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  1. Article ; Online: Enhanced Cholesterol-Dependent Hemifusion by Internal Fusion Peptide 1 of SARS Coronavirus-2 Compared to Its N-Terminal Counterpart.

    Pattnaik, Gourab Prasad / Bhattacharjya, Surajit / Chakraborty, Hirak

    Biochemistry

    2021  Volume 60, Issue 8, Page(s) 559–562

    Abstract: ... IFP1) of SARS-CoV-2 is far more efficient than its N-terminal counterpart (FP) to induce hemifusion ... coronaviruses contain more than one fusion peptide sequences. We have shown that the internal fusion peptide 1 ... instrumental in fusion and is called as a "fusion peptide". However, severe acute respiratory syndrome (SARS ...

    Abstract 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.
    MeSH term(s) Amino Acid Sequence ; COVID-19/genetics ; COVID-19/metabolism ; Cholesterol/genetics ; Cholesterol/metabolism ; Humans ; Membrane Fusion/physiology ; Peptide Fragments/genetics ; Peptide Fragments/metabolism ; Phosphatidylcholines/genetics ; Phosphatidylcholines/metabolism ; SARS-CoV-2/genetics ; SARS-CoV-2/metabolism ; Virus Internalization
    Chemical Substances Peptide Fragments ; Phosphatidylcholines ; Cholesterol (97C5T2UQ7J) ; 1,2-oleoylphosphatidylcholine (EDS2L3ODLV)
    Language English
    Publishing date 2021-02-11
    Publishing country United States
    Document type Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021/acs.biochem.1c00046
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Enhanced Cholesterol-Dependent Hemifusion by Internal Fusion Peptide 1 of SARS Coronavirus-2 Compared to Its N-Terminal Counterpart

    Pattnaik, Gourab Prasad / Bhattacharjya, Surajit / Chakraborty, Hirak

    Biochemistry. 2021 Feb. 11, v. 60, no. 8

    2021  

    Abstract: ... IFP1) of SARS-CoV-2 is far more efficient than its N-terminal counterpart (FP) to induce hemifusion ... coronaviruses contain more than one fusion peptide sequences. We have shown that the internal fusion peptide 1 ... instrumental in fusion and is called as a “fusion peptide”. However, severe acute respiratory syndrome (SARS ...

    Abstract 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.
    Keywords Severe acute respiratory syndrome coronavirus 2 ; amino acid sequences ; cholesterol ; membrane fusion ; peptides ; viruses
    Language English
    Dates of publication 2021-0211
    Size p. 559-562.
    Publishing place American Chemical Society
    Document type Article
    Note NAL-AP-2-clean
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021/acs.biochem.1c00046
    Database NAL-Catalogue (AGRICOLA)

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  3. Article ; Online: Enhanced Cholesterol-dependent Hemifusion by Internal Fusion Peptide 1 of SARS Coronavirus-2 Compared to its N-terminal Counterpart

    Pattnaik, Gourab Prasad / Bhattacharjya, Surajit / Chakraborty, Hirak

    bioRxiv

    Abstract: ... fusion peptide 1 (IFP1) of SARS-CoV is far more efficient than its N-terminal counterpart (FP) to induce ... Coronavirus (SARS) coronaviruses contain more than one fusion peptide sequences. We have shown that the internal ... The class I viruses contains a 20-25 amino acid sequence at its N-terminal of the fusion domain, which is ...

    Abstract 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 contain more than one fusion peptide sequences. We have shown that the internal fusion peptide 1 (IFP1) of SARS-CoV 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 pore.
    Keywords covid19
    Language English
    Publishing date 2021-01-15
    Publisher Cold Spring Harbor Laboratory
    Document type Article ; Online
    DOI 10.1101/2021.01.14.426613
    Database COVID19

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