Author
Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.
8 papers
Recent·Most cited
L. Zhu, M. Pichon, Z. Pietras, X. Wang, J. Ren, E. E. Fry, D. I. Stuart, A. Perrakis, E. von Castelmur
The paper investigates structural plasticity in Parechovirus 2A proteins, revealing structural rearrangements that affect their oligomeric state and potential function in viral RNA replication.
bioRxiv · Apr 6, 2024 · PreprintBiochemistry
L. Sherry, K. Grehan, J. J. Swanson, M. W. Bahar, C. Porta, E. E. Fry, D. I. Stuart, D. Rowlands, N. J. Stonehouse
This paper produces and characterizes stabilized PV-3 virus-like particles using Pichia pastoris, showing improved thermostability and antigen ratio compared to wild-type PV-3.
bioRxiv · Sep 16, 2022Microbiology
M. W. Bahar, V. Nasta, H. Fox, L. Sherry, K. Grehan, C. Porta, A. J. Macadam, N. J. Stonehouse, D. J. Rowlands, E. E. Fry, D. I. Stuart
This study identifies a conserved glutathione binding site in poliovirus VLPs that can be targeted by antivirals and used to stabilize vaccines.
bioRxiv · Sep 8, 2022Biochemistry
A. Tuekprakhon, J. Huo, R. Nutalai, A. Dijokaite-Guraliuc, D. Zhou, H. M. Ginn, M. Sekvaraj, C. Liu, A. J. Mentzer, P. Supasa, H. M. E. Duyvesteyn, R. Das, D. Skelly, T. G. Ritter, A. Amini, , G. R. Screaton
This study shows that BA.4 and BA.5 variants are more resistant to neutralization by vaccine and BA.1 immune sera compared to BA.1 and BA.2.
bioRxiv · May 21, 2022 · PreprintMicrobiology
T. Shirasaki, H. Feng, H. M. E. Duyvesteyn, W. G. Fusco, K. L. McKnight, L. Xie, M. Boyce, S. Kumar, R. Barouch-Bentov, O. Gonzalez-Lopez, R. McNamara, L. Wang, A. Hertel-Wulff, X. Chen, S. Einav, , S. M. Lemon
This study identifies a viral export signal in hepatitis A virus that requires dual recruitment of HD-PTP and ALIX for nonlytic release in extracellular vesicles.
bioRxiv · Apr 26, 2022Microbiology
J. Huo, Y. Zhao, J. Ren, D. Zhou, H. M. E. Duyvesteyn, H. M. Ginn, L. Carrique, T. Malinauskas, R. R. Ruza, P. N. Shah, T. K. Tan, P. Rijal, N. Coombes, K. Bewley, J. Radecke, , D. I. Stuart
This paper identifies CR3022 as a monoclonal antibody that neutralizes SARS-CoV-2 by destroying its prefusion Spike conformation, suggesting therapeutic potential.
Cell Host & Microbe · Sep 1, 2020Peer-reviewedMicrobiology
L. Carrique, H. M. E. Duyvesteyn, T. Malinaukas, Y. Zhao, J. Ren, D. Zhou, T. S. Walter, J. Radecke, J. Huo, R. Ruza, P. N. Shah, E. E. Fry, D. I. Stuart
The paper identifies a lipid-binding pocket in the SARS-CoV-2 Spike that stabilizes the prefusion trimer and shields neutralizing epitopes, suggesting it as a potential drug target.
bioRxiv · Aug 13, 2020 · PreprintMicrobiology
D. Zhou, H. M. E. Duyvesteyn, C.-P. Chen, C.-G. Huang, T.-H. Chen, S.-R. Shih, Y.-C. Lin, C.-Y. Cheng, S.-H. Cheng, Y.-C. Huang, T.-Y. Lin, C. Ma, J. Huo, L. Carrique, T. Malinauskas, , K.-Y. A. Huang
This paper identifies an antibody, EY6A, from a convalescent patient that neutralizes SARS-CoV-2 and cross-reacts with SARS-CoV-1 by binding a conserved epitope on the Spike protein.
bioRxiv · Jun 12, 2020Microbiology