The Conserved Fusion Peptide Sequence of SARS-CoVs is Insensitive to Ca2+ in Inducing Lipid Mixing in Model Membranes

Insights into the mechanism of action of the bipartite fusion module of SARS-CoV-2 spike protein

ABSTRACT SARS-CoV-2 entry into host cells is mediated by the spike glycoprotein, which promotes fusion between viral and host membranes. Despite its importance, the precise location and mode of action of the fusion peptide, a key spike region that inserts into and perturbs the host membrane, remain elusive. Two regions...

Sequential HIV-1 fusion protein gates control the initiation of host cell entry

HIV-1 fusion with host cells is initiated upon engagement of the viral envelope (Env) protein by its receptors and co-receptors. Receptor-induced conformational changes in the Env ectodomain expose the fusion machinery and position the HIV-1 fusion peptide for release and transit to the host membrane. However, no allos...

Research Paper Comparison of S2 Subunits of the Spike (S) Glycoprotein From Different Strains of SARS-Cov-2 (COVID-19), Aiming to Understand the S2 Role in Virus Transfection Which May Help Its Harness

Biophysical Characterization of K33A Mutation to Stable Signal Peptide Reveals Insights into Lassa Virus Fusion Mechanism

The role of SSP is understood by examining the structural changes that occur within SSP during the fusion process and concluding that the conformational changes undergone by SSP are crucial for LASV fusion activity.

Nanobodies against the S2 region of the spike protein potently neutralize SARS-CoV-2 viruses and show resistance to viral immune escape

The results show the value of nanobody technology for identifying novel neutralising epitopes in the S2 region of beta-coronaviruses with potential for the development of new selective anti-viral agents.

The α-helix-facilitating amino acid sequence EAAAK dramatically increases the antiviral activity of SARS-CoV-2 fusion-inhibitory peptides via the endosome fusion pathway

It is demonstrated that the C-terminal EAAAK motif in IPB29—originally designed as a rigid linker connecting the peptide backbone to the lipid moiety—is critical for its antiviral activity and functions via the endosomal fusion pathway.