Author

N. Czudnochowski

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· 6 Microbiology· 4 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 11 Research Focus:host-pathogen & immune response· 8 Organism:human· 7 Assay:proteomics· 6 Research Focus:cell type annotation· 3 Assay:cryo-EM· 2 Research Focus:differential expression· 2 Research Focus:drug response / drug discovery· 2

Frequent Co-Authors

E. Cameroni· 8 shared K. Culap· 8 shared D. Pinto· 7 shared C. Havenar-Daughton· 6 shared J. E. Bowen· 6 shared L. E. Rosen· 6 shared A. Ceschi· 5 shared A. Telenti· 5 shared

Activity by Year

2019-2023 · peak 6/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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Curved chords = mutual co-authorship

8 shared papersImmunology

E. Cameroni

Mutual co-authors in cluster

Author profile →

11 papers

Recent·Most cited

Therapeutic and vaccine-induced cross-reactive antibodies with effector function against emerging Omicron variants

A. Addetia, L. Piccoli, J. B. Case, Y.-J. Park, M. Beltramello, B. Guarino, H. Dang, D. Pinto, S. Scheaffer, K. Sprouse, J. Bassi, C. Silacci-Fregni, F. Muoio, M. Dini, L. Vincenzetti, , Fran

The paper shows that cross-reactive antibodies, like S309, retain effector functions against emerging Omicron variants despite reduced neutralization.

bioRxiv · Jan 17, 2023 · PreprintImmunology

Maturation of SARS-CoV-2 Spike-specific memory B cells drives resilience to viral escape

R. Marzi, J. Bassi, C. Silacci-Fregni, I. Bartha, F. Muoio, K. Culap, N. Sprugasci, G. Lombardo, C. Saliba, E. Cameroni, A. Cassotta, J. S. Low, A. C. Walls, M. McCallum, M. A. Tortorici, , L. Piccoli

The paper examines the kinetics, avidity, and cross-reactivity of SARS-CoV-2-specific memory B cells and antibodies in infected and vaccinated individuals over 16 months, finding that MBC maturation enhances resilience to viral escape.

bioRxiv · Sep 30, 2022Immunology

Structural basis of SARS-CoV-2 Omicron immune evasion and receptor engagement

M. McCallum, N. Czudnochowski, L. E. Rosen, S. K. Zepeda, J. E. Bowen, J. R. Dillen, A. Powell, T. Croll, J. Nix, H. W. Virgin, D. Corti, G. Snell, D. Veesler

This study determines the structural basis of SARS-CoV-2 Omicron's immune evasion and receptor engagement through cryo-EM and X-ray crystal structures of the spike and RBD bound to antibodies and ACE2.

bioRxiv · Dec 28, 2021Biochemistry

Broadly neutralizing antibodies overcome SARS-CoV-2 Omicron antigenic shift

E. Cameroni, C. Saliba, J. E. Bowen, L. E. Rosen, K. Culap, D. Pinto, L. A. VanBlargan, A. De Marco, S. K. Zepeda, J. di Iulio, F. Zatta, H. Kaiser, J. Noack, N. Farhat, N. Czudnochowski, , P

This study shows that Omicron variant's spike protein has enhanced ACE2 binding and reduces neutralizing activity, but some broadly neutralizing antibodies remain effective.

bioRxiv · Dec 12, 2021Immunology

A human antibody that broadly neutralizes betacoronaviruses protects against SARS-CoV-2 by blocking the fusion machinery

D. Pinto, M. M. Sauer, N. Czudnochowski, J. S. Low, M. A. Tortorici, M. P. Housley, J. Noack, A. C. Walls, J. E. Bowen, B. Guarino, L. E. Rosen, J. di Iulio, J. Jerak, H. Kaiser, S. Islam, , Lanzave

This paper identifies a human antibody that broadly neutralizes betacoronaviruses by targeting the stem helix, showing protection against SARS-CoV-2 and potential for vaccine design.

bioRxiv · May 9, 2021 · PreprintImmunology

Structural basis for broad sarbecovirus neutralization by a human monoclonal antibody

M. A. Tortorici, N. Czudnochowski, T. N. Starr, R. Marzi, A. C. Walls, F. Zatta, J. E. Bowen, S. Jaconi, J. di Iulio, Z. Wang, A. De Marco, S. Zepeda, D. Pinto, Z. Liu, M. Beltramello, , J. Bloom

This paper identifies a human monoclonal antibody that broadly neutralizes SARS-CoV-2 variants and zoonotic sarbecoviruses by targeting a conserved epitope on the spike protein.

bioRxiv · Apr 7, 2021 · PreprintImmunology

Antibodies to the SARS-CoV-2 receptor-binding domain that maximize breadth and resistance to viral escape

T. N. Starr, N. Czudnochowski, F. Zatta, Y.-J. Park, Z. Liu, A. Addetia, D. Pinto, M. Beltramello, P. Hernandez, A. J. Greaney, R. Marzi, W. G. Glass, I. Zhang, A. S. Dingens, J. E. Bowen, , Veesler

This study identifies antibodies against SARS-CoV-2 that balance neutralization potency and breadth, with some showing high resistance to viral escape.

bioRxiv · Apr 6, 2021 · PreprintMicrobiology

The dual function monoclonal antibodies VIR-7831 and VIR-7832 demonstrate potent in vitro and in vivo activity against SARS-CoV-2

A. L. Cathcart, C. Havenar-Daughton, F. A. Lempp, D. Ma, M. Schmid, M. L. Agostini, B. Guarino, J. Di iulio, L. Rosen, H. Tucker, J. Dillen, S. Subramanian, B. Sloan, S. Bianchi, J. Wojcechowskyj, , C. M. Hebner

This paper evaluates the in vitro and in vivo efficacy of dual-action monoclonal antibodies VIR-7831 and VIR-7832 against SARS-CoV-2, showing potent neutralization and reduced viral load in a hamster model.

bioRxiv · Mar 9, 2021 · PreprintImmunology

The circulating SARS-CoV-2 spike variant N439K maintains fitness while evading antibody-mediated immunity

E. C. Thomson, L. E. Rosen, J. G. Shepherd, R. Spreafico, A. da Silva Filipe, J. A. Wojcechowskyj, C. Davis, L. Piccoli, D. J. Pascall, J. Dillen, S. Lytras, N. Czudnochowski, R. Shah, M. Meury, N. Jesudason, , J. Nichols

The paper shows the N439K SARS-CoV-2 spike variant maintains replication fitness while evading antibody neutralization.

bioRxiv · Nov 4, 2020Microbiology

A large inner membrane pore defines the ESX translocon

N. Poweleit, N. Czudnochowski, R. Nakagawa, K. C. Murphy, C. M. Sassetti, O. Rosenberg

The paper reports the cryo-EM structure of the ESX-3 secretion system, revealing a large pore capable of translocating folded substrates and a regulatory cytoplasmic complex.

bioRxiv · Oct 10, 2019 · PreprintMicrobiology

Two accessory proteins govern MmpL3 mycolic acid transport in mycobacteria

A. Fay, N. Czudnochowski, J. Rock, J. Johnson, N. Krogan, O. Rosenberg, M. Glickman

This study identifies two new proteins involved in the MmpL3-mediated mycolic acid transport in mycobacteria, revealing their roles in transport and stress response.

bioRxiv · Mar 27, 2019Microbiology