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首页> 外文期刊>Biochemistry >Enhanced Cholesterol-Dependent Hemifusion by Internal Fusion Peptide 1 of SARS Coronavirus-2 Compared to Its N-Terminal Counterpart
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Enhanced Cholesterol-Dependent Hemifusion by Internal Fusion Peptide 1 of SARS Coronavirus-2 Compared to Its N-Terminal Counterpart

机译：与其N末端对应物相比，通过SARS Coronavirus-2的内融合肽1增强胆固醇依赖性偏移。

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摘要

Membrane fusion is an important step for the entry of the lipid-sheathed viruses into the host cells. The fusion process is being carried out by fusion proteins present in the viral envelope. The class I virus contains a 20–25 amino acid sequence at its N-terminal of the fusion domain, which is instrumental in fusion and is called as a “fusion peptide”. However, severe acute respiratory syndrome (SARS) coronaviruses contain more than one fusion peptide sequences. We have shown that the internal fusion peptide 1 (IFP1) of SARS-CoV-2 is far more efficient than its N-terminal counterpart (FP) to induce hemifusion between small unilamellar vesicles. Moreover, the ability of IFP1 to induce hemifusion formation increases dramatically with growing cholesterol content in the membrane. Interestingly, IFP1 is capable of inducing hemifusion but fails to open the pore.
机译：膜融合是脂质鞘病毒进入宿主细胞的重要步骤。融合过程是由存在于病毒包膜中的融合蛋白进行的。I类病毒在其融合域的N端含有一个20-25个氨基酸序列，该序列有助于融合，被称为“融合肽”。然而，严重急性呼吸综合征（SARS）冠状病毒包含不止一个融合肽序列。我们已经证明，SARS-CoV-2的内部融合肽1（IFP1）比其N末端对应物（FP）更有效地诱导小单板小泡之间的半融合。此外，随着膜中胆固醇含量的增加，IFP1诱导半融合形成的能力显著增加。有趣的是，IFP1能够诱导半融合，但不能打开毛孔。

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