Related Experiment Video

Updated: Sep 28, 2026

An Improved and High Throughput Respiratory Syncytial Virus RSV Micro-neutralization Assay
09:14

An Improved and High Throughput Respiratory Syncytial Virus RSV Micro-neutralization Assay

Published on: January 26, 2019

11.6K

Potent single-domain antibodies that arrest respiratory syncytial virus fusion protein in its prefusion state

Iebe Rossey1,2, Morgan S A Gilman3, Stephanie C Kabeche3

  • 1Medical Biotechnology Center, VIB, Technologiepark 927, Ghent B-9052, Belgium.

Nature Communications
|February 15, 2017
PubMed

Insights

Two llama-derived antibodies neutralize respiratory syncytial virus (RSV) by targeting its fusion protein (F). These potent VHHs show promise as antiviral agents against RSV infections in mice.

Area of Science:

  • Virology
  • Immunology
  • Structural Biology

Background:

  • Human respiratory syncytial virus (RSV) is a leading cause of lower respiratory tract infections in young children.
  • The RSV fusion (F) protein is essential for viral entry and a key target for antiviral therapies.
  • The prefusion conformation of the F protein is the primary target of neutralizing antibodies.

Purpose of the Study:

  • To identify and characterize novel llama-derived single-domain antibodies (VHHs) with potent RSV-neutralizing activity.
  • To investigate the binding characteristics and structural basis of VHH interaction with the prefusion RSV F protein.
  • To evaluate the in vivo efficacy of these VHHs against RSV infection.

Main Methods:

  • Generation and screening of llama-derived single-domain antibodies (VHHs).
  • Biochemical and biophysical characterization of VHH binding to prefusion RSV F protein, including affinity measurements.
  • X-ray crystallography to determine the structures of VHH-F protein complexes.
  • In vivo studies in RSV-challenged mice to assess viral replication and inflammatory responses.

Main Results:

  • Two VHHs were identified with potent neutralizing activity against RSV.
  • These VHHs exhibit picomolar affinity and selective binding to the prefusion conformation of the RSV F protein.
  • Structural analysis revealed that the VHHs bind to a conserved cavity on the prefusion F protein.
  • In vivo studies demonstrated that the VHHs reduced RSV replication and inflammatory cell infiltration in the lungs of infected mice.

Conclusions:

  • Llama-derived VHHs targeting the prefusion RSV F protein are potent antiviral agents.
  • These VHHs offer a promising therapeutic strategy for combating RSV infections.
  • The identified VHHs provide valuable tools for further research into RSV pathogenesis and vaccine development.

More Related Videos

Generation, Amplification, and Titration of Recombinant Respiratory Syncytial Viruses11:48

Generation, Amplification, and Titration of Recombinant Respiratory Syncytial Viruses

Published on: April 4, 2019

17.4K
Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus09:08

Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus

Published on: July 27, 2021

4.2K

Related Concept Videos

Respiratory Syncytial Virus Disease01:29

Respiratory Syncytial Virus Disease

Human respiratory syncytial virus (RSV) is a widespread pathogen that primarily targets infants and young children but also poses a serious health risk to elderly and immunocompromised individuals. Belonging to the Pneumoviridae family, RSV is a negative-sense, single-stranded RNA virus within the Pneumovirus genus. Its global health burden is significant, with millions of cases annually resulting in hospitalizations and mortality, particularly in resource-limited settings. Although most...
Inhibitors of Viral Protein Synthesis01:30

Inhibitors of Viral Protein Synthesis

Protein synthesis is indispensable for viral replication, as viruses lack the cellular machinery required for this process and must hijack the host's translational apparatus. In response, host cells deploy a critical innate immune defense involving interferons, specialized cytokines that play a central role in inhibiting viral propagation.Upon viral detection, infected cells release interferons that bind to receptors on adjacent uninfected cells, activating the JAK-STAT signaling pathway and...
Inhibitors Of Virion Release01:25

Inhibitors Of Virion Release

Viral replication and dissemination rely on efficient mechanisms for host cell entry, genome replication, assembly, and release. Influenza viruses, such as types A and B, are negative-sense single-stranded RNA viruses with a segmented genome, that depend on two critical surface glycoproteins to carry out these processes: hemagglutinin (HA) and neuraminidase (NA). HA initiates infection by binding to sialic acid residues on the surface of host epithelial cells, facilitating receptor-mediated...
Inhibitors of Virion Maturation and Assembly01:19

Inhibitors of Virion Maturation and Assembly

As part of their replication cycle, certain viruses synthesize long precursor proteins called polyproteins within infected host cells. In human immunodeficiency virus (HIV), two major polyproteins are produced: Gag and Gag-Pol. The Gag polyprotein supplies the structural components of the virus, while Gag-Pol includes essential viral enzymes such as reverse transcriptase, integrase, and protease. After synthesis, these polyproteins move to the host cell membrane, where they assemble into an...