Author

K. A. Matreyek

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Microbiology· 3 Biochemistry· 2 Bioengineering· 1 Biophysics· 1 Immunology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 6 Research Focus:host-pathogen & immune response· 4 Assay:proteomics· 4 Approach:deep learning· 3 Research Focus:drug response / drug discovery· 2 Organism:mouse· 2 Research Focus:protein folding & dynamics· 2 Organism:virus· 2

Frequent Co-Authors

N. C. Wu· 3 shared R. Lei· 3 shared T. J. C. Tan· 3 shared A. J. Greaney· 2 shared A. N. Loes· 2 shared B. Dadonaite· 2 shared C. Kieffer· 2 shared D. M. Fowler· 2 shared

Activity by Year

2020-2023 · peak 5/yr

Co-Author Collaboration Network

10 top collaborators · 16 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

3 shared papersBiochemistry

N. C. Wu

Mutual co-authors in cluster

Author profile →

8 papers

Recent·Most cited

Evidence of antigenic drift in the fusion machinery core of SARS-CoV-2 spike

T. J. C. Tan, A. Odle, R. Lei, K. A. Matreyek, S. Perlman, L.-Y. R. Wong, N. C. Wu

This study identifies S2 domain mutations in SARS-CoV-2 spike that reduce binding to antibodies, showing antigenic drift in this region and its impact on vaccine efficacy.

bioRxiv · Sep 27, 2023Microbiology

High-throughput identification of prefusion-stabilizing mutations in SARS-CoV-2 spike

T. J. C. Tan, Z. Mou, R. Lei, W. O. Ouyang, M. Yuan, G. Song, R. Andrabi, I. A. Wilson, C. Kieffer, X. Dai, K. A. Matreyek, N. C. Wu

The paper identifies mutations that stabilize the prefusion conformation of SARS-CoV-2 spike while improving expression, using a combination of fluorescence-based assays, cell display, and deep mutational scanning.

bioRxiv · Sep 24, 2022Biochemistry

Receptor binding domain (RBD) antibodies contribute more to SARS-CoV-2 neutralization when target cells express high levels of ACE2

A. G. Farrell, B. Dadonaite, A. J. Greaney, R. Eguia, A. N. Loes, N. M. Francko, J. Logue, J. M. Carreno, A. Abbad, H. Y. Chu, K. A. Matreyek, J. D. Bloom

This study shows that RBD antibodies contribute more to SARS-CoV-2 neutralization when target cells have high ACE2 expression, highlighting ACE2 levels as a critical experimental factor.

bioRxiv · Aug 29, 2022Immunology

Probing the biophysical constraints of SARS-CoV-2 spike N-terminal domain using deep mutational scanning

W. O. Ouyang, T. J. C. Tan, R. Lei, G. Song, C. Kieffer, R. Andrabi, K. A. Matreyek, N. C. Wu

This study quantifies the effects of NTD mutations on S protein expression and identifies mutations that enhance expression without altering antigenicity.

bioRxiv · Jun 20, 2022Biochemistry

Opto-MASS: a high-throughput engineering platform for genetically encoded fluorescentsensors enabling all optical in vivo detection of monoamines and neuropeptides

M. Rappleye, A. Gordon-Fennel, D. C. Castro, A. K. Matarasso, C. A. Zamorano, C. Stine, S. J. Wait, J. D. Lee, J. D. Siebart, A. Suko, N. C. Smith, J. Muster, K. A. Matreyek, D. M. Fowler, G. D. Stuber, , A. Berndt

The paper introduces Opto-MASS, a high-throughput platform for engineering fluorescent sensors to detect monoamines and neuropeptides in vivo by screening thousands of variants in mammalian cells.

bioRxiv · Jun 1, 2022 · PreprintBioengineering

Shifting mutational constraints in the SARS-CoV-2 receptor-binding domain during viral evolution

T. N. Starr, A. J. Greaney, W. W. Hannon, A. N. Loes, K. Hauser, J. R. Dillen, E. Ferri, A. Ghez Farrell, B. Dadonaite, M. McCallum, K. A. Matreyek, D. Corti, D. Veesler, G. Snell, J. D. Bloom

The paper analyzes epistatic shifts in SARS-CoV-2 RBD mutations across variants to understand how they influence ACE2 binding and future evolution.

bioRxiv · Feb 24, 2022Microbiology

Expanded ACE2 dependencies of diverse SARS-like coronavirus receptor binding domains

S. M. Roelle, N. Shukla, A. T. Pham, A. M. Bruchez, K. A. Matreyek

This study identifies ACE2 receptor usage by SARS-like coronaviruses, showing clade 3 viruses use Rhinolophus ACE2 while clade 2 viruses may use an unknown receptor.

bioRxiv · Dec 25, 2021Microbiology

The biophysical basis of protein domain compatibility

W. Coyote-Maestas, D. Nedrud, A. Suma, Y. He, K. A. Matreyek, D. M. Fowler, V. Carnevale, C. L. Myers, D. Schmidt

The paper uses high-throughput assays and machine learning to model biophysical interactions governing protein domain compatibility in fusion proteins.

bioRxiv · Dec 9, 2020 · PreprintBiophysics