Author

S. Iketani

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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Microbiology· 15 Immunology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 15 Research Focus:host-pathogen & immune response· 13 Organism:human· 8 Organism:virus· 6 Assay:proteomics· 5 Research Focus:drug response / drug discovery· 4 Research Focus:cell type annotation· 1 Approach:deep learning· 1

Frequent Co-Authors

D. D. Ho· 15 shared Y. Guo· 13 shared L. Liu· 12 shared Y. Huang· 12 shared J. Yu· 11 shared Z. Sheng· 11 shared M. S. Nair· 7 shared M. Wang· 7 shared

Activity by Year

2020-2023 · peak 6/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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15 shared papersMicrobiology

D. D. Ho

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16 papers

Recent·Most cited

Antigenicity and receptor affinity of SARS-CoV-2 BA.2.86 spike

Q. Wang, Y. Guo, L. Liu, L. T. Schwanz, Z. Li, J. Ho, R. M. Zhang, S. Iketani, J. Yu, Y. Huang, Y. Qu, R. Valdez, A. S. Lauring, A. Gordon, H. H. Wang, , D. D. Ho

This paper evaluates the antigenicity and receptor affinity of the SARS-CoV-2 BA.2.86 subvariant, finding it not more resistant to human sera than other variants but with specific mAb resistance and high receptor affinity.

bioRxiv · Sep 24, 2023Microbiology

Antibodies that neutralize all current SARS-CoV-2 variants of concern by conformational locking

L. Liu, R. G. Casner, Y. Guo, Q. Wang, S. Iketani, J. F.-W. Chan, J. Yu, B. Dadonaite, M. S. Nair, H. Mohri, E. R. Reddem, S. Yuan, V. K.-M. Poon, C. C.-S. Chan, K.-Y. Yuen, , D. D. Ho

This study identifies two antibodies that neutralize all SARS-CoV-2 variants by locking the spike protein in a down conformation, showing a novel mechanism and potential for prophylaxis.

bioRxiv · Apr 8, 2023 · PreprintMicrobiology

Evolving antibody evasion and receptor affinity of the Omicron BA.2.75 sublineage of SARS-CoV-2

Q. Wang, Z. Li, Y. Guo, I. A. Mellis, S. Iketani, M. Liu, J. Yu, R. Valdez, A. S. Lauring, Z. Sheng, A. Gordon, L. Liu, D. D. Ho

The paper analyzes the receptor affinity and antibody evasion properties of SARS-CoV-2 BA.2.75 subvariants, identifying two evolutionary pathways and three mutations that influence their virological features.

bioRxiv · Mar 22, 2023Microbiology

Alarming antibody evasion properties of rising SARS-CoV-2 BQ and XBB subvariants

Q. Wang, S. Iketani, Z. Li, L. Liu, Y. Guo, Y. Huang, A. D. Bowen, M. Liu, M. Wang, J. Yu, R. Valdez, A. S. Lauring, Z. Sheng, H. H. Wang, A. Gordon, , D. D. Ho

This study shows that new SARS-CoV-2 BQ and XBB subvariants have significantly reduced neutralization by vaccines and monoclonal antibodies, suggesting a threat to current immunity.

bioRxiv · Nov 23, 2022Microbiology

Multiple pathways for SARS-CoV-2 resistance to nirmatrelvir

S. Iketani, H. Mohri, B. Culbertson, S. J. Hong, Y. Duan, M. I. Luck, M. K. Annavajhala, Y. Guo, Z. Sheng, A.-C. Uhlemann, S. P. Goff, Y. Sabo, H. Yang, A. Chavez, D. D. Ho

This study identifies multiple mutational pathways leading to nirmatrelvir resistance in SARS-CoV-2 through in vitro experiments and structural analysis.

bioRxiv · Aug 7, 2022Microbiology

Antigenic characterization of the SARS-CoV-2 Omicron subvariant BA.2.75

Q. Wang, S. Iketani, Z. Li, Y. Guo, A. Y. Yeh, M. Liu, J. Yu, Z. Sheng, Y. Huang, L. Liu, D. D. Ho

This study characterizes the antigenic properties of the SARS-CoV-2 Omicron subvariant BA.2.75, showing increased neutralization resistance to vaccinated sera and specific monoclonal antibodies.

bioRxiv · Jul 31, 2022Microbiology

The Functional Landscape of SARS-CoV-2 3CL Protease

S. Iketani, S. J. Hong, J. Sheng, F. Bahari, B. Culbertson, F. F. Atanaki, A. K. Aditham, A. F. Kratz, M. I. Luck, R. Tian, S. P. Goff, H. Montazeri, Y. Sabo, D. D. Ho, A. Chavez

This study maps the functional landscape of SARS-CoV-2 3CL protease by profiling all single mutants and identifies resistance mutations to nirmatrelvir.

bioRxiv · Jun 23, 2022 · PreprintMicrobiology

Antibody evasion by SARS-CoV-2 Omicron subvariants BA.2.12.1, BA.4, and BA.5

Q. Wang, Y. Guo, S. Iketani, Z. Li, H. Mohri, M. Wang, J. Yu, A. D. Bowen, J. Y. Chan, J. G. Shah, N. Nguyen, Z. Chen, K. Meyers, M. T. Yin, M. E. Sobieszczyk, , D. Ho

This study analyzes antibody evasion by SARS-CoV-2 Omicron subvariants BA.2.12.1, BA.4, and BA.5, finding BA.4/5 shows greater resistance to neutralizing antibodies than BA.2.12.1.

bioRxiv · May 26, 2022Microbiology

Antibody Evasion Properties of SARS-CoV-2 Omicron Sublineages

S. Iketani, L. Liu, Y. Guo, L. Liu, Y. Huang, M. Wang, Y. Luo, J. Yu, M. T. Yin, M. E. Sobieszczyk, Y. Huang, H. H. Wang, Z. Sheng, D. D. Ho

This study characterizes the antigenic properties of SARS-CoV-2 Omicron sublineages BA.1+R346K and BA.2, showing they exhibit significant antibody evasion similar to BA.1.

bioRxiv · Feb 7, 2022Microbiology

Functional properties of the spike glycoprotein of the emerging SARS-CoV-2 variant B.1.1.529

Q. Wang, S. Anang, S. Iketani, Y. Guo, L. Liu, D. D. Ho, J. G. Sodroski

This study compares the functional properties of the B.1.1.529 SARS-CoV-2 spike glycoprotein with previous variants, finding reduced processing and lower stability but equivalent infection efficiency and increased ACE2 binding affinity.

bioRxiv · Dec 27, 2021Microbiology

Striking Antibody Evasion Manifested by the Omicron Variant of SARS-CoV-2

L. Liu, S. Iketani, Y. Guo, J. F.-W. Chan, M. Wang, L. Liu, Y. Luo, H. Chu, Y. Huang, M. S. Nair, J. Yu, K. K.-H. Chik, T. T.-T. Yuen, C. Yoon, K. K.-W. To, , D. D. Ho

This study shows that the Omicron variant of SARS-CoV-2 is highly resistant to neutralization by convalescent serum and vaccines, and many monoclonal antibodies.

bioRxiv · Dec 14, 2021Microbiology

Isolation and comparative analysis of antibodies that broadly neutralize sarbecoviruses

L. Liu, S. Iketani, Y. Guo, R. Casner, E. Reddem, M. S. Nair, J. Yu, J. Chan, M. Wang, G. Cerutti, Z. Li, C. Castagna, L. Corredor, H. Chu, S. Yuan, , D. D. Ho

The paper identifies a human monoclonal antibody that neutralizes all tested sarbecoviruses and describes a new antibody class with potential for pandemic preparedness.

bioRxiv · Dec 11, 2021 · PreprintMicrobiology

A monoclonal antibody that neutralizes SARS-CoV-2 variants, SARS-CoV, and other sarbecoviruses

P. Wang, R. G. Casner, M. S. Nair, J. Yu, Y. Guo, M. Wang, J. F. W. Chan, G. Cerutti, S. Iketani, L. Liu, Z. Sheng, Z. Chen, K.-Y. Yuen, P. D. Kwong, Y. Huang, , D. D. Ho

This paper identifies a monoclonal antibody, 2-36, that neutralizes SARS-CoV-2 variants, SARS-CoV, and other sarbecoviruses, with a conserved epitope in the RBD identified through cryo-EM.

bioRxiv · Oct 13, 2021Microbiology

Antibody Resistance of SARS-CoV-2 Variants B.1.351 and B.1.1.7

P. Wang, M. S. Nair, L. Liu, S. Iketani, Y. Luo, Y. Guo, M. Wang, J. Yu, B. Zhang, P. D. Kwong, B. S. Graham, J. R. Mascola, J. Y. Chang, M. T. Yin, M. E. Sobieszczyk, , D. D. Ho

This study evaluates the neutralization resistance of SARS-CoV-2 variants B.1.1.7 and B.1.351 to monoclonal antibodies and sera, finding increased resistance in B.1.351.

bioRxiv · Jan 25, 2021 · PreprintImmunology

A simplified cell-based assay to identify coronavirus 3CL protease inhibitors

S. J. Resnick, S. Iketani, S. J. Hong, A. Zask, H. Liu, S. Kim, S. Melore, M. S. Nair, Y. Huang, N. E. S. Tay, T. Rovis, H. W. Yang, B. R. Stockwell, D. D. Ho, A. Chavez

This paper introduces a cell-based assay to identify coronavirus 3CL protease inhibitors without live virus, demonstrating its effectiveness through compound screening and structure-activity profiling.

bioRxiv · Aug 29, 2020 · PreprintMicrobiology

Lead compounds for the development of SARS-CoV-2 3CL protease inhibitors

S. Iketani, F. Forouhar, H. Liu, S. J. Hong, F.-Y. Lin, M. S. Nair, A. Zask, Y. Huang, L. Xing, B. R. Stockwell, A. Chavez, D. D. Ho

The paper identifies three structurally diverse compounds as inhibitors of the SARS-CoV-2 3CL protease and provides structural insights for inhibitor design.

bioRxiv · Aug 3, 2020Microbiology