T. J. C. Tan

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.

This study curates a dataset of influenza HA antibodies and develops an explainable language model to predict antibody specificity, identifying and validating HA stem antibodies.

This study shows that human respiratory syncytial virus can propagate in black flying fox kidney cells without prior adaptation, suggesting these cells are a useful model for studying RSV infection.

This study shows that IGV allelic polymorphisms widely affect antibody reactivity by analyzing antibody-antigen structures and experimental data.

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.

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

This study shows that intersegment epistasis between hemagglutinin and neuraminidase constrains the evolutionary potential of the influenza A virus hemagglutinin gene.

The paper identifies deleterious mutations in human influenza H3N2 neuraminidase and reveals epistatic networks shaping its evolution.

The paper shows that natural mutations in human H3N2 HA influence the egg-adaptation pathway, affecting mutation emergence during vaccine production.

This study identifies how influenza A virus nucleoprotein interactions with gene segment UTRs selectively modulate viral gene expression, revealing a new role for NP in gene-segment specific regulation.

This study shows that Caprin-1 binds to G3BP1's NTF2 domain with pH sensitivity, regulating stress granule formation through a SLiM-mediated mechanism.

The paper identifies two public IGHV3-53/3-66 clonotypes with distinct CDR H3 motifs and shows Y58F mutation enhances binding affinity to SARS-CoV-2 RBD.