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  1. Article ; Online: The SARS-CoV heptad repeat 2 exhibits pH-induced helix formation.

    Celigoy, Jessica / McReynolds, Susanna / Caffrey, Michael

    Biochemical and biophysical research communications

    2011  Volume 412, Issue 3, Page(s) 483–486

    Abstract: The heptad repeats 1 and 2 of SARS-CoV spike, termed HR1 and HR2, play critical roles in viral entry. Moreover, HR1 and HR2 derived free peptides are inhibitors of SARS-CoV entry. In this work we used circular dichroism to show that HR2 helix formation ... ...

    Abstract The heptad repeats 1 and 2 of SARS-CoV spike, termed HR1 and HR2, play critical roles in viral entry. Moreover, HR1 and HR2 derived free peptides are inhibitors of SARS-CoV entry. In this work we used circular dichroism to show that HR2 helix formation is induced at pH 5, the pH of the endosome. In addition, we demonstrate that the HR2 helix is further stabilized at physiological ionic strengths. Together, these observations provide new insight into the mechanism of SARS-CoV entry and suggest that HR2 may be an attractive target for therapeutic intervention.
    MeSH term(s) Circular Dichroism ; Hydrogen-Ion Concentration ; Protein Structure, Secondary ; Repetitive Sequences, Amino Acid ; SARS Virus/chemistry ; Static Electricity ; Virus Internalization
    Keywords covid19
    Language English
    Publishing date 2011-08-03
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 205723-2
    ISSN 1090-2104 ; 0006-291X ; 0006-291X
    ISSN (online) 1090-2104 ; 0006-291X
    ISSN 0006-291X
    DOI 10.1016/j.bbrc.2011.07.126
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: SARS-CoV heptad repeat 2 is a trimer of parallel helices.

    Celigoy, Jessica / Ramirez, Benjamin / Caffrey, Michael

    Protein science : a publication of the Protein Society

    2011  Volume 20, Issue 12, Page(s) 2125–2129

    Abstract: In severe acute respiratory syndrome coronavirus, the envelope heptad repeat 2 (HR2) plays a critical role in viral entry. Moreover, HR2 is both the target for novel antiviral therapies and, as an isolated peptide, presents a potential antiviral ... ...

    Abstract In severe acute respiratory syndrome coronavirus, the envelope heptad repeat 2 (HR2) plays a critical role in viral entry. Moreover, HR2 is both the target for novel antiviral therapies and, as an isolated peptide, presents a potential antiviral therapeutic. The structure of HR2, as determined by NMR spectroscopy in the presence of the co-solvent trifluoroethanol (TFE), is a trimer of parallel helices, whereas the structure of HR2, as determined by X-ray crystallography, is a tetramer of anti-parallel helices. In this work, we added a nitroxide spin label to the N-terminal region of HR2 and used paramagnetic relaxation enhancement to assess the orientation of the HR2 helices under different solution conditions. We find that the relaxation effects are consistent with an orientation corresponding to a trimer of parallel helices in both the presence and absence of TFE. This work suggests that the different orientation and oligomerization states observed by NMR and X-ray are due to the 11 additional residues present at the N-terminus of the NMR construct.
    MeSH term(s) Models, Molecular ; Nuclear Magnetic Resonance, Biomolecular ; Protein Multimerization ; Protein Structure, Secondary ; SARS Virus/chemistry ; Severe Acute Respiratory Syndrome/virology ; Spin Labels ; Viral Envelope Proteins/chemistry
    Chemical Substances Spin Labels ; Viral Envelope Proteins
    Keywords covid19
    Language English
    Publishing date 2011-11-01
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1106283-6
    ISSN 1469-896X ; 0961-8368
    ISSN (online) 1469-896X
    ISSN 0961-8368
    DOI 10.1002/pro.736
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  3. Article: The SARS-CoV heptad repeat 2 exhibits pH-induced helix formation

    Celigoy, Jessica / McReynolds, Susanna / Caffrey, Michael

    Biochemical and biophysical research communications. 2011 Sept. 2, v. 412, no. 3

    2011  

    Abstract: The heptad repeats 1 and 2 of SARS-CoV spike, termed HR1 and HR2, play critical roles in viral entry. Moreover, HR1 and HR2 derived free peptides are inhibitors of SARS-CoV entry. In this work we used circular dichroism to show that HR2 helix formation ... ...

    Abstract The heptad repeats 1 and 2 of SARS-CoV spike, termed HR1 and HR2, play critical roles in viral entry. Moreover, HR1 and HR2 derived free peptides are inhibitors of SARS-CoV entry. In this work we used circular dichroism to show that HR2 helix formation is induced at pH 5, the pH of the endosome. In addition, we demonstrate that the HR2 helix is further stabilized at physiological ionic strengths. Together, these observations provide new insight into the mechanism of SARS-CoV entry and suggest that HR2 may be an attractive target for therapeutic intervention.
    Keywords Severe acute respiratory syndrome coronavirus ; ionic strength ; pH ; peptides ; covid19
    Language English
    Dates of publication 2011-0902
    Size p. 483-486.
    Publishing place Elsevier Inc.
    Document type Article
    ZDB-ID 205723-2
    ISSN 0006-291X ; 0006-291X
    ISSN (online) 0006-291X
    ISSN 0006-291X
    DOI 10.1016/j.bbrc.2011.07.126
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  4. Article ; Online: Probing the HIV gp120 envelope glycoprotein conformation by NMR.

    Celigoy, Jessica / Ramirez, Benjamin / Tao, Lin / Rong, Lijun / Yan, Lianying / Feng, Yan-Ru / Quinnan, Gerald V / Broder, Christopher C / Caffrey, Michael

    The Journal of biological chemistry

    2011  Volume 286, Issue 27, Page(s) 23975–23981

    Abstract: The HIV envelope glycoprotein gp120 plays a critical role in virus entry, and thus, its structure is of extreme interest for the development of novel therapeutics and vaccines. To date, high resolution structural information about gp120 in complex with ... ...

    Abstract The HIV envelope glycoprotein gp120 plays a critical role in virus entry, and thus, its structure is of extreme interest for the development of novel therapeutics and vaccines. To date, high resolution structural information about gp120 in complex with gp41 has proven intractable. In this study, we characterize the structural properties of gp120 in the presence and absence of gp41 domains by NMR. Using the peptide probe 12p1 (sequence, RINNIPWSEAMM), which was identified previously as an entry inhibitor that binds to gp120, we identify atoms of 12p1 in close contact with gp120 in the monomeric and trimeric states. Interestingly, the binding mode of 12p1 with gp120 is similar for clades B and C. In addition, we show a subtle difference in the binding mode of 12p1 in the presence of gp41 domains, i.e. the trimeric state, which we interpret as small differences in the gp120 structure in the presence of gp41.
    MeSH term(s) HIV Envelope Protein gp120/chemistry ; HIV Envelope Protein gp120/metabolism ; HIV Envelope Protein gp41/chemistry ; HIV Envelope Protein gp41/metabolism ; HIV-1/chemistry ; HIV-1/physiology ; Molecular Probes/chemistry ; Nuclear Magnetic Resonance, Biomolecular/methods ; Peptides/chemistry ; Peptides/metabolism ; Protein Binding ; Protein Structure, Quaternary
    Chemical Substances HIV Envelope Protein gp120 ; HIV Envelope Protein gp41 ; Molecular Probes ; Peptides ; gp120 protein, Human immunodeficiency virus 1 ; gp41 protein, Human immunodeficiency virus 1
    Keywords covid19
    Language English
    Publishing date 2011-05-18
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M111.251025
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  5. Article ; Online: Characterization of the prefusion and transition states of severe acute respiratory syndrome coronavirus S2-HR2.

    McReynolds, Susanna / Jiang, Shaokai / Guo, Ying / Celigoy, Jessica / Schar, Christine / Rong, Lijun / Caffrey, Michael

    Biochemistry

    2008  Volume 47, Issue 26, Page(s) 6802–6808

    Abstract: The envelope glycoproteins of the class I family, which include human immunodeficiency virus (HIV), influenza, and severe acute respiratory syndrome coronavirus (SARS-CoV), mediate viral entry by first binding to their cellular receptors and subsequently ...

    Abstract The envelope glycoproteins of the class I family, which include human immunodeficiency virus (HIV), influenza, and severe acute respiratory syndrome coronavirus (SARS-CoV), mediate viral entry by first binding to their cellular receptors and subsequently inducing fusion of the viral and cellular membranes. In the case of SARS-CoV, heptad repeat domains of the envelope glycoprotein, termed S2-HR1 and S2-HR2, are thought to undergo structural changes from a prefusion state, in which S2-HR1 and S2-HR2 do not interact, to a postfusion state in which S2-HR1 and S2-HR2 associate to form a six-helix bundle. In the present work, the structural and dynamic properties of S2-HR2 have been characterized. Evidence is presented for an equilibrium between a structured trimer thought to represent a prefusion state and an ensemble of unstructured monomers thought to represent a novel transition state. A model for viral entry is presented in which S2-HR2 is in a dynamic equilibrium between an ensemble of unstructured monomers in the transition state and a structured trimer in the prefusion state. Conversion from the prefusion state to the postfusion state requires passage through the transition state, a state that may give insight into the design of structure-based antagonists of SARS-CoV in particular, as well as other enveloped viruses in general.
    MeSH term(s) Amino Acid Sequence ; Circular Dichroism ; Glycoproteins/chemistry ; Glycoproteins/genetics ; Glycoproteins/metabolism ; Models, Molecular ; Molecular Sequence Data ; Nuclear Magnetic Resonance, Biomolecular ; Protein Binding ; Protein Structure, Quaternary ; SARS Virus/chemistry ; SARS Virus/genetics ; SARS Virus/metabolism ; Viral Proteins/chemistry ; Viral Proteins/genetics ; Viral Proteins/metabolism ; Virus Internalization
    Chemical Substances Glycoproteins ; Viral Proteins
    Keywords covid19
    Language English
    Publishing date 2008-07-01
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021/bi800622t
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 217: Show issues Location:
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