scholarly journals Generation and Characterization of ALX-0171, a Potent Novel Therapeutic Nanobody for the Treatment of Respiratory Syncytial Virus Infection

2015 ◽  
Vol 60 (1) ◽  
pp. 6-13 ◽  
Author(s):  
Laurent Detalle ◽  
Thomas Stohr ◽  
Concepción Palomo ◽  
Pedro A. Piedra ◽  
Brian E. Gilbert ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
Virus Infection ◽  
Limit Of Detection ◽  
Antigenic Site ◽  
Antiviral Compound ◽  
F Protein ◽  
Fixed Concentration ◽  
Syncytial Virus ◽  
Tract Infections

ABSTRACTRespiratory syncytial virus (RSV) is an important causative agent of lower respiratory tract infections in infants and elderly individuals. Its fusion (F) protein is critical for virus infection. It is targeted by several investigational antivirals and by palivizumab, a humanized monoclonal antibody used prophylactically in infants considered at high risk of severe RSV disease. ALX-0171 is a trimeric Nanobody that binds the antigenic site II of RSV F protein with subnanomolar affinity. ALX-0171 demonstratedin vitroneutralization superior to that of palivizumab against prototypic RSV subtype A and B strains. Moreover, ALX-0171 completely blocked replication to below the limit of detection for 87% of the viruses tested, whereas palivizumab did so for 18% of the viruses tested at a fixed concentration. Importantly, ALX-0171 was highly effective in reducing both nasal and lung RSV titers when delivered prophylactically or therapeutically directly to the lungs of cotton rats. ALX-0171 represents a potent novel antiviral compound with significant potential to treat RSV-mediated disease.

scholarly journals DEVELOPMENT AND PROPERTIES OF NEUTRALIZING MONOCLONAL ANTIBODIES FOR FUSION PROTEIN OF RESPIRATORY SYNCYTIAL VIRUS

2019 ◽  
Vol 64 (2) ◽  
pp. 90-96
Author(s):  
A. A. Kushch ◽  
R. R. Klimova ◽  
N. E. Fedorova ◽  
O. V. Masalova ◽  
A. A. Niconova ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Respiratory Syncytial Virus ◽  
Culture Method ◽  
The Elderly ◽  
F Protein ◽  
Wide Range ◽  
Infected Cells ◽  
Syncytial Virus ◽  
Tract Infections

Introduction. Respiratory syncytial virus (RSV) is the most common cause of lower respiratory tract infections in infants and the elderly. The absence of a wide range of therapeutic drugs and vaccines indicates to the high relevance of the development of new effective drugs for the prevention and treatment of RSV infections. Purpose: to obtain highly active and specific monoclonal antibodies (MAbs) capable of detecting RSV in infected cells and neutralizing the infectious activity of the virus in vitro. Material and methods. RSV reference strains of group A 2 subgroups (A2 and Long) were propagated in HEp-2 and MA-104 cell lines, respectively. Mice were immunized with purified RSV A2 virus. MAbs were obtained using hybridoma technology. Results. A panel of 6 MAbs reacting with RSV strains А2 and Long has been obtained. Four MAbs were IgG (IgG2a or IgG2b subtype), two MAbs were IgM. All MAbs reacted with RSV F-protein in immunochemical tests. The MAbs actively reacted with RSV in ELISA, in immufluorescence and peroxidase staining of infected cells, and in immunodot test. Five out of 6 MAbs neutralized of RSV in cell culture. Different properties of MAbs suggest that they target different antigenic sites of F-protein. Discussion. Comparative analysis suggests that the obtained MAbs can be used for the development of diagnostic preparations, for RSV detection in clinical materials and confirmation of infection etiology by rapid culture method. Conclusion. High activity and specificity of MAbs indicate that they can serve as a basis for development vaccines and preventive medicines.

scholarly journals Ficus religiosa L. bark extracts inhibit human rhinovirus and respiratory syncytial virus infection in vitro

2015 ◽  
Vol 176 ◽  
pp. 252-257 ◽  
Author(s):  
Valeria Cagno ◽  
Andrea Civra ◽  
Ravi Kumar ◽  
Subhankar Pradhan ◽  
Manuela Donalisio ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
Virus Infection ◽  
Respiratory Syncytial Virus Infection ◽  
Human Rhinovirus ◽  
Ficus Religiosa ◽  
Syncytial Virus

scholarly journals Respiratory syncytial virus infection and meningococcal disease

1996 ◽  
Vol 117 (1) ◽  
pp. 107-111 ◽  
Author(s):  
J. M. Stuart ◽  
K. Cartwright ◽  
N. J. Andrews
Keyword(s):  
Time Series ◽  
Respiratory Syncytial Virus ◽  
Virus Infection ◽  
Meningococcal Disease ◽  
Respiratory Tract Infections ◽  
Seasonal Component ◽  
Syncytial Virus ◽  
Tract Infections ◽  
Viral Respiratory ◽  
Do So

SummaryAlthough viral respiratory tract infections may predispose to meningococcal disease, strong evidence that they do so exists only for influenza. Data on laboratory reported cases of respiratory syncytial virus (RSV) infections and meningococcal disease in England and Wales from mid-1989 to mid-1994 were analysed. Although the rise in RSV cases preceded the rise in meningococcal disease cases each winter, the interval between the rise and fall of the two diseases was inconsistent, no association was found between time series after removal of the seasonal component, and there was no evidence that more cases of meningococcal disease occurred in winters with more RSV disease. RSV may have less effect on the two most likely mechanisms whereby influenza predisposes to meningococcal disease, namely lowered immunity and impaired pharyngeal defences.

scholarly journals Characterization of the epitope for anti-human respiratory syncytial virus F protein monoclonal antibody 101F using synthetic peptides and genetic approaches

2007 ◽  
Vol 88 (10) ◽  
pp. 2719-2723 ◽  
Author(s):  
Sheng-Jiun Wu ◽  
Albert Schmidt ◽  
Eric J. Beil ◽  
Nicole D. Day ◽  
Patrick J. Branigan ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
Antigenic Site ◽  
Neutralizing Antibody ◽  
Human Respiratory Syncytial Virus ◽  
Peptide Sequence ◽  
F Protein ◽  
Syncytial Virus ◽  
A Minor ◽  
Key Residues

Chimeric 101F (ch101F) is a mouse–human chimeric anti-human respiratory syncytial virus (HRSV) neutralizing antibody that recognizes residues within antigenic site IV, V, VI of the fusion (F) glycoprotein. The binding of ch101F to a series of peptides overlapping aa 422–438 spanning antigenic site IV, V, VI was analysed. Residues 423–436 comprise the minimal peptide sequence for ch101F binding. Substitution analysis revealed that R429 and K433 are critical for ch101F binding, whilst K427 makes a minor contribution. Binding of ch101F to a series of single mutations at positions 427, 429 and 433 in the F protein expressed recombinantly on the cell surface confirmed the peptide results. Sequence analysis of viruses selected for resistance to neutralization by ch101F indicated that a single change (K433T) in the F protein allowed ch101F escape. The results confirm that ch101F and palivizumab have different epitope specificity and define key residues for ch101F recognition.

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