fusion peptide influenza fusion peptides - Peptidecalculator two routes through which the peptides can lower free energy barrier The Crucial Role of the Influenza Fusion Peptide in Viral Entry

Fusionpeptides The influenza fusion peptide (IFP), a critical component of the influenza virus, plays a pivotal role in the fusion process that allows the virus to infect host cells作者：RU Kadam·2017·被引用次数：175—Thepeptideinhibitors bind to the highly conserved stem epitope and block the low pH–induced conformational rearrangements associated with membranefusion.. This highly conserved domain, located within the influenza A spike protein hemagglutinin (HA), is responsible for mediating the critical step of fusion of the viral membrane with the host. Understanding the molecular mechanisms and functions of the IFP is essential for comprehending viral entry and for developing potential antiviral strategies作者：KJ Cross·2009·被引用次数：194—Fusionof theinfluenzavirus envelope with the endosomal membrane of host cells is mediated by the hemagglutinin glycoprotein (HA)..

The influenza virus employs its hemagglutinin glycoprotein (HA) to facilitate cellular infection作者：R Worch·2021·被引用次数：8—Influenza virus entry to the cells requires fusion of viral and cellular membranes. It is mediated by a homotrimeric viral protein hemagglutinin .... A key moiety within the HA is the amphipathic fusion peptide (FP). Upon activation, typically triggered by a low pH environment within the endosome, the HA undergoes significant structural rearrangements.作者：F Collu·2015·被引用次数：11—In this manuscript we report findings targeted at understanding the fusogenic properties and the collective behavior of these trimers of FPpeptides. This conformational change leads to the exposure and insertion of the fusion peptide into the host cell membrane. Research has demonstrated that this insertion is not merely for anchoring the ectodomain but is crucial for acting within the host membrane to promote fusion.

The fusion peptide's primary function is to destabilize lipid bilayers, thereby initiating hemifusion – the fusion of the viral and host membranes. This process is complex and can involve two routes through which the peptides can lower the free energy barrier towards fusion.作者：T Stegmann·2000·被引用次数：176—Fusion is triggered by low pH, which in- duces conformational changes in the protein, leading to insertion of a hydrophobic 'fusion peptide' into the viral. Studies have explored how a single fusion peptide interacts with the bilayers, revealing that it can cause local perturbations that facilitate membrane merging. The influenza virus entry to the cells requires fusion of viral and cellular membranes, and the IFP is the primary mediator of this eventA Specific Point Mutant at Position 1 of the Influenza ....

The composition and functions of the influenza fusion peptide have been extensively investigated. It is understood that the amino acid sequences of viral fusion peptides are thought to be critical for fusion to occur. Mutations within the fusion peptide can significantly impact its ability to promote fusion, highlighting the importance of its specific structure. For instance, changes at the N-terminus of the IFP, such as substitutions of glutamic acid, have been shown to affect fusion. The peptide itself is stable within a pH range of 3-7, becoming less stable at higher pH levels.

The fusion peptide is not just an inert insertor; it actively participates in the membrane merging process. It has been observed that influenza fusion peptides can aggregate and form complex structures within the lipid environment. The assembly of influenza hemagglutinin fusion peptides in a collective manner may contribute to the efficiency of viral entry. Furthermore, research into fusion peptide analogs of influenza virus HA2 has provided insights into the specific structural changes that occur during fusion.

The fusion peptide's mechanism of action is intrinsically linked to the properties of the influenza HA. The hemagglutinin (HA), the membrane-bound fusion protein of the influenza virus, undergoes a low pH-induced conformational change that releases the fusion peptide and initiates the fusion cascade. This process involves the insertion of the hydrophobic fusion peptide into the target membrane, leading to the formation of a fusion pore and the subsequent release of the viral genetic material into the host cell.

The importance of the IFP extends beyond its direct role in entryTransient Excursions to Membrane Core as Determinants .... It represents a highly conserved target, making it a potential site for peptidic fusion inhibitors of influenza virus.Lipid-Mediated Aggregation of Influenza Fusion Peptide These inhibitors can be designed to bind to the conserved stem epitope of the HA and block the low pH-induced conformational rearrangements associated with membrane fusion.

In summary, the influenza fusion peptide is a vital element in the influenza virus's infectious cycle. Its ability to destabilize lipid bilayers and promote fusion is fundamental to viral entry作者：D Lousa·2020·被引用次数：27—Overall, these results indicate that thepeptideis stable in the pH range 3–7, becoming more unstable at pH 9. However, we note that the .... Ongoing research continues to unravel the intricate molecular mechanisms, two modes of fusogenic action for influenza virus fusion, and interactions of these peptides with cellular membranes, paving the way for a deeper understanding of influenza pathogenesis and the development of novel therapeutic interventions.作者：NK Garcia·2023·被引用次数：12—Our data reveal subtype-specific behavior in the regions of HA that undergo structural rearrangement during fusion, including thefusion peptideand HA1/HA2 ...