Author

D. J. Sheward

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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Immunology· 11 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 11 Research Focus:host-pathogen & immune response· 9 Organism:human· 7 Assay:proteomics· 6 Research Focus:cell type annotation· 3 Approach:deep learning· 2 Research Focus:drug response / drug discovery· 2 Organism:mouse· 2

Frequent Co-Authors

B. Murrell· 11 shared C. Kim· 7 shared G. B. Karlsson Hedestam· 6 shared J. Albert· 6 shared L. Hanke· 5 shared G. M. McInerney· 4 shared R. A. Ehling· 4 shared S. Muschiol· 4 shared

Activity by Year

2020-2024 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 38 mutual co-author links

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11 shared papersImmunology

B. Murrell

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Author profile →

12 papers

Recent·Most cited

Neutralisation sensitivity of the SARS-CoV-2 BA.2.87.1 variant

D. J. Sheward, U. Marking, O. Bladh, S. Held, E. Looyens, L. Vandenabeele, S. Muschiol, K. Aguilera, N. G. Norin, S. Oling, M. Westerberg, D. Martin, G. B. K. Hedestam, J. Albert, C. Thalin, B. Murrell

This study characterizes the neutralization sensitivity of the SARS-CoV-2 BA.2.87.1 variant and shows it is less resistant to antibodies than other variants, with a booster increasing neutralizing titers.

bioRxiv · Mar 21, 2024 · PreprintImmunology

Humoral immune responses to the monovalent XBB.1.5-adapted BNT162b2 mRNA booster

U. Marking, O. Bladh, K. Aguilera, Y. Yang, N. Greilert-Norin, K. Blom, S. Hober, J. Klingstrom, S. Havervall, M. Aberg, D. J. Sheward, C. Thalin

This study shows that a monovalent XBB.1.5-adapted BNT162b2 booster vaccine enhances binding and neutralizing antibodies against XBB.1.5 and BA.2.86 in elderly individuals with prior vaccinations.

bioRxiv · Dec 21, 2023 · PreprintImmunology

Sensitivity of BA.2.86 to prevailing neutralising antibody responses

D. J. Sheward, Y. Yang, M. Westerberg, S. Öling, S. Muschiol, K. Sato, T. P. Peacock, G. B. Karlsson Hedestam, J. Albert, B. Murrell

This study assesses BA.2.86's sensitivity to neutralising antibodies using monoclonal antibodies and serum samples from Stockholm.

bioRxiv · Sep 2, 2023 · PreprintImmunology

Omicron sublineage BA.2.75.2 exhibits extensive escape from neutralising antibodies

D. J. Sheward, C. Kim, J. Fischbach, S. Muschiol, R. A. Ehling, N. K. Björkström, G. B. Karlsson Hedestam, S. T. Reddy, J. Albert, T. P. Peacock, B. Murrell

The paper evaluates neutralisation resistance of Omicron sublineages BA.2.75.2, BA.4.6, and BA.2.10.4, finding BA.2.75.2 shows extensive escape from neutralising antibodies.

bioRxiv · Sep 16, 2022Immunology

Evasion of neutralizing antibodies by Omicron sublineage BA.2.75

D. J. Sheward, C. Kim, J. Fischbach, S. Muschiol, R. A. Ehling, N. K. Björkström, G. B. Karlsson Hedestam, S. T. Reddy, J. Albert, T. P. Peacock, B. Murrell

This study evaluates the neutralization sensitivity of the SARS-CoV-2 BA.2.75 sublineage to monoclonal antibodies and sera from individuals infected with earlier variants.

bioRxiv · Jul 19, 2022 · PreprintImmunology

Structural basis of Omicron neutralization by affinity-matured public antibodies

D. J. Sheward, P. Pushparaj, H. Das, C. Kim, S. Kim, L. Hanke, R. Dyrdak, G. M. McInerney, J. Albert, B. Murrell, G. B. Karlsson Hedestam, B. M. Hällberg

The paper identifies affinity-matured antibodies that neutralize SARS-CoV-2 Omicron with high potency and resolves their structure to explain cross-neutralization.

bioRxiv · Jan 3, 2022 · PreprintImmunology

Variable loss of antibody potency against SARS-CoV-2 B.1.1.529 (Omicron)

D. J. Sheward, C. Kim, R. A. Ehling, A. Pankow, X. Castro Dopico, D. P. Martin, S. T. Reddy, J. Dillner, G. B. Karlsson Hedestam, J. Albert, B. Murrell

This study assesses neutralizing antibody responses against the SARS-CoV-2 Omicron variant, showing reduced potency compared to the pandemic founder but with some cross-neutralizing capacity in vaccinated individuals.

bioRxiv · Dec 19, 2021 · PreprintImmunology

Multivariate mining of an alpaca immune repertoire identifies potent cross-neutralising SARS-CoV-2 nanobodies

L. Hanke, D. J. Sheward, A. Pankow, L. Perez Vidakovics, V. Karl, C. Kim, E. Urgard, N. L. Smith, J. Astorga-Wells, S. Ekström, J. M. Coquet, G. M. McInerney, B. Murrell

This study identifies potent cross-neutralizing SARS-CoV-2 nanobodies from an alpaca immune repertoire using phage display and epitope mapping.

bioRxiv · Jul 25, 2021Immunology

Driving potent neutralization of a SARS-CoV-2 Variant of Concern with a heterotypic boost

D. J. Sheward, M. Mandolesi, E. Urgard, C. Kim, L. Hanke, L. Perez Vidakovics, A. Pankow, N. L. Smith, X. Castro Dopico, G. M. McInerney, J. M. Coquet, G. Karlsson Hedestam, B. Murrell

A single dose of a VOC-derived RBD protein boost enhances potent neutralizing antibodies against both Wu-Hu-1 and the VOC in previously vaccinated rhesus macaques.

bioRxiv · Apr 3, 2021 · PreprintImmunology

Single-cell sequencing of plasma cells from COVID-19 patients reveals highly expanded clonal lineages produce specific and neutralizing antibodies to SARS-CoV-2

R. A. Ehling, C. R. Weber, D. M. Mason, S. Friedensohn, B. Wagner, F. Bieberich, E. Kapetanovic, R. Vazquez-Lombardi, R. B. Di Roberto, K.-L. Hong, C. Wagner, D. J. Sheward, B. Murrell, A. Yermanos, A. Cuny, , S. T. Reddy

Single-cell sequencing and screening identify expanded plasma cell clones in COVID-19 patients producing SARS-CoV-2-specific neutralizing antibodies.

bioRxiv · Feb 12, 2021 · PreprintImmunology

SARS-CoV-2 protein subunit vaccination elicits potent neutralizing antibody responses

M. Mandolesi, D. J. Sheward, L. Hanke, J. Ma, P. Pushparaj, L. Perez Vidakovics, C. Kim, K. Lore, X. Castro Dopico, J. M. Coquet, G. McInerney, G. B. Karlsson Hedestam, B. Murrell

This study shows that SARS-CoV-2 spike protein subunit vaccines induce strong neutralizing antibodies in mice and macaques, with high titers after a single dose or dose-sparing regimen.

bioRxiv · Jul 31, 2020Immunology

Selection, biophysical and structural analysis of synthetic nanobodies that effectively neutralize SARS-CoV-2

T. F. Custodio, H. Das, D. J. Sheward, L. Hanke, S. Pazicky, J. Pieprzyk, M. Sorgenfrei, M. Schroer, A. Gruzinov, C. Jeffries, M. Graewert, D. I. Svergun, N. Dobrev, K. Remans, M. Seeger, , C. Löw

This study isolates and characterizes synthetic nanobodies that neutralize SARS-CoV-2, identifying Sb23 with high affinity and neutralization activity.

bioRxiv · Jun 23, 2020Biophysics