Conformational studies of a short linear peptide corresponding to a major conserved neutralizing epitope of human respiratory syncytial virus fusion glycoprotein

Biopolymers ◽  
1998 ◽  
Vol 39 (4) ◽  
pp. 537-548 ◽  
Author(s):  
Catherine Toiron ◽  
Juan A. López ◽  
Germán Rivas ◽  
David Andreu ◽  
José A. Melero ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
Human Respiratory Syncytial Virus ◽  
Neutralizing Epitope ◽  
Conformational Studies ◽  
Linear Peptide ◽  
Virus Fusion ◽  
Fusion Glycoprotein ◽  
Syncytial Virus

Purification of human respiratory syncytial virus fusion glycoprotein

2012 ◽  
Vol 81 (1) ◽  
pp. 115-118 ◽  
Author(s):  
Yanpeng Zheng ◽  
Yaning Tang ◽  
Yuanhui Fu ◽  
Jinsheng He ◽  
Xiaobo Wang ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
Human Respiratory Syncytial Virus ◽  
Virus Fusion ◽  
Fusion Glycoprotein ◽  
Syncytial Virus

scholarly journals Fatty Acid Acylation of the Fusion Glycoprotein of Human Respiratory Syncytial Virus

1989 ◽  
Vol 264 (18) ◽  
pp. 10339-10342
Author(s):  
R G Arumugham ◽  
R C Seid ◽  
S Doyle ◽  
S W Hildreth ◽  
P R Paradiso
Keyword(s):  
Fatty Acid ◽  
Respiratory Syncytial Virus ◽  
Human Respiratory Syncytial Virus ◽  
Fusion Glycoprotein ◽  
Syncytial Virus

scholarly journals Trivalency of a Nanobody Specific for the Human Respiratory Syncytial Virus Fusion Glycoprotein Drastically Enhances Virus Neutralization and Impacts Escape Mutant Selection

2016 ◽  
Vol 60 (11) ◽  
pp. 6498-6509 ◽  
Author(s):  
Concepción Palomo ◽  
Vicente Mas ◽  
Laurent Detalle ◽  
Erik Depla ◽  
Olga Cano ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
Antigenic Site ◽  
Serial Passage ◽  
Human Respiratory Syncytial Virus ◽  
Escape Mutant ◽  
Comprehensive Description ◽  
Mutant Selection ◽  
Fusion Glycoprotein ◽  
Escape Mutants ◽  
Syncytial Virus

ABSTRACTALX-0171 is a trivalent Nanobody derived from monovalent Nb017 that binds to antigenic site II of the human respiratory syncytial virus (hRSV) fusion (F) glycoprotein. ALX-0171 is about 6,000 to 10,000 times more potent than Nb017 in neutralization tests with strains of hRSV antigenic groups A and B. To explore the effect of this enhanced neutralization on escape mutant selection, viruses resistant to either ALX-0171 or Nb017 were isolated after serial passage of the hRSV Long strain in the presence of suboptimal concentrations of the respective Nanobodies. Resistant viruses emerged notably faster with Nb017 than with ALX-0171 and in both cases contained amino acid changes in antigenic site II of hRSV F. Detailed binding and neutralization analyses of these escape mutants as well as previously described mutants resistant to certain monoclonal antibodies (MAbs) offered a comprehensive description of site II mutations which are relevant for neutralization by MAbs and Nanobodies. Notably, ALX-0171 showed a sizeable neutralization potency with most escape mutants, even with some of those selected with the Nanobody, and these findings make ALX-0171 an attractive antiviral for treatment of hRSV infections.

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
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