Author

G. M. McInerney

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· 4 Biochemistry· 2 Biophysics· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 8 Organism:human· 6 Assay:proteomics· 5 Research Focus:cell type annotation· 4 Research Focus:host-pathogen & immune response· 4 Approach:deep learning· 1 Research Focus:drug response / drug discovery· 1 Organism:mouse· 1

Frequent Co-Authors

L. Hanke· 6 shared B. Murrell· 5 shared D. J. Sheward· 4 shared A. Pankow· 3 shared C. Kim· 3 shared E. Urgard· 3 shared H. Das· 3 shared J. M. Coquet· 3 shared

Activity by Year

2019-2022 · peak 5/yr

Co-Author Collaboration Network

10 top collaborators · 43 mutual co-author links

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Curved chords = mutual co-authorship

6 shared papersImmunology

L. Hanke

Mutual co-authors in cluster

Author profile →

8 papers

Recent·Most cited

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

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

Large scale discovery of coronavirus-host factor protein interaction motifs reveals SARS-CoV-2 specific mechanisms and vulnerabilities

T. Kruse, C. Benz, D. H. Garvanska, R. Lindqvist, F. Mihalic, F. Coscia, R. Inturi, A. Sayadi, L. Simonetti, E. Nilsson, M. Ali, J. Kliche, A. Moliner Morro, A. Mund, E. Andersson, , Y. Ivarsson

The paper identifies coronavirus-host protein interaction motifs, revealing SARS-CoV-2 specific mechanisms and a peptide-based inhibitor that blocks infection.

bioRxiv · Apr 19, 2021Biochemistry

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

A bispecific monomeric nanobody induces spike trimer dimers and neutralizes SARS-CoV-2 in vivo

L. Hanke, H. Das, D. Sheward, L. Perez Vidakovics, E. Urgard, A. Moliner Morro, K. Changil, V. Karl, A. Pankow, N. Smith, B. Porebski, O. Fernandez-Capetillo, E. Sezgin, G. Pedersen, J. M. Coquet, , G. M. McInerney

A bispecific nanobody neutralizes SARS-CoV-2 and its variant B.1.351 by inducing spike trimer-dimers that prevent ACE2 binding.

bioRxiv · Mar 20, 2021Immunology

Caprin-1 binding to the critical stress granule protein G3BP1 is regulated by pH

T. Schulte, M. D. Panas, L. Wiliams, N. Kedersha, J. S. Fleck, T. J. C. Tan, A. Olsson, A. M. Morro, L. Hanke, J. Nilvebrant, K. A. Giang, P.-A. Nygren, P. Anderson, A. Achour, G. M. McInerney

This study shows that Caprin-1 binds to G3BP1's NTF2 domain with pH sensitivity, regulating stress granule formation through a SLiM-mediated mechanism.

bioRxiv · Feb 5, 2021Biochemistry

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

Separate domains of G3BP promote efficient clustering of alphavirus replication complexes and recruitment of the translation initiation machinery

B. Gotte, M. D. Panas, K. Hellstrom, L. Liu, B. Samreen, O. Larsson, T. Ahola, G. M. McInerney

This study shows that G3BP domains are required for alphavirus replication complex clustering and translation initiation, with SFV and CHIKV relying on different G3BP domains for replication.

bioRxiv · Apr 5, 2019Microbiology