Author

A. S. Olia

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· 9 Biochemistry· 1 Bioengineering· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 11 Research Focus:host-pathogen & immune response· 8 Assay:proteomics· 5 Research Focus:drug response / drug discovery· 4 Organism:human· 4 Organism:mouse· 3 Research Focus:protein structure prediction· 3 Organism:virus· 3

Frequent Co-Authors

P. D. Kwong· 11 shared T. Zhou· 10 shared Y. Tsybovsky· 9 shared J. R. Mascola· 7 shared I.-T. Teng· 6 shared L. Wang· 6 shared W. Shi· 6 shared A. Pegu· 5 shared

Activity by Year

2020-2022 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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11 shared papersImmunology

P. D. Kwong

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11 papers

Recent·Most cited

A multispecific antibody prevents immune escape and confers pan-SARS-CoV-2 neutralization

J. Misasi, R. R. Wei, L. Wang, A. Pegu, C.-J. Wei, O. Oloniniyi, T. Zhou, J. I. Moliva, B. Zhao, M. Choe, E. S. Yang, Y. Zhang, M. Boruszczak, M. Chen, K. Leung, , N. J. Sullivan

This paper develops multispecific antibodies that neutralize all SARS-CoV-2 variants, including Omicron, by targeting multiple epitopes on the spike protein.

bioRxiv · Jul 29, 2022 · PreprintImmunology

Potent and pan-neutralization of SARS-CoV-2 variants of concern by DARPins

V. K. Chonira, Y.-D. Kwon, J. Gorman, J. B. Case, Z. Ku, R. Simeon, R. G. Casner, D. R. Harris, A. S. Olia, T. Stevens, L. Shapiro, H. Boyd, Y. Tsybovsky, F. Krammer, M. Diamond, , Z. Chen

This paper reports the development of two DARPins, FSR16m and FSR22, that potently neutralize SARS-CoV-2 variants, including emerging ones, with efficacy comparable to therapeutic antibodies.

bioRxiv · May 30, 2022 · PreprintBioengineering

Vaccine-elicited murine antibody WS6 neutralizes diverse beta-coronaviruses by recognizing a helical stem supersite of vulnerability

W. Shi, L. Wang, T. Zhou, M. Sastry, E. S. Yang, Y. Zhang, M. Chen, X. Chen, M. Choe, A. Creanga, K. Leung, A. S. Olia, A. Pegu, R. Rawi, C.-H. Shen, , P. D. Kwong

This paper identifies an antibody, WS6, from a mouse immunized with SARS-CoV-2 spike mRNA, which neutralizes diverse beta-coronaviruses by targeting a conserved helical epitope on the S2 subunit.

bioRxiv · Jan 25, 2022Immunology

Structural basis for potent antibody neutralization of SARS-CoV-2 variants including B.1.1.529

T. Zhou, L. Wang, J. Misasi, A. Pegu, Y. Zhang, D. R. Harris, A. S. Olia, C. A. Talana, E. S. Yang, M. Chen, M. Choe, W. Shi, I.-T. Teng, A. Creanga, C. Jenkins, , P. D. Kwong

The paper identifies potent monoclonal antibodies that neutralize the B.1.1.529 SARS-CoV-2 variant and reveals structural mechanisms enabling their effectiveness.

bioRxiv · Dec 27, 2021Immunology

Augmenting Neutralization breadth against Diverse HIV-1 by increasing the Ab-Ag interface on V2

N. Gao, Y. Gai, L. Meng, C. Wang, W. Wang, X. Li, T. Gu, M. K. Louder, N. A. Doria-Rose, K. Wiehe, A. F. Nazzari, A. S. Olia, J. Gorman, R. Rawi, W. Wu, , F. Gao

This study identifies a lineage of antibodies from infected rhesus macaques that neutralize 54% of HIV-1 strains by expanding the antibody-Env interface around the V2 loop.

bioRxiv · Aug 7, 2021 · PreprintImmunology

Antibodies with potent and broad neutralizing activity against antigenically diverse and highly transmissible SARS-CoV-2 variants

L. Wang, T. Zhou, Y. Zhang, E. S. Yang, C. A. Schramm, W. Shi, A. Pegu, O. K. Oloninyi, A. Ransier, S. Darko, S. R. Narpala, C. Hatcher, D. R. Martinez, Y. Tsybovsky, E. Phung, , Mascol

The paper identifies ultrapotent antibodies from convalescent donors that neutralize SARS-CoV-2 variants and reduce escape mutant generation.

bioRxiv · Feb 25, 2021Immunology

Potent SARS-CoV-2 Neutralizing Antibodies Directed Against Spike N-Terminal Domain Target a Single Supersite

G. Cerutti, Y. Guo, T. Zhou, J. Gorman, M. Lee, M. Rapp, E. R. Reddem, J. Yu, F. Bahna, J. Bimela, Y. Huang, P. S. Katsamba, L. Lihong, M. S. Nair, R. Rawi, , L. Shapiro

This study identifies potent SARS-CoV-2 neutralizing antibodies targeting the N-terminal domain (NTD) and reveals they bind a common supersite on the spike protein.

bioRxiv · Jan 10, 2021Biochemistry

Paired heavy and light chain signatures contribute to potent SARS-CoV-2 neutralization in public antibody responses

B. B. Banach, G. Cerutti, A. S. Fahad, C.-H. Shen, M. Oliveira de Souza, P. S. Katsamba, Y. Tsybovsky, P. Wang, M. S. Nair, Y. Huang, I. M. Francino Urdaniz, P. J. Steiner, M. Gutierrez-Gonzalez, L. Liu, S. N. Lopez Acevedo, , B. J. DeKosky

This study identifies a public antibody class, IGHV3-53/3-66, with potent SARS-CoV-2 neutralization capabilities through paired heavy and light chain interactions.

bioRxiv · Dec 31, 2020Immunology

Cryo-EM Structures Delineate a pH-Dependent Switch that Mediates Endosomal Positioning of SARS-CoV-2 Spike Receptor-Binding Domains

T. Zhou, Y. Tsybovsky, A. S. Olia, J. Gorman, M. A. Rapp, G. Cerutti, G.-Y. Chuang, P. S. Katsamba, A. Nazzari, J. M. Sampson, A. Schon, P. D. Wang, J. Bimela, W. Shi, I.-T. Teng, , P. D. Kwong

This paper uses cryo-EM to show how SARS-CoV-2 spike protein undergoes pH-dependent structural changes that affect ACE2 binding and antibody evasion.

bioRxiv · Jul 4, 2020 · PreprintImmunology

Structure-Based Design with Tag-Based Purification and In-Process Biotinylation Enable Streamlined Development of SARS-CoV-2 Spike Molecular Probes

T. Zhou, I.-T. Teng, A. S. Olia, G. Cerutti, J. Gorman, A. Nazzari, W. Shi, Y. Tsybovsky, L. Wang, S. Wang, B. Zhang, Y. Zhang, P. S. Katsamba, Y. Petrova, B. B. Banach, , P. D. Kwong

The paper develops biotin-labeled SARS-CoV-2 spike molecular probes using structure-based design and purification methods, achieving high yields and enabling antibody characterization.

bioRxiv · Jun 22, 2020Immunology

A Platform Incorporating Trimeric Antigens into Self-Assembling Nanoparticles Reveals SARS-CoV-2-Spike Nanoparticles to Elicit Substantially Higher Neutralizing Responses than Spike Alone

B. Zhang, C. W. Chao, Y. Tsybovsky, O. M. Abiona, G. B. Hutchinson, J. I. Moliva, A. S. Olia, A. Pegu, E. Phung, G. Stewart-Jones, R. Verardi, L. Wang, S. Wang, A. Werner, E. S. Yang, , P. D. Kwong

This paper develops a nanoparticle platform for displaying trimeric antigens, showing that SARS-CoV-2 spike-LuS nanoparticles induce 25-fold higher neutralizing responses than spike alone.

bioRxiv · Jun 11, 2020Immunology