Literature DB >> 3122462

Significance of viral glycoproteins for infectivity and pathogenicity.

R Rott1, H D Klenk.   

Abstract

Disease resulting from virus infection is a complex event depending on the close interaction of viral and cellular factors. Through the application of biochemical and genetic methods, it is now possible to gain an insight into the molecular basis of these interactions. Thus, it has been shown that the glycoproteins of enveloped viruses play a central role in the initiation of infection. They are responsible not only for the adsorption of virions to cellular receptors, but are also for the entry of the genome into the cell by the fusion of viral envelopes with cellular membranes. Evidence is growing that the fusogenic glycoproteins are frequently activated by cellular proteases. The structure of the proteins at the cleavage site and the availability of a suitable protease are critical for tissue tropism, spread of the virus in the infected organism and, thus, for pathogenicity. This will be demonstrated here by the example of the haemagglutinin of influenza viruses.

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Year:  1987        PMID: 3122462      PMCID: PMC7134480          DOI: 10.1016/s0176-6724(87)80028-7

Source DB:  PubMed          Journal:  Zentralbl Bakteriol Mikrobiol Hyg A        ISSN: 0176-6724


  36 in total

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Authors:  H D Klenk; R Rott; M Orlich; J Blödorn
Journal:  Virology       Date:  1975-12       Impact factor: 3.616

2.  Proteolytic cleavage of the viral glycoproteins and its significance for the virulence of Newcastle disease virus.

Authors:  Y Nagai; H D Klenk; R Rott
Journal:  Virology       Date:  1976-07-15       Impact factor: 3.616

3.  Complete nucleotide sequence of the AIDS virus, HTLV-III.

Authors:  L Ratner; W Haseltine; R Patarca; K J Livak; B Starcich; S F Josephs; E R Doran; J A Rafalski; E A Whitehorn; K Baumeister
Journal:  Nature       Date:  1985 Jan 24-30       Impact factor: 49.962

Review 4.  Molecular basis of infectivity and pathogenicity of myxovirus. Brief review.

Authors:  R Rott
Journal:  Arch Virol       Date:  1979       Impact factor: 2.574

5.  Nucleotide sequence of the gene encoding the fusion (F) glycoprotein of human respiratory syncytial virus.

Authors:  P L Collins; Y T Huang; G W Wertz
Journal:  Proc Natl Acad Sci U S A       Date:  1984-12       Impact factor: 11.205

Review 6.  Cotranslational and posttranslational processing of viral glycoproteins.

Authors:  H D Klenk; R Rott
Journal:  Curr Top Microbiol Immunol       Date:  1980       Impact factor: 4.291

Review 7.  Fatty acid binding: a new kind of posttranslational modification of membrane proteins.

Authors:  M F Schmidt
Journal:  Curr Top Microbiol Immunol       Date:  1983       Impact factor: 4.291

Review 8.  Post-translational proteolysis in polypeptide hormone biosynthesis.

Authors:  K Docherty; D F Steiner
Journal:  Annu Rev Physiol       Date:  1982       Impact factor: 19.318

9.  Nucleotide sequence of cdna coding for Semliki Forest virus membrane glycoproteins.

Authors:  H Garoff; A M Frischauf; K Simons; H Lehrach; H Delius
Journal:  Nature       Date:  1980-11-20       Impact factor: 49.962

10.  Role of Staphylococcus protease in the development of influenza pneumonia.

Authors:  M Tashiro; P Ciborowski; H D Klenk; G Pulverer; R Rott
Journal:  Nature       Date:  1987 Feb 5-11       Impact factor: 49.962

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  9 in total

1.  A synthetic peptide corresponding to the cleavage region of VP3 from rotavirus SA11 induces neutralizing antibodies.

Authors:  H J Streckert; H Brüssow; H Werchau
Journal:  J Virol       Date:  1988-11       Impact factor: 5.103

2.  The pH of activation of the hemagglutinin protein regulates H5N1 influenza virus pathogenicity and transmissibility in ducks.

Authors:  Mark L Reed; Olga A Bridges; Patrick Seiler; Jeong-Ki Kim; Hui-Ling Yen; Rachelle Salomon; Elena A Govorkova; Robert G Webster; Charles J Russell
Journal:  J Virol       Date:  2009-11-18       Impact factor: 5.103

3.  Reverse genetics provides direct evidence for a correlation of hemagglutinin cleavability and virulence of an avian influenza A virus.

Authors:  T Horimoto; Y Kawaoka
Journal:  J Virol       Date:  1994-05       Impact factor: 5.103

4.  Monoclonal antipeptide antibodies recognize epitopes upon VP4 and VP7 of simian rotavirus SA11 in infected MA104 cells.

Authors:  G Hansen; F Mehnert; H J Streckert; H Werchau
Journal:  Arch Virol       Date:  1992       Impact factor: 2.574

5.  Proprotein-processing endoproteases PC6 and furin both activate hemagglutinin of virulent avian influenza viruses.

Authors:  T Horimoto; K Nakayama; S P Smeekens; Y Kawaoka
Journal:  J Virol       Date:  1994-09       Impact factor: 5.103

6.  Amino acid residues in the fusion peptide pocket regulate the pH of activation of the H5N1 influenza virus hemagglutinin protein.

Authors:  Mark L Reed; Hui-Ling Yen; Rebecca M DuBois; Olga A Bridges; Rachelle Salomon; Robert G Webster; Charles J Russell
Journal:  J Virol       Date:  2009-02-04       Impact factor: 5.103

7.  Acid stability of the hemagglutinin protein regulates H5N1 influenza virus pathogenicity.

Authors:  Rebecca M DuBois; Hassan Zaraket; Muralidhar Reddivari; Richard J Heath; Stephen W White; Charles J Russell
Journal:  PLoS Pathog       Date:  2011-12-01       Impact factor: 6.823

8.  Influenza HA subtypes demonstrate divergent phenotypes for cleavage activation and pH of fusion: implications for host range and adaptation.

Authors:  Summer E Galloway; Mark L Reed; Charles J Russell; David A Steinhauer
Journal:  PLoS Pathog       Date:  2013-02-14       Impact factor: 6.823

9.  Amino acid substitutions in the H5N1 avian influenza haemagglutinin alter pH of fusion and receptor binding to promote a highly pathogenic phenotype in chickens.

Authors:  Joshua E Sealy; Wendy A Howard; Eleonora Molesti; Munir Iqbal; Nigel J Temperton; Jill Banks; Marek J Slomka; Wendy S Barclay; Jason S Long
Journal:  J Gen Virol       Date:  2021-11       Impact factor: 3.891

  9 in total

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