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

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 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.

scholarly journals Shifting immunodominance pattern of two cytotoxic T-lymphocyte epitopes in the F glycoprotein of the Long strain of respiratory syncytial virus

2004 ◽  
Vol 85 (11) ◽  
pp. 3229-3238 ◽  
Author(s):  
Carolina Johnstone ◽  
Patricia de León ◽  
Francisco Medina ◽  
José A. Melero ◽  
Blanca García-Barreno ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
Vaccinia Virus ◽  
T Lymphocyte ◽  
Cytotoxic T Lymphocyte ◽  
Recombinant Vaccinia Virus ◽  
Recombinant Vaccinia ◽  
F Protein ◽  
Syncytial Virus ◽  
Lymphocyte Responses

Human respiratory syncytial virus (RSV) is a major cause of respiratory infection in children and in the elderly. The RSV fusion (F) glycoprotein has long been recognized as a vaccine candidate as it elicits cytotoxic T-lymphocyte (CTL) and antibody responses. Two murine H-2Kd-restricted CTL epitopes (F85–93 and F92–106) are known in the F protein of the A2 strain of RSV. F-specific CTL lines using BCH4 fibroblasts that are persistently infected with the Long strain of human RSV as stimulators were generated, and it was found that in this strain only the F85–93 epitope is conserved. Motif based epitope prediction programs and an F2 chain deleted F protein encoded in a recombinant vaccinia virus enabled identification of a new epitope in the Long strain, F249–258, which is presented by Kd as a 9-mer (TYMLTNSEL) or a 10-mer (TYMLTNSELL) peptide. The results suggest that the 10-mer might be a naturally processed endogenous Kd ligand. The CD8+ T-lymphocyte responses to epitopes F85–93 and F249–258 present in the F protein of RSV Long were found to be strongly skewed to F85–93 in in vitro multispecific CTL lines and in vivo during a secondary response to a recombinant vaccinia virus that expresses the entire F protein. However, no hierarchy in CD8+ T-lymphocyte responses to F85–93 and F249–258 epitopes was observed in vivo during a primary response.

Immunogenicity and efficacy of codon optimized DNA vaccines encoding the F-protein of respiratory syncytial virus

Vaccine ◽  
2007 ◽  
Vol 25 (41) ◽  
pp. 7271-7279 ◽  
Author(s):  
Nicola Ternette ◽  
Bettina Tippler ◽  
Klaus Überla ◽  
Thomas Grunwald
Keyword(s):  
Respiratory Syncytial Virus ◽  
Dna Vaccines ◽  
F Protein ◽  
Syncytial Virus
Sign in / Sign up

Export Citation Format

Share Document