Spike Glycoprotein (1147-1162) | Broadly Neutralizing SARS-CoV-2 S2 Peptide for Universal Vaccine Research

Description

Product Description

Spike Glycoprotein (1147-1162) represents a highly conserved epitope within the S2 subunit of the SARS-CoV-2 spike (S) glycoprotein, a key structural protein responsible for viral entry into host cells. The spike protein mediates the fusion between the viral envelope and host cell membrane through conformational transitions driven by the S1 and S2 domains.

Unlike the more variable receptor-binding domain (RBD) located in S1, the S2 domain contains regions that are functionally conserved across coronaviruses, making it an ideal target for broadly neutralizing antibodies (bnAbs) and pan-coronavirus vaccine design. The peptide region spanning residues 1147–1162 (sequence corresponding to the heptad repeat 2 or HR2 region) has been identified as one of the few linear epitopes capable of inducing cross-reactive neutralizing immunity.

Biological Significance

The S2 region of the spike protein facilitates membrane fusion by forming a six-helix bundle with HR1 and HR2 motifs, bringing viral and host membranes into close proximity. The peptide Spike Glycoprotein (1147-1162) corresponds to a portion of this fusion machinery, and antibodies or mimetic peptides targeting this region effectively block the conformational changes necessary for viral fusion and entry.

In multiple studies, monoclonal antibodies (mAbs) recognizing Spike Glycoprotein (1147-1162) demonstrated cross-neutralization between SARS-CoV-2 and SARS-CoV, and partial cross-reactivity with other zoonotic betacoronaviruses such as BatCoV RaTG13. This epitope has thus emerged as a promising target for universal coronavirus vaccine design, focusing on conserved functional regions rather than variable spike head domains.

Key Research Insights

• Conservation: 100% sequence conservation in most SARS-CoV-2 variants (Alpha, Delta, Omicron) and >95% homology with SARS-CoV.

• Broad Neutralization: mAbs targeting this peptide block both SARS-CoV and SARS-CoV-2 fusion events.

• Fusion Inhibition Mechanism: Prevents formation of the post-fusion six-helix bundle, thereby blocking membrane fusion.

• Vaccine Application: A potential candidate epitope for universal or next-generation SARS-CoV-2 vaccines.

Spike Glycoprotein (1147-1162) has been studied as part of peptide-based vaccine constructs, multivalent display nanoparticles, and diagnostic assays for cross-reactive antibody screening.

Product Specifications

Mechanism of Action

The Spike Glycoprotein (1147-1162) peptide functions by targeting the S2-mediated membrane fusion process, one of the most conserved and essential stages of coronavirus infection.

1. Role in Viral Fusion

The SARS-CoV-2 spike glycoprotein is a trimeric class I fusion protein composed of two main subunits: S1, responsible for receptor binding (via the RBD), and S2, which mediates membrane fusion. Upon binding to ACE2, the S2 subunit undergoes proteolytic cleavage and refolding, exposing the HR1 and HR2 regions that form a six-helix bundle, driving membrane juxtaposition and fusion.

2. HR2-Derived Peptide Neutralization

The 1147–1162 peptide sequence resides in the HR2 region. Antibodies recognizing this region block the formation of the six-helix bundle, preventing the conformational rearrangements that enable viral–host membrane fusion. This mechanism effectively neutralizes infection regardless of mutations in the RBD, offering variant-independent protection.

3. Cross-Species Reactivity

Studies have demonstrated that antibodies targeting this conserved peptide cross-neutralize SARS-CoV and SARS-CoV-2 and recognize epitopes present in bat coronaviruses. This suggests that the peptide mimics an ancestral conserved structure, vital for viral fusion integrity.

4. Applications in Vaccine and Therapeutics

• Universal Vaccine Design: Incorporation into multi-epitope constructs or nanoparticle displays for pan-coronavirus protection.

• Therapeutic Antibody Development: Enables screening of monoclonal antibodies with broad neutralization profiles.

• Fusion Inhibitor Design: Serves as a template for small peptides or peptidomimetics that block HR1–HR2 interaction.

• Diagnostics: Used in serological assays to identify cross-reactive antibodies in convalescent plasma or vaccinated individuals.

By focusing on this stable, fusion-critical region, researchers can design interventions that remain effective even as surface mutations in other domains evolve.

Side Effects

As a synthetic research peptide, Spike Glycoprotein (1147-1162) has no reported clinical side effects, but researchers should consider general laboratory safety and experimental limitations:

• Immunogenicity: May elicit strong immune responses in animal models; dosage optimization is essential.

• Peptide Stability: Peptide degradation may occur in serum or biological fluids; stabilization via formulation is recommended.

• Cross-reactivity: Broad epitope conservation may cause antibody cross-reactivity with related coronaviruses.

• No Cytotoxicity: In vitro assays show no cytotoxic effects at working concentrations.

This peptide is intended for laboratory research only and should not be used in humans or animals for therapeutic or diagnostic purposes.

Disclaimer

For research use only. Not intended for diagnostic, therapeutic, or clinical applications. Handle using appropriate protective measures and follow institutional biosafety guidelines.

Keywords

Spike Glycoprotein (1147-1162), SARS-CoV-2 S2 peptide, coronavirus fusion inhibitor, HR2 epitope, broadly neutralizing antibody, universal vaccine candidate, SARS-CoV cross-reactivity, S2 domain peptide, fusion blocking peptide, pan-coronavirus vaccine research.

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