Literature DB >> 7416969

Processing of influenza HA protein in MDCK cells: components with different mobilities in polyacrylamide gel electrophoresis and their precursor-product relationships.

E I Sklyanskaya, I A Rudneva, T S Vovk, N V Kaverin.   

Abstract

In influenza virus-infected MDCK cells labelled with 14C-chlorella hydrolysate or 35S-methionine a virus-specific protein component is revealed migrating slightly faster than HA protein in polyacrylamide gel electrophoresis. Under chase conditions the component disappears either completely or partially, with a concomitant intensification of the HA band. The rate and extent of this transition are strain-dependent. Both the HA band and the faster moving component are not revealed if the cells are labelled in the presence of 20 mM of D-glucosamine. In primary cell cultures of chick embryos a single HA band with a mobility similar to that of the faster moving component in MDCK cells has been observed. It is suggested that the transition of the label from the faster moving component to the HA band reflects the final step of HA processing specific for MDCK cells.

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Year:  1980        PMID: 7416969     DOI: 10.1007/bf01314542

Source DB:  PubMed          Journal:  Arch Virol        ISSN: 0304-8608            Impact factor:   2.574


  14 in total

1.  Size and chemical composition of influenza virus hemagglutinin chains.

Authors:  C W Ward; A A Dopheide
Journal:  FEBS Lett       Date:  1976-06-15       Impact factor: 4.124

2.  Polypeptides specified by the influenza virus genoma. 2. Assignement of protein coding functions to individual genome segments by in vitro translation.

Authors:  S C Inglis; D J McGeoch; B W Mahy
Journal:  Virology       Date:  1977-05-15       Impact factor: 3.616

3.  Carbohydrates of influenza virus. I. Glycopeptides derived from viral glycoproteins after labeling with radioactive sugars.

Authors:  R T Schwarz; M F Schmidt; U Anwer; H D Klenk
Journal:  J Virol       Date:  1977-08       Impact factor: 5.103

4.  A mutant of influenza virus with a temperature-sensitive defect in the posttranslational processing of the hemagglutinin.

Authors:  J Lohmeyer; H D Klenk
Journal:  Virology       Date:  1979-02       Impact factor: 3.616

5.  Host cell- and virus strain-dependent differences in oligosaccharides of hemagglutinin glycoproteins of influenza A viruses.

Authors:  K Nakamura; R W Compans
Journal:  Virology       Date:  1979-05       Impact factor: 3.616

6.  Plaque formation by influenza viruses in the presence of trypsin.

Authors:  G Appleyard; H B Maber
Journal:  J Gen Virol       Date:  1974-12       Impact factor: 3.891

7.  Inhibition of glycoprotein biosynthesis of influenza virus by D-glucosamine and 2-deoxy-D-glucose.

Authors:  H D Klenk; C Scholtissek; R Rott
Journal:  Virology       Date:  1972-09       Impact factor: 3.616

8.  Cleavage of structural proteins during the assembly of the head of bacteriophage T4.

Authors:  U K Laemmli
Journal:  Nature       Date:  1970-08-15       Impact factor: 49.962

9.  Biosynthesis of the oligosaccharides of influenza viral glycoproteins.

Authors:  N Nakamura; R W Compans
Journal:  Virology       Date:  1979-02       Impact factor: 3.616

10.  Inhibition of glycosylation of the influenza virus hemagglutinin.

Authors:  R T Schwarz; H D Klenk
Journal:  J Virol       Date:  1974-11       Impact factor: 5.103

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  1 in total

1.  Virus-specific and cell-specific RNA transcripts in influenza virus-infected cells: the rate of synthesis and the content in the nuclei.

Authors:  N L Varich; Y Petrík; V R Farashyan; N V Kaverin
Journal:  Arch Virol       Date:  1981       Impact factor: 2.574

  1 in total

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