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  1. Artikel ; Online: Boceprevir, Calpain Inhibitors II and XII, and GC-376 Have Broad-Spectrum Antiviral Activity against Coronaviruses.

    Hu, Yanmei / Ma, Chunlong / Szeto, Tommy / Hurst, Brett / Tarbet, Bart / Wang, Jun

    ACS infectious diseases

    2021  Band 7, Heft 3, Seite(n) 586–597

    Abstract: As the COVID-19 pandemic continues to unfold, the morbidity and mortality are increasing daily. Effective treatment for SARS-CoV-2 is urgently needed. We recently discovered four SARS-CoV-2 main protease ( ... ...

    Abstract As the COVID-19 pandemic continues to unfold, the morbidity and mortality are increasing daily. Effective treatment for SARS-CoV-2 is urgently needed. We recently discovered four SARS-CoV-2 main protease (M
    Mesh-Begriff(e) Adenosine Monophosphate/analogs & derivatives ; Adenosine Monophosphate/pharmacology ; Alanine/analogs & derivatives ; Alanine/pharmacology ; Animals ; Antiviral Agents/pharmacology ; Caco-2 Cells ; Carbonates/pharmacology ; Cathepsin L/antagonists & inhibitors ; Cell Line ; Chlorocebus aethiops ; Coronavirus 229E, Human/drug effects ; Coronavirus 3C Proteases/antagonists & inhibitors ; Coronavirus NL63, Human/drug effects ; Coronavirus OC43, Human/drug effects ; Drug Combinations ; Glycoproteins/pharmacology ; HEK293 Cells ; Humans ; Leucine/pharmacology ; Middle East Respiratory Syndrome Coronavirus/drug effects ; Oligopeptides/pharmacology ; Proline/analogs & derivatives ; Proline/pharmacology ; SARS-CoV-2/drug effects ; Serine Endopeptidases/metabolism ; Sulfonic Acids/pharmacology ; Vero Cells ; COVID-19 Drug Treatment
    Chemische Substanzen Antiviral Agents ; Carbonates ; Drug Combinations ; Glycoproteins ; Oligopeptides ; Sulfonic Acids ; calpain inhibitors ; calpain inhibitor 2 (110115-07-6) ; remdesivir (3QKI37EEHE) ; Adenosine Monophosphate (415SHH325A) ; N-(3-amino-1-(cyclobutylmethyl)-2,3-dioxopropyl)-3-(2-((((1,1-dimethylethyl)amino)carbonyl)amino)-3,3-dimethyl-1-oxobutyl)-6,6-dimethyl-3-azabicyclo(3.1.0)hexan-2-carboxamide (89BT58KELH) ; Proline (9DLQ4CIU6V) ; Serine Endopeptidases (EC 3.4.21.-) ; transmembrane serine protease 2, human (EC 3.4.21.-) ; Cathepsin L (EC 3.4.22.15) ; Coronavirus 3C Proteases (EC 3.4.22.28) ; Leucine (GMW67QNF9C) ; GC376 (H1NMJ5XDG5) ; Alanine (OF5P57N2ZX)
    Sprache Englisch
    Erscheinungsdatum 2021-03-01
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ISSN 2373-8227
    ISSN (online) 2373-8227
    DOI 10.1021/acsinfecdis.0c00761
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel: Boceprevir, calpain inhibitors II and XII, and GC-376 have broad-spectrum antiviral activity against coronaviruses in cell culture.

    Hu, Yanmei / Ma, Chunlong / Szeto, Tommy / Hurst, Brett / Tarbet, Bart / Wang, Jun

    bioRxiv : the preprint server for biology

    2020  

    Abstract: As the COVID-19 pandemic continues to fold out, the morbidity and mortality are increasing daily. Effective treatment for SARS-CoV-2 is urgently needed. We recently discovered four SARS-CoV-2 main protease (Mpro) inhibitors including boceprevir, calpain ... ...

    Abstract As the COVID-19 pandemic continues to fold out, the morbidity and mortality are increasing daily. Effective treatment for SARS-CoV-2 is urgently needed. We recently discovered four SARS-CoV-2 main protease (Mpro) inhibitors including boceprevir, calpain inhibitors II and XII and GC-376 with potent antiviral activity against infectious SARS-CoV-2 in cell culture. Despite the weaker enzymatic inhibition of calpain inhibitors II and XII against Mpro compared to GC-376, calpain inhibitors II and XII had more potent cellular antiviral activity. This observation promoted us to hypothesize that the cellular antiviral activity of calpain inhibitors II and XII might also involve the inhibition of cathepsin L in addition to Mpro. To test this hypothesis, we tested calpain inhibitors II and XII in the SARS-CoV-2 pseudovirus neutralization assay in Vero E6 cells and found that both compounds significantly decreased pseudoviral particle entry into cells, indicating their role in inhibiting cathepsin L. The involvement of cathepsin L was further confirmed in the drug time-of-addition experiment. In addition, we found that these four compounds not only inhibit SARS-CoV-2, but also SARS-CoV, MERS-CoV, as well as human coronaviruses (CoVs) 229E, OC43, and NL63. The mechanism of action is through targeting the viral Mpro, which was supported by the thermal shift binding assay and enzymatic FRET assay. We further showed that these four compounds have additive antiviral effect when combined with remdesivir. Altogether, these results suggest that boceprevir, calpain inhibitors II and XII, and GC-376 are not only promising antiviral drug candidates against existing human coronaviruses, but also might work against future emerging CoVs.
    Schlagwörter covid19
    Sprache Englisch
    Erscheinungsdatum 2020-11-01
    Erscheinungsland United States
    Dokumenttyp Preprint
    DOI 10.1101/2020.10.30.362335
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  3. Artikel ; Online: Boceprevir, GC-376, and calpain inhibitors II, XII inhibit SARS-CoV-2 viral replication by targeting the viral main protease

    Ma, Chunlong / Hurst, Brett / Hu, Yanmei / Szeto, Tommy / Tarbet, Bart / Wang, Jun

    bioRxiv

    Abstract: A novel coronavirus SARS-CoV-2, also called novel coronavirus 2019 (nCoV-19), started to circulate among humans around December 2019, and it is now widespread as a global pandemic. The disease caused by SARS-CoV-2 virus is called COVID-19, which is ... ...

    Abstract A novel coronavirus SARS-CoV-2, also called novel coronavirus 2019 (nCoV-19), started to circulate among humans around December 2019, and it is now widespread as a global pandemic. The disease caused by SARS-CoV-2 virus is called COVID-19, which is highly contagious and has an overall mortality rate of 6.4% as of April 15, 2020. There is no vaccine or antiviral available for SARS-CoV-2. In this study, we report our discovery of inhibitors targeting the SARS-CoV-2 main protease (Mpro). Using the FRET-based enzymatic assay, several inhibitors including boceprevir, GC-376, calpain inhibitors II, XII, and MG-132 were identified to have potent activity with single-digit to submicromolar IC50 values in the enzymatic assay. The mechanism of action of the hits was further characterized using enzyme kinetic studies and thermal shift binding assays. Significantly, four compounds (boceprevir, GC-376, calpain inhibitors II and XII) inhibit SARS-CoV-2 viral replication in cell culture with EC50 values ranging from 0.49 to 3.37 micromolar. Notably, boceprevir, calpain inhibitors II and XII represent novel chemotypes that are distinct from known Mpro inhibitors. Overall, the compounds identified herein provide promising starting points for the further development of SARS-CoV-2 therapeutics.
    Schlagwörter covid19
    Sprache Englisch
    Erscheinungsdatum 2020-04-20
    Verlag Cold Spring Harbor Laboratory
    Dokumenttyp Artikel ; Online
    DOI 10.1101/2020.04.20.051581
    Datenquelle COVID19

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  4. Artikel ; Online: Rational design of a new class of protease inhibitors for the potential treatment of coronavirus diseases

    Westberg, Michael / Su, Yichi / Zou, Xinzhi / Ning, Lin / Hurst, Brett / Tarbet, Bart / Lin, Michael

    bioRxiv

    Abstract: The main protease, Mpro, of SARSCoV2 is a key protein in the coronavirus life cycle and a major drug target. Based on crystal structures of SARSCoV2 Mpro complexed with peptidomimetic inhibitors, we recognized a structural motif shared with approved ... ...

    Abstract The main protease, Mpro, of SARSCoV2 is a key protein in the coronavirus life cycle and a major drug target. Based on crystal structures of SARSCoV2 Mpro complexed with peptidomimetic inhibitors, we recognized a structural motif shared with approved inhibitors of hepatitis C virus protease. Initial tests showed that several HCV protease inhibitors could indeed also inhibit Mpro. Based on the identified molecular scaffolds we designed a new generation of ketoamide-based Mpro inhibitors with a preorganized backbone conformation. One of the designed inhibitors, ML1000, shows particularly high affinity towards Mpro and inhibits SARSCoV2 viral replication in human cells at sub-micromolar concentrations. Our findings identify ML1000 as a promising new scaffold for the development of anti-coronavirus drugs.
    Schlagwörter covid19
    Sprache Englisch
    Erscheinungsdatum 2020-09-16
    Verlag Cold Spring Harbor Laboratory
    Dokumenttyp Artikel ; Online
    DOI 10.1101/2020.09.15.275891
    Datenquelle COVID19

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  5. Artikel ; Online: Boceprevir, calpain inhibitors II and XII, and GC-376 have broad-spectrum antiviral activity against coronaviruses in cell culture

    Hu, Yanmei / Ma, Chunlong / Szeto, Tommy / Hurst, Brett / Tarbet, Bart / Wang, Jun

    bioRxiv

    Abstract: As the COVID-19 pandemic continues to fold out, the morbidity and mortality are increasing daily. Effective treatment for SARS-CoV-2 is urgently needed. We recently discovered four SARS-CoV-2 main protease (Mpro) inhibitors including boceprevir, calpain ... ...

    Abstract As the COVID-19 pandemic continues to fold out, the morbidity and mortality are increasing daily. Effective treatment for SARS-CoV-2 is urgently needed. We recently discovered four SARS-CoV-2 main protease (Mpro) inhibitors including boceprevir, calpain inhibitors II and XII and GC-376 with potent antiviral activity against infectious SARS-CoV-2 in cell culture. Despite the weaker enzymatic inhibition of calpain inhibitors II and XII against Mpro compared to GC-376, calpain inhibitors II and XII had more potent cellular antiviral activity. This observation promoted us to hypothesize that the cellular antiviral activity of calpain inhibitors II and XII might also involve the inhibition of cathepsin L in addition to Mpro. To test this hypothesis, we tested calpain inhibitors II and XII in the SARS-CoV-2 pseudovirus neutralization assay in Vero E6 cells and found that both compounds significantly decreased pseudoviral particle entry into cells, indicating their role in inhibiting cathepsin L. The involvement of cathepsin L was further confirmed in the drug time-of-addition experiment. In addition, we found that these four compounds not only inhibit SARS-CoV-2, but also SARS-CoV, MERS-CoV, as well as human coronaviruses (CoVs) 229E, OC43, and NL63. The mechanism of action is through targeting the viral Mpro, which was supported by the thermal shift binding assay and enzymatic FRET assay. We further showed that these four compounds have additive antiviral effect when combined with remdesivir. Altogether, these results suggest that boceprevir, calpain inhibitors II and XII, and GC-376 are not only promising antiviral drug candidates against existing human coronaviruses, but also might work against future emerging CoVs.
    Schlagwörter covid19
    Sprache Englisch
    Erscheinungsdatum 2020-11-01
    Verlag Cold Spring Harbor Laboratory
    Dokumenttyp Artikel ; Online
    DOI 10.1101/2020.10.30.362335
    Datenquelle COVID19

    Volltext online

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  6. Artikel ; Online: Efficacy of an isoxazole-3-carboxamide analog of pleconaril in mouse models of Enterovirus-D68 and Coxsackie B5.

    Lane, Thomas R / Fu, Jianing / Sherry, Barbara / Tarbet, Bart / Hurst, Brett L / Riabova, Olga / Kazakova, Elena / Egorova, Anna / Clarke, Penny / Leser, J Smith / Frost, Joshua / Rudy, Michael / Tyler, Kenneth L / Klose, Thomas / Volobueva, Alexandrina S / Belyaevskaya, Svetlana V / Zarubaev, Vladimir V / Kuhn, Richard J / Makarov, Vadim /
    Ekins, Sean

    Antiviral research

    2023  Band 216, Seite(n) 105654

    Abstract: Enteroviruses (EV) cause a number of life-threatening infectious diseases. EV-D68 is known to cause respiratory illness in children that can lead to acute flaccid myelitis. Coxsackievirus B5 (CVB5) is commonly associated with hand-foot-mouth disease. ... ...

    Abstract Enteroviruses (EV) cause a number of life-threatening infectious diseases. EV-D68 is known to cause respiratory illness in children that can lead to acute flaccid myelitis. Coxsackievirus B5 (CVB5) is commonly associated with hand-foot-mouth disease. There is no antiviral treatment available for either. We have developed an isoxazole-3-carboxamide analog of pleconaril (11526092) which displayed potent inhibition of EV-D68 (IC
    Mesh-Begriff(e) Animals ; Mice ; Enterovirus D, Human ; Isoxazoles/pharmacology ; Isoxazoles/therapeutic use ; Cryoelectron Microscopy ; Enterovirus Infections/drug therapy ; Enterovirus ; Antiviral Agents/pharmacology ; Antiviral Agents/therapeutic use ; Hand, Foot and Mouth Disease/drug therapy ; Enterovirus B, Human
    Chemische Substanzen pleconaril (9H4570Q89D) ; Isoxazoles ; Antiviral Agents
    Sprache Englisch
    Erscheinungsdatum 2023-06-14
    Erscheinungsland Netherlands
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 306628-9
    ISSN 1872-9096 ; 0166-3542
    ISSN (online) 1872-9096
    ISSN 0166-3542
    DOI 10.1016/j.antiviral.2023.105654
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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    Verfügbar in ZB MED Köln/Königswinter

    Zs.A 1627: Hefte anzeigen Standort:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  7. Artikel ; Online: Rational design of a new class of protease inhibitors for the potential treatment of coronavirus diseases

    Westberg, Michael / Su, Yichi / Zou, Xinzhi / Ning, Lin / Hurst, Brett / Tarbet, Bart / Lin, Michael Z.

    bioRxiv

    Abstract: The coronavirus main protease, Mpro, is a key protein in the virus life cycle and a major drug target. Based on crystal structures of SARSCoV2 Mpro complexed with peptidomimetic inhibitors, we recognized a binding characteristic shared with proline- ... ...

    Abstract The coronavirus main protease, Mpro, is a key protein in the virus life cycle and a major drug target. Based on crystal structures of SARSCoV2 Mpro complexed with peptidomimetic inhibitors, we recognized a binding characteristic shared with proline-containing inhibitors of hepatitis C virus protease. Initial tests showed that this subclass of HCV protease inhibitors indeed exhibited activity against Mpro. Postulating a benefit for a preorganized backbone conformation, we designed new ketoamide-based Mpro inhibitors based on central proline rings. One of the designed compounds, ML1000, inhibits Mpro with low-nanomolar affinity and suppresses SARSCoV2 viral replication in human cells at sub-micromolar concentrations. Our findings identify ML1000 as a promising new pre-organized scaffold for the development of anti-coronavirus drugs.
    Schlagwörter covid19
    Verlag BioRxiv; WHO
    Dokumenttyp Artikel ; Online
    DOI 10.1101/2020.09.15.275891
    Datenquelle COVID19

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  8. Artikel: Structure and inhibition of the SARS-CoV-2 main protease reveals strategy for developing dual inhibitors against M(pro) and cathepsin L

    Sacco, M. D. / Ma, C. / Lagarias, P. / Gao, A. / Townsend, J. A. / Meng, X. / Dube, P. / Zhang, X. / Hu, Y. / Kitamura, N. / Hurst, B. / Tarbet, B. / Marty, M. T. / Kolocouris, A. / Xiang, Y. / Chen, Y. / Wang, J.

    Sci Adv

    Abstract: The main protease (M(pro)) of SARS-CoV-2 is a key antiviral drug target While most M(pro) inhibitors have a γ-lactam glutamine surrogate at the P1 position, we recently discovered several M(pro) inhibitors have hydrophobic moieties at the P1 site, ... ...

    Abstract The main protease (M(pro)) of SARS-CoV-2 is a key antiviral drug target While most M(pro) inhibitors have a γ-lactam glutamine surrogate at the P1 position, we recently discovered several M(pro) inhibitors have hydrophobic moieties at the P1 site, including calpain inhibitors II and XII, which are also active against human cathepsin L, a host-protease that is important for viral entry In this study, we solved X-ray crystal structures of M(pro) in complex with calpain inhibitors II and XII, and three analogs of GC-376 The structure of M(pro) with calpain inhibitor II confirmed the S1 pocket can accommodate a hydrophobic methionine side chain, challenging the idea that a hydrophilic residue is necessary at this position Interestingly, the structure of calpain inhibitor XII revealed an unexpected, inverted binding pose Taken together, the biochemical, computational, structural, and cellular data presented herein provide new directions for the development of dual inhibitors as SARS-CoV-2 antivirals
    Schlagwörter covid19
    Verlag WHO
    Dokumenttyp Artikel
    Anmerkung WHO #Covidence: #913665
    Datenquelle COVID19

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  9. Artikel: Boceprevir, GC-376, and calpain inhibitors II, XII inhibit SARS-CoV-2 viral replication by targeting the viral main protease.

    Ma, Chunlong / Sacco, Michael D / Hurst, Brett / Townsend, Julia A / Hu, Yanmei / Szeto, Tommy / Zhang, Xiujun / Tarbet, Bart / Marty, Michael T / Chen, Yu / Wang, Jun

    bioRxiv : the preprint server for biology

    2020  

    Abstract: A novel coronavirus SARS-CoV-2, also called novel coronavirus 2019 (nCoV-19), started to circulate among humans around December 2019, and it is now widespread as a global pandemic. The disease caused by SARS-CoV-2 virus is called COVID-19, which is ... ...

    Abstract A novel coronavirus SARS-CoV-2, also called novel coronavirus 2019 (nCoV-19), started to circulate among humans around December 2019, and it is now widespread as a global pandemic. The disease caused by SARS-CoV-2 virus is called COVID-19, which is highly contagious and has an overall mortality rate of 6.96% as of May 4, 2020. There is no vaccine or antiviral available for SARS-CoV-2. In this study, we report our discovery of inhibitors targeting the SARS-CoV-2 main protease (M
    Schlagwörter covid19
    Sprache Englisch
    Erscheinungsdatum 2020-01-06
    Erscheinungsland United States
    Dokumenttyp Preprint
    DOI 10.1101/2020.04.20.051581
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  10. Artikel ; Online: Boceprevir, GC-376, and calpain inhibitors II, XII inhibit SARS-CoV-2 viral replication by targeting the viral main protease.

    Ma, Chunlong / Sacco, Michael Dominic / Hurst, Brett / Townsend, Julia Alma / Hu, Yanmei / Szeto, Tommy / Zhang, Xiujun / Tarbet, Bart / Marty, Michael Thomas / Chen, Yu / Wang, Jun

    Cell research

    2020  Band 30, Heft 8, Seite(n) 678–692

    Abstract: A new coronavirus SARS-CoV-2, also called novel coronavirus 2019 (2019-nCoV), started to circulate among humans around December 2019, and it is now widespread as a global pandemic. The disease caused by SARS-CoV-2 virus is called COVID-19, which is ... ...

    Abstract A new coronavirus SARS-CoV-2, also called novel coronavirus 2019 (2019-nCoV), started to circulate among humans around December 2019, and it is now widespread as a global pandemic. The disease caused by SARS-CoV-2 virus is called COVID-19, which is highly contagious and has an overall mortality rate of 6.35% as of May 26, 2020. There is no vaccine or antiviral available for SARS-CoV-2. In this study, we report our discovery of inhibitors targeting the SARS-CoV-2 main protease (M
    Mesh-Begriff(e) A549 Cells ; Animals ; Antiviral Agents/chemistry ; Antiviral Agents/pharmacology ; Betacoronavirus/enzymology ; COVID-19 ; Caco-2 Cells ; Chlorocebus aethiops ; Coronavirus 3C Proteases ; Coronavirus Infections/metabolism ; Coronavirus Infections/virology ; Cysteine Endopeptidases/chemistry ; Cysteine Endopeptidases/metabolism ; Drug Discovery/methods ; Glycoproteins/pharmacology ; Humans ; Inhibitory Concentration 50 ; Kinetics ; Pandemics ; Pneumonia, Viral/metabolism ; Pneumonia, Viral/virology ; Proline/analogs & derivatives ; Proline/pharmacology ; Protein Conformation ; Pyrrolidines/chemistry ; Pyrrolidines/pharmacology ; SARS-CoV-2 ; Sulfonic Acids ; Vero Cells ; Viral Nonstructural Proteins/antagonists & inhibitors ; Viral Nonstructural Proteins/chemistry ; Viral Nonstructural Proteins/metabolism ; Virus Replication/drug effects
    Chemische Substanzen Antiviral Agents ; Glycoproteins ; Pyrrolidines ; Sulfonic Acids ; Viral Nonstructural Proteins ; calpain inhibitors ; N-(3-amino-1-(cyclobutylmethyl)-2,3-dioxopropyl)-3-(2-((((1,1-dimethylethyl)amino)carbonyl)amino)-3,3-dimethyl-1-oxobutyl)-6,6-dimethyl-3-azabicyclo(3.1.0)hexan-2-carboxamide (89BT58KELH) ; Proline (9DLQ4CIU6V) ; Cysteine Endopeptidases (EC 3.4.22.-) ; Coronavirus 3C Proteases (EC 3.4.22.28) ; GC376 (H1NMJ5XDG5)
    Schlagwörter covid19
    Sprache Englisch
    Erscheinungsdatum 2020-06-15
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1319303-x
    ISSN 1748-7838 ; 1001-0602
    ISSN (online) 1748-7838
    ISSN 1001-0602
    DOI 10.1038/s41422-020-0356-z
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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