine-containing proteins exposed on the surface of cell membranes can be directly labeled. This technique has been used to examine proteins on the membranes of erythrocytes (6, 7), lymphocytes (8, 9), platelets (10, 11), fibroblasts (12), and viruses (13,14).In this study, lactoperoxidase-catalyzed iodination has been used to characterize the membranes of intact normal cell lines and their transformed derivatives. It was hoped that the iodination procedure was sufficiently mild that membrane architecture remained relatively unperturbed.…”

mentioning

confidence: 99%

A Comparison of Membrane Proteins of Normal and Transformed Cells by Lactoperoxidase Labeling

Hogg

1974

Proc. Natl. Acad. Sci. U.S.A.

114

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The enzyme lactoperoxidase (iodide: hydrogen-peroxide oxidoreductase, EC 1.11.1.8) was used to iodinate ('2I) accessible proteins on membranes of intact virally transformed and untransformed cells. A number of labeled bands of proteins were detected by acrylamide gel electrophoresis. A heavily labeled band with a molecular weight of approximately 250,000 daltons was found in all untransformed cells but was absent from transformed cells. When Coomassie-blue-stained membrane preparations were compared, a band was seen in normal cells which comigrated with the lactoperoxidase-labeled band. In transformed cell membranes, three discrete bands were present in the same position. Thus, the expression of this protein may be altered when cells are in the transformed state.The identification of alterations in membrane proteins and glycoproteins after transformation by DNA or RNA oncogenic viruses has been confusing. In general, there is reported to be an overall decrease in numbers of membrane glycoproteins (1, 2), but there are demonstrations of an increased glycosylation of a restricted number of membrane glycoproteins in transformed cells (3, 4). Conversely, other studies have suggested an association with untransformed cell membranes (5), or their growth media (2), of glycoproteins which were absent from membranes of transformed cells.It was considered that a fruitful approach to resolving some of these complexities would be to examine directly the membranes of intact cells rather than isolated membrane fragments. The lactoperoxidase (iodide: hydrogen-peroxide oxidoreductase, EC 1.11.1.8) catalyzed iodination procedure (6) is a technique by which tyrosine-containing proteins exposed on the surface of cell membranes can be directly labeled. This technique has been used to examine proteins on the membranes of erythrocytes (6, 7), lymphocytes (8, 9), platelets (10, 11), fibroblasts (12), and viruses (13,14).In this study, lactoperoxidase-catalyzed iodination has been used to characterize the membranes of intact normal cell lines and their transformed derivatives. It was hoped that the iodination procedure was sufficiently mild that membrane architecture remained relatively unperturbed. MATERIALS AND METHODSCells. The cell lines used were BALB/C 3T3 (clone A31), Swiss 3T6, and secondary cultures of mouse-embryo fibroblasts from Taylors Own mice (ICRF), referred to as TO cells. All transformed cells used were derivatives of the 3T3 line A31: Py-3T3 and SV-3T3 were isolated after infection of 3T3 cells by the DNA viruses, polyoma and SV-40 viruses, respectively, and were a gift from Dr. Mike Fried. Transformed cells MSV-3T3 were isolated from a single infection of 3T3 by murine leukemia virus (Moloney pseudotype) which contained both sarcoma and leukemia virus activity. MSV-3T3 cells had a transformed morphology and were releasing sarcoma virus, as detected by the focus-forming assay, and leukemia virus, as detected by the XC plaque assay (15). The LX cells were a kind gift from Dr. Mike Shodell.All the cell lines, e...

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“…In the particular case of the influenza and parainfluenza viruses, haemagglutination involves adsorption of a virus envelope glycoprotein (designated as either HA or HN respectively) to mucoprotein receptors on the erythrocyte surface (Lazarowitz et al, 1971(Lazarowitz et al, , 1973Stanley and Haslam, 1971;Klenk et al, 1972;Scheid et al, 1972;Skehel, 1972;Scheid and Choppin, 1973). Viral neuraminidases, a separate envelope glycoprotein, NA, of the influenza viruses but a component of the HN glycoprotein of parainfluenza viruses, elute virus from the erythrocyte surface by hydrolytic cleavage of the glycoside linkage joining neuraminic acid to galactose with the release of N-acetyl neuraminic acid (Gottschalk, 1959;Scheid et al, 1972;Laver, 1973).…”

Section: Introductionmentioning

confidence: 99%

A simple procedure for the analysis of the structural proteins of influenza and parainfluenza viruses involving adsorption to erythrocytes

Cowley

Tannock

Barry

1984

Journal of Virological Methods

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A simple procedure for the analysis of the structural proteins of influenza and parainfluenza viruses utilizing adsorption to erythrocytes is described. The method involves virus growth in the presence of [35S]methionine, adsorption of clarified culture medium with a 0.5% suspension of either guinea-pig or chicken erythrocytes and analysis of the virus-erythrocyte aggregates by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). All of the structural proteins can be detected using this procedure, and the protein profiles of virus-adsorbed erythrocyte complexes compare extremely well with those of sucrose density gradient purified virus preparations.

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The polypeptides of influenza virus

Cited by 85 publications

References 15 publications

Size and chemical composition of influenza virus hemagglutinin chains

Size and chemical composition of influenza virus hemagglutinin chains

A Comparison of Membrane Proteins of Normal and Transformed Cells by Lactoperoxidase Labeling

A simple procedure for the analysis of the structural proteins of influenza and parainfluenza viruses involving adsorption to erythrocytes

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