Author

B. S. Zha

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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Biochemistry· 2 Immunology· 2 Bioengineering· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Research Focus:host-pathogen & immune response· 4 Organism:human· 3 Assay:proteomics· 3 Assay:bulk RNA-seq· 1 Research Focus:drug response / drug discovery· 1 Assay:flow cytometry· 1 Organism:mouse· 1

Frequent Co-Authors

I. Lui· 2 shared J. A. Wells· 2 shared J. D. Ernst· 2 shared J. Liu· 2 shared K. K. Leung· 2 shared K. Schaefer· 2 shared N. J. Rettko· 2 shared P. Solomon· 2 shared

Activity by Year

2020-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 36 mutual co-author links

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2 shared papersBioengineering

I. Lui

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

Mycobacterium tuberculosis resides in lysosome-poor monocyte-derived lung cells during chronic infection

W. Zheng, I.-C. Chang, J. Limberis, J. M. Budzik, B. S. Zha, Z. Howard, L. Chen, J. D. Ernst

This study identifies lysosome-poor monocyte-derived lung cells as a niche for Mtb persistence during chronic infection, suggesting a target for host-directed therapy.

bioRxiv · Jan 19, 2023Immunology

Bacterial strain-dependent dissociation of cell recruitment and cell-to-cell spread in early M. tuberculosis infection

B. S. Zha, L. Desvignes, T. Fergus, A. Cornelius, T.-Y. Cheng, D. B. Moody, J. D. Ernst

This study compares early infection dynamics of two M. tuberculosis strains, showing strain-specific differences in bacterial spread and immune activation.

bioRxiv · May 10, 2022Immunology

An ultra-potent synthetic nanobody neutralizes SARS-CoV-2 by locking Spike into an inactive conformation

M. Schoof, B. Faust, R. A. Saunders, S. Sangwan, V. V. Rezelj, N. Hoppe, M. Boone, C. Billesboelle, C. Puchades, C. M. Azumaya, H. T. Kratochvil, M. Zimanyi, I. Deshpande, J. Liang, S. Dickinson, , Barile-H

This paper develops a potent synthetic nanobody that neutralizes SARS-CoV-2 by locking its Spike protein in an inactive conformation, enabling aerosol delivery as a prophylactic or therapeutic agent.

bioRxiv · Aug 8, 2020Biochemistry

Bi-paratopic and multivalent human VH domains neutralize SARS-CoV-2 by targeting distinct epitopes within the ACE2 binding interface of Spike

C. J. Bracken, S. A. Lim, P. Solomon, N. J. Rettko, D. P. Nguyen, B. S. Zha, K. Schaefer, J. R. Byrnes, J. Zhou, I. Lui, J. Liu, K. Pance, QCRG Structural Biology Consortium, X. X. Zhou, K. K. Leung, J. A. Wells

This paper identifies and engineers multivalent human VH domains that neutralize SARS-CoV-2 by targeting distinct epitopes on the Spike protein's ACE2 binding interface, showing increased affinity and potency.

bioRxiv · Aug 8, 2020 · PreprintBioengineering

Trimeric SARS-CoV-2 Spike interacts with dimeric ACE2 with limited intra-Spike avidity

I. Lui, X. X. Zhou, S. A. Lim, S. Elledge, P. Solomon, N. J. Rettko, B. S. Zha, L. L. Kirkemo, J. A. Gramespacher, J. Liu, F. Muecksch, J. C. C. Lorenzi, F. Schmidt, Y. Weisblum, D. F. Robbiani, , J. A. Wells

This study investigates the interaction between SARS-CoV-2 Spike and ACE2, showing that dimeric ACE2 binds with high affinity to Spike and blocks viral entry, with limited intra-Spike avidity.

bioRxiv · May 21, 2020 · PreprintBiochemistry