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Query: UMLS:C0272170 (SDS)
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HA1 and HA2 polypeptides of influenza A virus haemagglutinin (HA) were separated in purified form using electrophoresis in SDS containing polyacrylamide gels (PAGE) or chloroform-methanol extraction. The populations of HA1 polypeptides were immunogenic but considerably less so than the intact HA molecule and induced antibody which cross-reacted with influenza A and B viruses. After absorption with heterologous influenza B virus, the cross-reacting antibodies were removed and the HA1 antisera then possessed antibodies which reacted only with the cross-reactive (CR) determinants of the HA of the homologous influenza A virus and viruses of the same subtype. Neither strain-specific (SS) nor virus-neutralizing antibodies were detected in these anti-HA1 sera. HA2 polypeptides were less immunogenic and anti-HA2 antisera after absorption with influenza B virus failed to react with influenza A virus in immuno double diffusion tests and only reacted with partially denatured HA in the more sensitive single radial diffusion tests.
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PMID:Immunological studies with the HA1 and HA2 polypeptides of influenza A virus haemagglutinin. 8 Nov 52

The intracellular development of membrane protein (MP) of influenza A virus was investigated by immunofluorescent staining. Monospecific antiserum was prepared by immunizing rabbits with MP eluted from SDS-polyacrylamide gels of SDS-disrupted NWS virions. In the productive infection in clone 1-5C-4 cells, MP antigen was first detected over the whole cell at 4 hr after infection, concomitantly with the appearance of hemagglutinin (HA) antigen in the cytoplasm, and bright nuclear fluorescence was then observed. Nucleoprotein (NP) antigen was detected in the nucleus prior to the appearance of fluorescence of MP antigen and thereafter the cytoplasmic fluorescence developed. Late in infection, all of these three antigens were observed predominantly in the cytoplasm with stronger fluorescence at the cell surface. Essentially similar findings were obtained in the abortive infections in L cells and BHK cells. The above results suggest that the membrane protein of influenza A virus is present in the nucleus as well as in the cytoplasm of infected cells.
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PMID:Intracellular development of membrane protein of influenza virus. 33 56

A comparative study of peptide maps of major proteins of hemagglutinin, nucleoprotein, membrane of influenza A virus strains A/WS/33, A/FM/1/47, A/Singapore/1/57, A/USSR/090/77, A/Port Chalmers/1/73 (MRC-11), was carried out. The greatest differences were observed in the peptide maps of heavy and light chains of hemagglutinin of different serotypes. The peptide maps of nucleoprotein and membrane were more similar. The A/USSR/090/77 strain by peptide maps was close to but not identical with the A/FM/1/47 strain. Structural polypeptides of the virion separated by SDS-polyacrylamide gel electrophoresis may be used satisfactorily for comparative studies of influenza virus peptide maps.
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PMID:[Comparative characteristics of the peptide maps of the major proteins of influenza viruses type A]. 43 39

Isolation of virion RNA of influenza virus by the SDS-phenol method from subviral particles obtained from purified virions by treating them with a cation detergent, cetyl-methyl-ammonium bromide, increased RNA yields approximately 2-fold as compared with isolation of this RNA from whole virions.
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PMID:[Use of the cation detergent, cetyltrimethylammonium bromide, in isolating the RNA of the influenza virus]. 48 82

The nucleoprotein (NP) antigen isolated from influenza A virus by solubilization with Triton X-100 (TX-100) and further electrophoresis with SDS-cellulose acetate membrane gave a single band on SDS-polyacrylamide gel electrophoresis. Rabbit anti-serum hyperimmunized with the NP reacted only against the NP antigen. Moreover, a well-defined single precipitin line was shown between the NP and human sera. These results suggested that the NP was possible to detect anti-NP antibody in human serum. Immuno double diffusion (IDD) and single radial immunodiffusion (SRD) tests using the NP were established to detect the anti-NP antibody in human sera. During an epidemic caused by antigenic drift strain, anti-NP antibody was detected by the IDD test in the cases which did not show any significant rise in HAI titer. During a mixed epidemic caused by the different strain of HA antigen, the infection ratio in mass population was revealed more convenient and sensitive by SRD than HAI. The anti-NP antibody was detected by IDD for long periods of one year or more after infection. These results suggest that the detection of anti-NP antibody is applicable to serologic studies, particularly serologic diagnosis and serologic surveys of influenza infection in mass population.
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PMID:Anti-nucleoprotein antibody response in influenza A infection. 49 46

Chicken fibroblasts and MDCK cells were infected with influenza virus labelled with either 3H-uridine or 14C-amino acids, and the location in infected cells and properties of input virus-labelled structures were studied. Input virus RNA and protein were found in the cytoplasm of nuclei 1 h p.i. A part of the intranuclear parental structures was associated with chromatin while the other part could be extracted from nucleoplasm by 0.16 M-NaCl and represented free ribonucleoprotein (RNP) particles. These RNPs sedimented in glycerol velocity gradients at 40 to 70S, very similar to cytoplasmic RNPs, but differed distinctly from them in buoyant density. The bulk of cytoplasmic RNPs after fixation with formaldehyde banded in CsCl at 1.34 g/ml while nucleoplasmic RNPs banded at 1.39 or 1.41 g/ml. RNPs isolated from virions and infected cells contained the NP polypeptide which was revealed by SDS-PAGE analysis as a double band. The ratio of the two bands varied in cytoplasmic and nucleoplasmic RNPs, the lower band being dominant in cytoplasmic but not in nucleoplasmic RNPs. In addition, cytoplasmic RNPs were phosphorylated. The possible significance of intracellular RNP modifications for virus replication is discussed.
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PMID:Cytoplasmic and nuclear input virus RNPs in influenza virus-infected cells. 54 71

Influenza A virus M protein was prepared by electrophoresis in SDS polyacrylamide gel from virus particles which had been pretreated with octylglucoside to remove the surface glycoproteins; M antigens from the influenza virus strains A/Victoria/3/75 (H3N2), A/FPV/Rostock (Hav1N1) and A/chick/Germany/49 (Hav2Neq1) did not protect mice against a lethal challenge infection with the virulent Victoria strain.
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PMID:The M protein of influenza viruses has no immunizing effect. 54 15

Influenza A/ZSSR/053/74 (H3N2) from egg ellantoic fluid was partially purified by absorption and elution on chick erythrocytes and chromatography on Sepharose 2B. Concentrated and partially purified preparation of virus containing 5000 HAV and 80 micrograms of protein per ml was subjected to PAGE in 0.1% SDS. Eleven protein bands were selected of which three were identified as NA, NP and HA.
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PMID:Purification of influenza A virus and preliminary characterization of virus proteins by polyacrylamide gel electrophoresis (PAGE). 74 5

Purified influenza virus contains ribonuclease activity. The enzyme does not hydrolyze viral RNA but both 28 S and 18 S host cell RNA are degraded forming large (about 16 S) and small (about 5 S) fragments with the release of the acid-soluble material. It has an optimum temperature of 37 degrees C, requires no divalent ions, and is inhibited by 0.1 M EDTA and 1% SDS. Treatment with 4 M urea increases enzymatic activity considerably (42%) but is not a prerequisite for eliciting ribonuclease activity suggesting that the enzyme is probably located near the surface of the virus particle. Results show that the observed enzyme activity is virus-associated as no host cell protein is detectable in the purified virus.
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PMID:Association of a ribonuclease with the purified influenza virus. 81 84

Analyses of the polypeptide composition of influenza B viruses by 13 per cent SDS-polyacrylamide gel electrophoresis are reported. The viruses contained polypeptides of eight species ranging in molecular weight from 27,000 to 78,000. Four of them were glocypeptides and were selectively removed from the surface of the virion by Bromelain treatment. One of the blycopeptides was identified as viral neuraminidase. Three antigenically distinct strains of influenza virus, B/Lee/40, B/Massachusetts/1/71 and B/Hong Kong/5/72, showed an essentially identical electrophoretic picture, although strain-to-strain difference was observed in the migration rate of HA1 and HA2 polypeptides.
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PMID:Structural polypeptides of antigenically distinct strains of influenza B virus. 113 2


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