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 Reduction of Respiratory Syncytial Virus (RSV) in Tracheal Aspirates in Intubated Infants by Use of Humanized Monoclonal Antibody to RSV F Protein

1998 ◽  
Vol 178 (6) ◽  
pp. 1555-1561 ◽  
Author(s):  
Richard Malley ◽  
John DeVincenzo ◽  
Octavio Ramilo ◽  
Penelope H. Dennehy ◽  
H. Cody Meissner ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Respiratory Syncytial Virus ◽  
F Protein ◽  
Humanized Monoclonal Antibody ◽  
Syncytial Virus ◽  
Tracheal Aspirates

Detection of Respiratory Syncytial Virus in Nasopharyngeal Secretions by 24-Well Plate Precentrifugation Assay Using a Monoclonal Antibody Against F Protein

2000 ◽  
Vol 31 (1) ◽  
pp. 93-96 ◽  
Author(s):  
Clara Savón ◽  
Angel Goyenechea ◽  
Angel Valdivia ◽  
Danay Chacón ◽  
Reynel Cancio ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Respiratory Syncytial Virus ◽  
F Protein ◽  
Syncytial Virus

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

Monoclonal antibody based in vitro potency assay as a predictor of antigenic integrity and in vivo immunogenicity of a Respiratory Syncytial Virus post-fusion F-protein based vaccine

Vaccine ◽  
2018 ◽  
Vol 36 (12) ◽  
pp. 1673-1680
Author(s):  
Matieyendou Didier Djagbare ◽  
Li Yu ◽  
Arun Parupudi ◽  
Jenny Sun ◽  
Melissa L. Coughlin ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Respiratory Syncytial Virus ◽  
Potency Assay ◽  
F Protein ◽  
Syncytial Virus

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 Bovine respiratory syncytial virus: immunohistochemichal detection in mouse and bovine tissues using a Mab against human respiratory syncytial virus

2006 ◽  
Vol 58 (6) ◽  
pp. 973-981 ◽  
Author(s):  
R.S. Almeida ◽  
F.R. Spilki ◽  
P.M. Roehe ◽  
L.M.C. Verinaud ◽  
C.W. Arns
Keyword(s):  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
Respiratory Syncytial Virus ◽  
Respiratory Disease ◽  
Cell Cultures ◽  
Post Infection ◽  
Bovine Respiratory Syncytial Virus ◽  
Human Respiratory Syncytial Virus ◽  
Clinical Samples ◽  
Syncytial Virus

An immunoistochemical (IHC) test was developed to detect bovine respiratory syncytial virus (BRSV) in cell cultures and tissues of experimentally infected mice and calves, using a commercial monoclonal antibody (Mab) against human respiratory syncytial virus (HRSV), as a less expensive alternative, instead of producing specific monoclonal antibodies to BRSV. Clinical samples from calves suffering respiratory disease were also submitted to this test. IHC detected BRSV antigens in mouse tracheas (3, 5 and 7 days post-infection) and lungs (5 and 7 days post-infection), and in one of three lungs from experimentally infected calves. Lungs samples from two naturally infected calves were tested and resulted positive for BRSV by the IHC test. These results suggest that this test may be used in the future for diagnosis as well as a useful tool to assess the distribution of BRSV infections in Brazilian herds.

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.

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