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SARS-CoV-2 proteins

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    Enhanced Cholesterol-dependent Hemifusion by Internal Fusion Peptide 1 of SARS Coronavirus-2 Compared to its N-terminal Counterpart

    Authors: Gourab Prasad Pattnaik; Surajit Bhattacharjya; Hirak Chakraborty; Yechun Xu; Chunfan Huang; Can Jin; Zhenyun Du; Xia Chen; Yaqi Ding; Hao Sun; Meixia Li; Rongjuan Pei; Shihai Zhang; Minbo Su; Yi Zhang; Jia Li; Laura Esparcia; Ana Marcos-Jimenez; Santiago Sanchez-Alonso; Irene Llorente; Joan B. Soriano; Carmen Suarez Fernandez; Rosario Garcia-Vicuna; Julio Ancochea; Jesus Sanz; Cecilia Munoz-Calleja; Rafael de la Camara; Alfonso Canabal Berlanga; Isidoro Gonzalez-Alvaro; Laura Cardenoso; John R Bradley

    doi:10.1101/2021.01.14.426613 Date: 2021-01-15 Source: bioRxiv

    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 viruses contains a 20-25 amino acid sequence at its N-terminal of the fusion domain, which is instrumental in fusion, and is termed as fusion peptide. However, Severe Acute Respiratory Syndrome Coronavirus (SARS) coronaviruses MESHD contain more than one fusion peptide sequences. We have shown that the internal fusion peptide 1 ( IFP1 HGNC) of SARS-CoV MESHD is far more efficient than its N-terminal counterpart (FP) to induce hemifusion between small unilamellar vesicles. Moreover, the ability of IFP1 HGNC to induce hemifusion formation increases dramatically with growing cholesterol content in the membrane. Interestingly, IFP1 HGNC is capable of inducing hemifusion, but fails to open pore.

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MeSH Disease
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