Author

J. di Iulio

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· 7 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 8 Research Focus:host-pathogen & immune response· 8 Organism:human· 6 Assay:proteomics· 5 Research Focus:drug response / drug discovery· 3 Research Focus:cell type annotation· 2 Organism:mouse· 2 Research Focus:clustering· 1

Frequent Co-Authors

D. Pinto· 8 shared E. Cameroni· 7 shared J. E. Bowen· 7 shared A. De Marco· 6 shared A. Telenti· 6 shared H. Kaiser· 6 shared K. Culap· 6 shared A. C. Walls· 5 shared

Activity by Year

2021-2022 · peak 7/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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8 shared papersImmunology

D. Pinto

Mutual co-authors in cluster

Author profile →

8 papers

Recent·Most cited

Imprinted antibody responses against SARS-CoV-2 Omicron sublineages

Y.-J. Park, D. Pinto, A. C. Walls, Z. Liu, A. De Marco, F. Benigni, F. Zatta, C. Silacci-Fregni, J. Bassi, K. R. Sprouse, A. Addetia, J. E. Bowen, C. Stewart, M. Giurdanella, C. Saliba, , Piccoli

This study shows that hybrid immunity and vaccine boosters provide potent neutralizing activity against Omicron BA.1 and BA.2, while breakthrough infections induce nasal mucosal neutralization and identify an ultrapotent pan-variant antibody.

bioRxiv · May 8, 2022Immunology

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

SARS-CoV-2 immune evasion by variant B.1.427/B.1.429

M. McCallum, J. Bassi, A. De Marco, A. Chen, A. C. Walls, J. Di Iulio, M. A. Tortorici, M.-J. Navarro, C. Silacci-Fregni, C. Saliba, M. Agostini, D. Pinto, K. Culap, S. Bianchi, S. Jaconi, , D. Veesler

This study evaluates how the B.1.427/B.1.429 SARS-CoV-2 variant evades neutralizing antibodies through mutations in the RBD and NTD, showing reduced neutralization by both vaccine-induced and infection-derived antibodies.

bioRxiv · Mar 31, 2021 · PreprintImmunology

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

N-terminal domain antigenic mapping reveals a site of vulnerability for SARS-CoV-2

M. McCallum, A. De Marco, F. Lempp, M. A. Tortorici, D. Pinto, A. C. Walls, M. Beltramello, A. Chen, Z. Liu, F. Zatta, S. Zepeda, J. di Iulio, J. E. Bowen, M. Montiel-Ruiz, J. Zhou, , D. Veesler

The paper identifies a conserved antigenic supersite on the SARS-CoV-2 N-terminal domain recognized by neutralizing antibodies and shows its vulnerability to mutations in variants.

bioRxiv · Jan 14, 2021Immunology