RSV F Specific Neutra™ Antibody Products

Respiratory syncytial virus (RSV) is a widespread respiratory pathogen causing mild, cold-like symptoms, particularly endangering infants and the elderly due to its contagiousness and respiratory tract targeting. Severe cases necessitate supportive measures like intubation with mechanical ventilation, oxygen therapy, or CPAP. The RSV F protein, crucial for viral entry, is a key target for drug and vaccine development. Its heptad-repeat regions potentially form fusion structures, resembling those in other viruses, facilitating membrane fusion and entry. Strategies blocking such fusion may offer avenues for RSV inhibition, akin to HIV-1 inhibition methods. Prophylactic monoclonal antibody treatments effectively prevent high-risk infant RSV infections.

Its Gene ID: 1494475, and UniProtKB ID: P03420.

RSV F Pathway

The RSV F protein stands as a promising candidate for vaccine and drug development due to its indispensable role in viral entry, high conservation, and pivotal function as the primary virus neutralization antigen. Upon recognition by TLR4, activation of NF-κB signaling is mediated by the recognition of the RSV F protein. TLR4 engages MyD88 and TIRAP as adaptor proteins, with TLR7 utilizing MyD88 similarly, while TLR3 signaling involves TICAM1. These adaptor proteins converge at TRAF3 or TRAF6, initiating their activation and culminating in an antiviral response via downstream signaling pathways.

Fig. 1 Activation of NF-κB signaling via TLR4 recognition of RSV F in innate immune response.^{1, 3}

Applications of Anti-RSV F Antibodies

• Function of Anti-RSV F Neutralizing Antibodies

RSV poses significant mortality risks in older adults and is a major cause of lower respiratory tract infections in children. The RSV F protein displays two discrete structural states: prefusion (preF) and postfusion (postF). While both are potential vaccine targets, preF induces the majority of neutralizing antibodies, making it the preferred antigen for vaccine development. Studies of neutralizing antibodies reveal the recognition of both preF and postF forms, with preF-specific antibodies predominantly derived from IGHV1 germline B-cell clonotypes. Targeting an epitope encompassing Site Ø, Site II, and Site V on the RSV F protein, these antibodies underscore a pivotal vulnerability for combating the pathogen.

Fig. 2 Functional profiling of identified neutralizing antibodies targeting RSV F protein.^{2, 3}

• Anti-RSV F Protein Monoclonal Antibody

The primary proteins of RSV, crucial for its pathogenicity and immunogenicity, are the F glycoproteins found on the viral surface. These glycoproteins facilitate fusion between the viral envelope and respiratory cell lipid membranes. Moreover, they facilitate fusion between adjacent cells, resulting in the formation of syncytia, contributing to the virus's nomenclature. Despite RSV's various subtypes and strains, the F protein remains highly conserved across all variants, making it an ideal target for monoclonal antibody development. Antibodies directed against the extensively conserved A epitope of the F protein hinder infection by blocking virus-host cell membrane fusion, subsequent transmission between cells, and viral replication. Humanized monoclonal antibodies targeting RSV F can effectively prevent lower respiratory tract infections, substantially reducing hospitalizations in high-risk infants caused by RSV.

Creative Biolabs offers a diverse selection of antibodies directed against RSV F, tailored specifically for exploring therapeutic strategies against RSV infection. Furthermore, our experts are available to provide customized blocking or neutralizing antibody options centered around RSV F upon request.

REFERENCES

1. Van Royen, Tessa, et al. "How RSV proteins join forces to overcome the host innate immune response." Viruses 14.2 (2022): 419.
2. Andreano, Emanuele, et al. "The respiratory syncytial virus (RSV) prefusion F‐protein functional antibody repertoire in adult healthy donors." EMBO Molecular Medicine 13.6 (2021): e14035.
3. Distributed under Open Access license CC BY 4.0, without modification.