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

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

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

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

scholarly journals Distinct patterns of within-host virus populations between two subgroups of human respiratory syncytial virus

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Gu-Lung Lin ◽  
Simon B. Drysdale ◽  
Matthew D. Snape ◽  
Daniel O’Connor ◽  
Anthony Brown ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Respiratory Syncytial Virus ◽  
Population Level ◽  
Human Respiratory Syncytial Virus ◽  
Sequencing Data ◽  
F Protein ◽  
Consensus Sequences ◽  
Escape Mutants ◽  
Syncytial Virus ◽  
Acid Alteration

AbstractHuman respiratory syncytial virus (RSV) is a major cause of lower respiratory tract infection in young children globally, but little is known about within-host RSV diversity. Here, we characterised within-host RSV populations using deep-sequencing data from 319 nasopharyngeal swabs collected during 2017–2020. RSV-B had lower consensus diversity than RSV-A at the population level, while exhibiting greater within-host diversity. Two RSV-B consensus sequences had an amino acid alteration (K68N) in the fusion (F) protein, which has been associated with reduced susceptibility to nirsevimab (MEDI8897), a novel RSV monoclonal antibody under development. In addition, several minor variants were identified in the antigenic sites of the F protein, one of which may confer resistance to palivizumab, the only licensed RSV monoclonal antibody. The differences in within-host virus populations emphasise the importance of monitoring for vaccine efficacy and may help to explain the different prevalences of monoclonal antibody-escape mutants between the two subgroups.

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

scholarly journals Enhanced Neutralizing Antibody Response Induced by Respiratory Syncytial Virus Prefusion F Protein Expressed by a Vaccine Candidate

2015 ◽  
Vol 89 (18) ◽  
pp. 9499-9510 ◽  
Author(s):  
Bo Liang ◽  
Sonja Surman ◽  
Emerito Amaro-Carambot ◽  
Barbora Kabatova ◽  
Natalie Mackow ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
Clinical Evaluation ◽  
Genetic Stability ◽  
Vaccine Candidate ◽  
Early Passage ◽  
F Protein ◽  
Syncytial Virus ◽  
Human Parainfluenza Virus ◽  
Type 3

ABSTRACTRespiratory syncytial virus (RSV) and human parainfluenza virus type 3 (HPIV3) are the first and second leading viral agents of severe respiratory tract disease in infants and young children worldwide. Vaccines are not available, and an RSV vaccine is particularly needed. A live attenuated chimeric recombinant bovine/human PIV3 (rB/HPIV3) vector expressing the RSV fusion (F) glycoprotein from an added gene has been under development as a bivalent vaccine against RSV and HPIV3. Previous clinical evaluation of this vaccine candidate suggested that increased genetic stability and immunogenicity of the RSV F insert were needed. This was investigated in the present study. RSV F expression was enhanced 5-fold by codon optimization and by modifying the amino acid sequence to be identical to that of an early passage of the original clinical isolate. This conferred a hypofusogenic phenotype that presumably reflects the original isolate. We then compared vectors expressing stabilized prefusion and postfusion versions of RSV F. In a hamster model, prefusion F induced increased quantity and quality of RSV-neutralizing serum antibodies and increased protection against wild-type (wt) RSV challenge. In contrast, a vector expressing the postfusion F was less immunogenic and protective. The genetic stability of the RSV F insert was high and was not affected by enhanced expression or the prefusion or postfusion conformation of RSV F. These studies provide an improved version of the previously well-tolerated rB/HPIV3-RSV F vaccine candidate that induces a superior RSV-neutralizing serum antibody response.IMPORTANCERespiratory syncytial virus (RSV) and human parainfluenza virus type 3 (HPIV3) are two major causes of pediatric pneumonia and bronchiolitis. The rB/HPIV3 vector expressing RSV F protein is a candidate bivalent live vaccine against HPIV3 and RSV. Previous clinical evaluation indicated the need to increase the immunogenicity and genetic stability of the RSV F insert. Here, we increased RSV F expression by codon optimization and by modifying the RSV F amino acid sequence to conform to that of an early passage of the original isolate. This resulted in a hypofusogenic phenotype, which likely represents the original phenotype before adaptation to cell culture. We also included stabilized versions of prefusion and postfusion RSV F protein. Prefusion RSV F induced a larger quantity and higher quality of RSV-neutralizing serum antibodies and was highly protective. This provides an improved candidate for further clinical evaluation.

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