Author

D. L. Hurdiss

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Microbiology· 7 Immunology· 3 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 10 Organism:human· 6 Research Focus:drug response / drug discovery· 5 Research Focus:host-pathogen & immune response· 5 Assay:cryo-EM· 3 Organism:mouse· 3 Research Focus:protein structure prediction· 2 Assay:proteomics· 2

Frequent Co-Authors

F. J. M. van Kuppeveld· 7 shared I. Drulyte· 7 shared W. Li· 5 shared C. Wang· 4 shared W. Du· 4 shared B. J. Bosch· 3 shared J. Snijder· 3 shared R. J. de Groot· 3 shared

Activity by Year

2019-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 34 mutual co-author links

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Curved chords = mutual co-authorship

7 shared papersMicrobiology

F. J. M. van Kuppeveld

Mutual co-authors in cluster

Author profile →

11 papers

Recent·Most cited

SARS-CoV-2 nucleocapsid protein inhibits the PKR-mediated integrated stress response through RNA-binding domain N2b

C. Aloise, J. G. Schipper, A. van Vliet, J. Oymans, T. Donselaar, D. L. Hurdiss, R. J. de Groot, F. J. M. van Kuppeveld

This study identifies the SARS-CoV-2 nucleocapsid protein's N2b domain as inhibiting PKR-mediated integrated stress response and innate immunity by sequestering dsRNA.

PLOS Pathogens · Aug 22, 2023Peer-reviewedMicrobiology

Sialoglycan binding triggers spike opening in a human coronavirus

M. F. Pronker, R. Creutznacher, I. Drulyte, R. J. G. Hulswit, Z. Li, F. J. M. van Kuppeveld, J. Snijder, Y. Lang, B.-J. Bosch, G.-J. Boons, M. Frank, R. J. de Groot, D. L. Hurdiss

This study shows that sialoglycan binding triggers the opening of the spike protein in the human coronavirus HKU1 through allosteric inter-domain cross-talk.

bioRxiv · Apr 20, 2023Microbiology

The virus-encoded ion channel "viroporin" activity of the agnoprotein is required for BK Polyomavirus release from infected kidney cells

G. Swinscoe, E. L. Prescott, D. L. Hurdiss, E. L. Morgan, S. J. Dobson, T. A. Edwards, R. Foster, M. Welberry-Smith, A. A. Macdonald

This study identifies agnoprotein as a viroporin required for BK polyomavirus release from infected cells and identifies small molecules that inhibit its activity.

bioRxiv · Jan 30, 2023 · PreprintMicrobiology

A broad-spectrum macrocyclic peptide inhibitor of the SARS-CoV-2 spike protein

V. Thijssen, D. L. Hurdiss, O. J. Debski-Antoniak, M. A. Spence, C. Franck, A. Norman, A. Aggarwal, N. J. Mokiem, D. A. A. van Dongen, S. W. Vermeir, M. Liu, W. Li, M. Chatziandreou, T. Donselaar, W. Du, , S. A. K. Jongkees

This paper discovers a macrocyclic peptide that inhibits SARS-CoV-2 and related sarbecoviruses by targeting a conserved site in the spike protein, offering a potential broad-spectrum antiviral.

bioRxiv · Nov 11, 2022 · PreprintBiochemistry

An ACE2-blocking antibody confers broad neutralization and protection against Omicron and other SARS-CoV-2 variants

W. Du, D. L. Hurdiss, D. Drabek, A. Z. Mykytyn, F. Kaiser, M. Gonzalez-Hernandez, D. Munoz-Santos, M. M. Lamers, R. van Haperen, W. Li, I. Drulyte, C. Wang, I. Sola, F. Armando, G. Beythien, , B. J. Bosch

bioRxiv · Feb 17, 2022 · PreprintMicrobiology

Fluoxetine targets an allosteric site in the enterovirus 2C AAA+ ATPase and stabilizes the hexameric complex

D. L. Hurdiss, P. El Kazzi, L. Bauer, N. Papageorgiou, F. P. Ferron, T. Donselaar, A. L. W. van Vliet, B. Canard, E. Decroly, A. Brancale, T. Zeev-Ben-Mordehai, F. Förster, F. J. M. van Kuppeveld, B. Coutard

This study identifies fluoxetine as an inhibitor of the enterovirus 2C AAA+ ATPase, revealing its mechanism of action through structural and functional analyses.

bioRxiv · Apr 26, 2021Microbiology

Ensovibep, a novel trispecific DARPin candidate that protects against SARS-CoV-2 variants

S. Rothenberger, D. L. Hurdiss, M. Walser, F. Malvezzi, J. Mayor, S. Ryter, H. Moreno, N. Liechti, A. Bosshart, C. Iss, V. Calabro, A. Cornelius, T. Hospodarsch, A. Neculcea, T. Looser, , Vassell

This paper describes ensovibep, a trispecific DARPin that inhibits SARS-CoV-2 variants by targeting the spike protein, showing potent antiviral activity and protection in animal models.

bioRxiv · Feb 3, 2021 · PreprintImmunology

A human monoclonal antibody targeting a conserved pocket in the SARS-CoV-2 receptor-binding domain core

J. Fedry, D. L. Hurdiss, C. Wang, W. Li, G. Obal, I. Drulyte, S. C. Howes, F. J. M. van Kuppeveld, F. Förster, B. J. Bosch

This paper identifies a human monoclonal antibody, 47D11, that targets a conserved hydrophobic pocket in the SARS-CoV-2 RBD, revealing its structural basis for neutralization and potential therapeutic use.

bioRxiv · Sep 30, 2020Immunology

Cryo-EM structure of coronavirus-HKU1 haemagglutinin esterase reveals architectural changes arising from prolonged circulation in humans

D. L. Hurdiss, I. Drulyte, Y. Lang, T. M. Shamorkina, M. F. Pronker, F. J. M. van Kuppeveld, J. Snijder, R. J. de Groot

The paper presents the cryo-EM structure of HKU1 HE, revealing structural changes due to prolonged human circulation, including a truncated lectin domain and intact esterase domain.

Nature Communications · Sep 16, 2020Peer-reviewedMicrobiology

Highly potent anti-SARS-CoV-2 multivalent DARPin therapeutic candidates

M. Walser, S. Rothenberger, D. L. Hurdiss, A. Schlegel, V. Calabro, S. Fontaine, D. Villemagne, M. Paladino, T. Hospodarsch, A. Neculcea, A. Cornelius, P. Schildknecht, M. Matzner, M. Haenggi, M. Franchini, , Stittela

This paper develops potent anti-SARS-CoV-2 DARPin therapeutics with low picomolar neutralization efficacy and reports their protective efficacy in a hamster model.

bioRxiv · Aug 25, 2020 · PreprintImmunology

High-Resolution Cryo-EM Reveals Dynamics in the Murine Norovirus Capsid

J. S. Snowden, D. L. Hurdiss, O. O. Adeyemi, N. A. Ranson, M. R. Herod, N. J. Stonehouse

This study uses cryo-EM to reveal the dynamic conformational changes in murine norovirus capsids, showing flexibility in protruding domains that impact virion stability and infectivity.

bioRxiv · Jul 4, 2019 · PreprintMicrobiology