scholarly journals Effect of Proteolytic Processing at Two Distinct Sites on Shape and Aggregation of an Anchorless Fusion Protein of Human Respiratory Syncytial Virus and Fate of the Intervening Segment

Virology ◽  
2002 ◽  
Vol 298 (2) ◽  
pp. 317-326 ◽  
Author(s):  
M. Begoña Ruiz-Argüello ◽  
Luis González-Reyes ◽  
Leslie J. Calder ◽  
Concepción Palomo ◽  
Diana Martı́n ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
Fusion Protein ◽  
Human Respiratory Syncytial Virus ◽  
Proteolytic Processing ◽  
Syncytial Virus

Molecular characterization of the glycoprotein and fusion protein in human respiratory syncytial virus subgroup A: Emergence of ON-1 genotype in Iran

2019 ◽  
Vol 71 ◽  
pp. 166-178 ◽  
Author(s):  
Somayeh Shatizadeh Malekshahi ◽  
Shaghayegh Razaghipour ◽  
Yazdan Samieipoor ◽  
Farhad B. Hashemi ◽  
Ali Akbar Rahbari Manesh ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
Fusion Protein ◽  
Molecular Characterization ◽  
Human Respiratory Syncytial Virus ◽  
Syncytial Virus

scholarly journals Molecular Epidemiology and Phylodynamics of the Human Respiratory Syncytial Virus Fusion Protein in Northern Taiwan

PLoS ONE ◽  
2013 ◽  
Vol 8 (5) ◽  
pp. e64012 ◽  
Author(s):  
Hsin Chi ◽  
Hsin-Fu Liu ◽  
Li-Chuan Weng ◽  
Nai-Yu Wang ◽  
Nan-Chang Chiu ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
Fusion Protein ◽  
Molecular Epidemiology ◽  
Human Respiratory Syncytial Virus ◽  
Virus Fusion ◽  
Syncytial Virus ◽  
Northern Taiwan

Immunovirological studies on human respiratory syncytial virus structural proteins

1986 ◽  
Vol 32 (1) ◽  
pp. 15-21 ◽  
Author(s):  
Michel Trudel ◽  
Francine Nadon ◽  
Cécile Séguin ◽  
Simone Ghoubril ◽  
Pierre Payment ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
Fusion Protein ◽  
Neutralizing Antibodies ◽  
Sodium Dodecyl ◽  
Human Respiratory Syncytial Virus ◽  
Structural Proteins ◽  
Membrane Glycoproteins ◽  
Protein Dimer ◽  
Syncytial Virus ◽  
Nucleoprotein N

Immunovirological studies suggest that human respiratory syncytial virus may well be composed of five structural proteins as are other members of the Paramyxoviridae family: the two external membrane glycoproteins H (90 000) and Fo (F1, 49 000; F2, 20 000; disulfide linked), the internal membrane protein M (34 000), the nucleoprotein N (42 000), and a protein (78 000) designated P that could be the equivalent of the polymerase of the morbillivirus and paramyxovirus genus. Neutralizing monoclonal antibodies showed, by immunoprecipitation and immunoblotting, that the fusion protein carries neutralizing epitopes. One monoclonal antibody, which shows a high neutralizing titer, immunoblotted directly with the F1 fragment (49 000) of the fusion protein. Analysis in mice of the immunogenicity of the structural proteins separated on sodium dodecyl sulphate gels indicated that, under our conditions, only the fusion protein dimer Fo and its F1 fragment were capable of inducing neutralizing antibodies.

scholarly journals Thermostability of the human respiratory syncytial virus fusion protein before and after activation: implications for the membrane-fusion mechanism

2004 ◽  
Vol 85 (12) ◽  
pp. 3677-3687 ◽  
Author(s):  
M. Begoña Ruiz-Argüello ◽  
Diana Martín ◽  
Steve A. Wharton ◽  
Lesley J. Calder ◽  
Steve R. Martín ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
Fusion Protein ◽  
Membrane Fusion ◽  
Human Respiratory Syncytial Virus ◽  
Virus Fusion ◽  
Before And After ◽  
Syncytial Virus

Expression and purification of human respiratory syncytial virus recombinant fusion protein

2008 ◽  
Vol 62 (2) ◽  
pp. 146-152 ◽  
Author(s):  
Helen A. Arcuri ◽  
Luciano H. Apponi ◽  
Sandro R. Valentini ◽  
Edison L. Durigon ◽  
Walter F. de Azevedo ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
Fusion Protein ◽  
Human Respiratory Syncytial Virus ◽  
Recombinant Fusion Protein ◽  
Expression And Purification ◽  
Virus Recombinant ◽  
Syncytial Virus

scholarly journals Electron Microscopy of the Human Respiratory Syncytial Virus Fusion Protein and Complexes That It Forms with Monoclonal Antibodies

Virology ◽  
2000 ◽  
Vol 271 (1) ◽  
pp. 122-131 ◽  
Author(s):  
Leslie J. Calder ◽  
Luis González-Reyes ◽  
Blanca García-Barreno ◽  
Steve A. Wharton ◽  
John J. Skehel ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Monoclonal Antibodies ◽  
Respiratory Syncytial Virus ◽  
Fusion Protein ◽  
Human Respiratory Syncytial Virus ◽  
Virus Fusion ◽  
Syncytial Virus

scholarly journals N-Glycans of F Protein Differentially Affect Fusion Activity of Human Respiratory Syncytial Virus

2001 ◽  
Vol 75 (10) ◽  
pp. 4744-4751 ◽  
Author(s):  
Gert Zimmer ◽  
Ina Trotz ◽  
Georg Herrler
Keyword(s):  
Respiratory Syncytial Virus ◽  
Cell Surface ◽  
Fusion Protein ◽  
Syncytium Formation ◽  
Human Respiratory Syncytial Virus ◽  
Fusion Activity ◽  
Triple Mutant ◽  
Activity Increase ◽  
F Protein ◽  
Syncytial Virus

ABSTRACT The human respiratory syncytial virus (Long strain) fusion protein contains six potential N-glycosylation sites: N27, N70, N116, N120, N126, and N500. Site-directed mutagenesis of these positions revealed that the mature fusion protein contains three N-linked oligosaccharides, attached to N27, N70, and N500. By introducing these mutations into the F gene in different combinations, four more mutants were generated. All mutants, including a triple mutant devoid of any N-linked oligosaccharide, were efficiently transported to the plasma membrane, as determined by flow cytometry and cell surface biotinylation. None of the glycosylation mutations interfered with proteolytic activation of the fusion protein. Despite similar levels of cell surface expression, the glycosylation mutants affected fusion activity in different ways. While the N27Q mutation did not have an effect on syncytium formation, loss of the N70-glycan caused a fusion activity increase of 40%. Elimination of both N-glycans (N27/70Q mutant) reduced the fusion activity by about 50%. A more pronounced reduction of the fusion activity of about 90% was observed with the mutants N500Q, N27/500Q, and N70/500Q. Almost no fusion activity was detected with the triple mutant N27/70/500Q. These data indicate that N-glycosylation of the F2 subunit at N27 and N70 is of minor importance for the fusion activity of the F protein. The single N-glycan of the F1 subunit attached to N500, however, is required for efficient syncytium formation.

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