Author

P. Supasa

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· 5 Immunology· 2 Biophysics· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 7 Research Focus:host-pathogen & immune response· 6 Organism:human· 4 Organism:virus· 4 Assay:proteomics· 3 Research Focus:cell-cell communication· 2 Approach:statistical model· 2 Assay:structural biology· 2

Frequent Co-Authors

J. Mongkolsapaya· 7 shared D. Zhou· 5 shared W. Dejnirattisai· 5 shared C. Liu· 4 shared D. I. Stuart· 4 shared G. R. Screaton· 4 shared H. M. E. Duyvesteyn· 4 shared J. Huo· 4 shared

Activity by Year

2020-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 44 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

7 shared papersMicrobiology

J. Mongkolsapaya

Mutual co-authors in cluster

Author profile →

8 papers

Recent·Most cited

Cooperativity and induced oligomerisation control the interaction of SARS- CoV-2 with its cellular receptor and patient-derived antibodies

R. Asor, A. Olerinyova, S. A. Burnap, M. S. Kushwah, F. Soltermann, L. P. Rudden, M. Hensen, S. Vasiljevic, J. Brun, M. Hill, L. Chang, W. Dejnirattisai, P. Supasa, J. Mongkolsapaya, D. Zhou, , P. Kukura

The paper investigates how multivalent interactions between SARS-CoV-2 spike protein, ACE2 receptor, and patient-derived antibodies influence viral entry and antibody inhibition.

bioRxiv · Sep 14, 2023 · PreprintBiophysics

Analysis of emergent bivalent antibody binding identifies the molecular reach as a critical determinant of SARS-CoV-2 neutralisation potency

A. Huhn, D. A. Nissley, D. B. Wilson, M. A. Kutuzov, R. Donat, T. K. Tan, Y. Zhang, M. I. Barton, C. Liu, W. Dejnirattisai, P. Supasa, J. Mongkolsapaya, A. Townsend, W. S. James, G. Screaton, , O. Dushek

This paper develops a bivalent binding model to analyze how molecular reach affects SARS-CoV-2 neutralization potency across antibodies.

bioRxiv · Sep 6, 2023 · PreprintImmunology

Further antibody escape by Omicron BA.4 and BA.5 from vaccine and BA.1 serum

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

Omicron-B.1.1.529 leads to widespread escape from neutralizing antibody responses

W. Dejnirattisai, J. Huo, D. Zhou, J. Zahradni_k, P. Supasa, C. Liu, H. M. E. Duyvesteyn, H. Ginn, A. J. Mentzer, A. Tuekprakhon, R. Nutalai, B. - Wang, A. Dijokaite, S. Khan, O. Avinoam, , Mad

This study shows that Omicron-B.1.1.529 has extensive mutations in Spike that reduce neutralization by antibodies from vaccinated and previously infected individuals, and escape most monoclonal antibodies.

bioRxiv · Dec 3, 2021 · PreprintMicrobiology

Native-like SARS-CoV-2 spike glycoprotein expressed by ChAdOx1 nCoV-19/AZD1222 vaccine

Y. Watanabe, L. Mendonca, E. R. Allen, A. Howe, M. Lee, J. D. Allen, H. Chawla, D. Pulido, F. Donnellan, H. Davies, M. Ulaszewska, S. Belij-Rammerstorfer, S. Morris, A.-S. Krebs, W. Dejnirattisai, , M. Crispin

This study characterizes the structure, conformation, and glycosylation of the SARS-CoV-2 spike protein expressed by the ChAdOx1 nCoV-19/AZD1222 vaccine, confirming its native-like properties.

bioRxiv · Jan 15, 2021Microbiology

Neutralization of SARS-CoV-2 by destruction of the prefusion Spike

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

Structural basis for the neutralization of SARS-CoV-2 by an antibody from a convalescent patient

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

Broad and strong memory CD4+ and CD8+ T cells induced by SARS-CoV-2 in UK convalescent COVID-19 patients.

T. Dong, Y. Peng, A. J. Mentzer, G. Liu, X. Yao, Z. Yin, D. Dong, W. Dejnirattisai, L. Turtle, T. Rostron, K. Subramaniam, P. Thomson, P. Zhang, C. Dold, J. Ratcliff, , Lopez-C

This study examines T cell immunity in UK COVID-19 patients, finding stronger and broader memory T cell responses in severe cases, with implications for vaccine design.

bioRxiv · Jun 5, 2020Immunology