Antigenic analysis of the F protein of the bovine respiratory syncytial virus: identification of two distinct antigenic sites involved in fusion inhibition

1995 ◽  
Vol 140 (6) ◽  
pp. 993-1005 ◽  
Author(s):  
J. P. Matheise ◽  
K. Walravens ◽  
A. Collard ◽  
P. Coppe ◽  
J. J. Letesson
Keyword(s):  
Respiratory Syncytial Virus ◽  
Bovine Respiratory Syncytial Virus ◽  
Antigenic Analysis ◽  
F Protein ◽  
Virus Identification ◽  
Antigenic Sites ◽  
Fusion Inhibition ◽  
Syncytial Virus

scholarly journals Genetic and antigenic analysis of the G attachment protein of bovine respiratory syncytial virus strains.

1998 ◽  
Vol 79 (12) ◽  
pp. 2939-2946 ◽  
Author(s):  
M Elvander ◽  
A Uttenthal ◽  
S Vilcek ◽  
A Ballagi-Pord√°ny ◽  
C Baule ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
Bovine Respiratory Syncytial Virus ◽  
Antigenic Analysis ◽  
Attachment Protein ◽  
Syncytial Virus ◽  
Virus Strains

Expression inEscherichia coliand Purification of Soluble Forms of the F Protein of Bovine Respiratory Syncytial Virus

1997 ◽  
Vol 9 (2) ◽  
pp. 288-294 ◽  
Author(s):  
Jordi Naval ◽  
Jaume Piñol ◽  
Xavier Rebordosa ◽  
Xavier Serra-Hartmann ◽  
Josep A. Pérez-Pons ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
Bovine Respiratory Syncytial Virus ◽  
F Protein ◽  
Syncytial Virus

Screening of phage-displayed peptide libraries with a monoclonal antibody raised against the F protein of the bovine respiratory syncytial virus

1995 ◽  
Vol 2 (3-4) ◽  
pp. 220-224
Author(s):  
Pascal Mertens ◽  
Jean-Philippe Matheise ◽  
Bernadette Lichtfouse ◽  
Chantal Clavareau ◽  
Jean-Jacques Letesson
Keyword(s):  
Monoclonal Antibody ◽  
Respiratory Syncytial Virus ◽  
Bovine Respiratory Syncytial Virus ◽  
Peptide Libraries ◽  
F Protein ◽  
Syncytial Virus

scholarly journals Global Molecular Epidemiology of Respiratory Syncytial Virus from the 2017−2018 INFORM-RSV Study

2020 ◽  
Vol 59 (1) ◽  
pp. e01828-20
Author(s):  
David E. Tabor ◽  
Fiona Fernandes ◽  
Annefleur C. Langedijk ◽  
Deidre Wilkins ◽  
Robert Jan Lebbink ◽  
...  
Keyword(s):  
South Africa ◽  
Respiratory Syncytial Virus ◽  
Molecular Epidemiology ◽  
Antigenic Site ◽  
Warning System ◽  
F Protein ◽  
Viral Spread ◽  
Antigenic Sites ◽  
Geographic Clustering ◽  
Syncytial Virus

ABSTRACTRespiratory syncytial virus (RSV) is the leading cause of lower respiratory tract infection among infants and young children, resulting in annual epidemics worldwide. INFORM-RSV is a multiyear clinical study designed to describe the global molecular epidemiology of RSV in children under 5 years of age by monitoring temporal and geographical evolution of current circulating RSV strains, F protein antigenic sites, and their relationships with clinical features of RSV disease. During the pilot season (2017–2018), 410 RSV G-F gene sequences were obtained from 476 RSV-positive nasal samples collected from 8 countries (United Kingdom, Spain, The Netherlands, Finland, Japan, Brazil, South Africa, and Australia). RSV B (all BA9 genotype) predominated over RSV A (all ON1 genotype) globally (69.0% versus 31.0%) and in all countries except South Africa. Geographic clustering patterns highlighted wide transmission and continued evolution with viral spread. Most RSV strains were from infants of <1 year of age (81.2%), males (56.3%), and patients hospitalized for >24 h (70.5%), with no differences in subtype distribution. Compared to 2013 reference sequences, variations at F protein antigenic sites were observed for both RSV A and B strains, with high-frequency polymorphisms at antigenic site Ø (I206M/Q209R) and site V (L172Q/S173L/K191R) in RSV B strains. The INFORM-RSV 2017–2018 pilot season establishes an important molecular baseline of RSV strain distribution and sequence variability with which to track the emergence of new strains and provide an early warning system of neutralization escape variants that may impact transmission or the effectiveness of vaccines and MAbs under development.

Antibody responses against epitopes on the F protein of bovine respiratory syncytial virus differ in infected or vaccinated cattle

1997 ◽  
Vol 142 (11) ◽  
pp. 2195-2210 ◽  
Author(s):  
R. S. Schrijver ◽  
E. J. Hensen ◽  
J. P. M. Langedijk ◽  
F. Daus ◽  
W. G. J. Middel ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
Bovine Respiratory Syncytial Virus ◽  
Antibody Responses ◽  
F Protein ◽  
Syncytial Virus

scholarly journals A novel protein expression strategy using recombinant bovine respiratory syncytial virus (BRSV): modifications of the peptide sequence between the two furin cleavage sites of the BRSV fusion protein yield secreted proteins, but affect processing and function of the BRSV fusion protein

2004 ◽  
Vol 85 (7) ◽  
pp. 1815-1824 ◽  
Author(s):  
Patricia König ◽  
Katrin Giesow ◽  
Kathrin Schuldt ◽  
Ursula J. Buchholz ◽  
Günther M. Keil
Keyword(s):  
Respiratory Syncytial Virus ◽  
Amino Acid ◽  
Fusion Protein ◽  
Bovine Respiratory Syncytial Virus ◽  
Peptide Sequence ◽  
Target Cells ◽  
Cleavage Sites ◽  
Furin Cleavage ◽  
F Protein ◽  
Syncytial Virus

The bovine respiratory syncytial virus (BRSV) fusion (F) protein is cleaved at two furin cleavage sites, which results in generation of the disulfide-linked F1 and F2 subunits and release of an intervening peptide of 27 aa (pep27). A series of mutated open reading frames encoding F proteins that lacked the entire pep27, that contained an arbitrarily chosen 23 aa sequence instead of pep27 or in which pep27 was replaced by the amino acid sequences for the bovine cytokines interleukin 2 (boIL2), interleukin 4 (boIL4) or gamma interferon (boIFN-γ) was constructed. Transient expression experiments revealed that the sequence of the intervening peptide influenced intracellular transport, maturation of the F protein and F-mediated syncytium formation. Expression of boIL2, boIL4 or boIFN-γ in place of pep27 resulted in secretion of the cytokines into the culture medium. All mutated F proteins except the boIFN-γ-containing variant could be expressed by and were functional for recombinant BRSV. Characterization of the cell culture properties of the recombinants demonstrated that the amino acid sequence between the two furin cleavage sites affected entry into target cells, direct spreading of virions from cell to cell and virus growth. Secretion of boIL2 and boIL4 into the medium of cells infected with the respective recombinants demonstrated that the F protein can be used to express secreted heterologous bioactive peptides or (glyco)proteins, which might be of interest for the development of novel RSV vaccines.

scholarly journals In silico virtual screening of lead compounds for major antigenic sites in respiratory syncytial virus fusion protein

2021 ◽  
Author(s):  
Shilu Mathew ◽  
Sara Taleb ◽  
Ali Hussein Eid ◽  
Asmaa A. Althani ◽  
Hadi M. Yassine
Keyword(s):  
Respiratory Syncytial Virus ◽  
Virtual Screening ◽  
In Silico ◽  
Neutralizing Antibodies ◽  
Antigenic Site ◽  
Crystallographic Structure ◽  
F Protein ◽  
Antigenic Sites ◽  
Syncytial Virus ◽  
Neutralizing Epitopes

AbstractHuman respiratory syncytial virus (RSV) is a leading ubiquitous respiratory pathogen in newborn infants, young children, and the elderly, with no vaccine available to date. The viral fusion glycoprotein (RSV F) plays an essential role in the infection process, and it is a primary target of neutralizing antibodies, making it an attractive site for vaccine development. With this in view, there is a persistent need to identify selective antiviral drugs against RSV, targeting the major antigenic sites on the F protein. We aimed to conduct a robust in silico high-throughput drug screening of one million compounds to explore potential inhibitors that bind the major antigenic site Ø and site II on RSV F protein, which are the main target of neutralizing antibodies (NAb). We utilized the three-dimensional crystallographic structure of both antigenic site Ø on pre-F and antigenic II on post-F to screen for potential anti-RSV inhibitors. A library of one million small compounds was docked to explore lead binders in the major antigenic sites by using virtual lab bench CLC Drug Discovery. We also performed Quantitative Structure-Activity and Relationship (QSAR) for the lead best binders known for their antiviral activity. Among one million tested ligands, seven ligands (PubChem ID: 3714418, 24787350, 49828911, 24802036, 79824892, 49726463, and 3139884) were identified as the best binders to neutralizing epitopes site Ø and four ligands (PubChem ID: 865999, 17505357, 24802036, and 24285058) to neutralizing epitopes site II, respectively. These binders exhibited significant interactions with neutralizing epitopes on RSV F, with an average of six H bonds, docking energy of − 15.43 Kcal·mol−1, and minimum interaction energy of − 7.45 Kcal·mol−1. Using in silico virtual screening, we identified potential RSV inhibitors that bind two major antigenic sites on the RSV F protein. Using structure-based design and combination-based drug therapy, identified molecules could be modified to generate the next generation anti-RSV drugs.

scholarly journals Baculovirus Expression of the Fusion Protein Gene of Bovine Respiratory Syncytial Virus and Utility of the Recombinant Protein in a Diagnostic Enzyme Immunoassay

1998 ◽  
Vol 36 (4) ◽  
pp. 1105-1108 ◽  
Author(s):  
Manoj K. Pastey ◽  
Siba K. Samal
Keyword(s):  
Respiratory Syncytial Virus ◽  
Polyclonal Antibodies ◽  
Bovine Respiratory Syncytial Virus ◽  
Enzyme Linked Immunosorbent Assay ◽  
Virus Infectivity ◽  
Specific Method ◽  
Serum Samples ◽  
Plaque Reduction Assay ◽  
F Protein ◽  
Syncytial Virus

The fusion (F) protein of bovine respiratory syncytial virus (BRSV) was expressed by using a baculovirus vector. Antigenicity was tested by immunofluorescence analysis with F-specific monoclonal and polyclonal antibodies. Antibodies to recombinant F protein raised in a rabbit neutralized BRSV and human respiratory syncytial virus infectivity when tested in a plaque reduction assay. The recombinant F protein was evaluated as a source of antigen in an enzyme-linked immunosorbent assay (ELISA), and this ELISA was compared with the virus neutralization (VN) test for detecting BRSV antibodies in 10 consecutive serum samples from four calves vaccinated with a live modified BRSV vaccine and from two nonvaccinated control calves. The ELISA with the baculovirus-expressed F protein as an antigen compared favorably with the VN test and is a rapid, sensitive, and specific method for detecting serum antibodies to BRSV.

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