Mougari, S., Favède, V., Predella, C., Reynard, O., Durand, S., Mazelier, M., Pizzioli, E., Decimo, D., Bovier, F. T., Lapsley, L. M., Castagna, C., Lieberman, N. A. P., Noel, G., Mathieu, C., Malissen, B., Briese, T., Greninger, A. L., Alabi, C. A., Dorrello, N. V., … Horvat, B. (2025). Intranasally administrated fusion-inhibitory lipopeptides block SARS-CoV-2 infection in mice and enable long-term protective immunity. Communications Biology, 8(1). https://doi.org/10.1038/s42003-025-07491-4

Wang, Q., Guo, Y., Schwanz, L. T., Mellis, I. A., Sun, Y., Qu, Y., Urtecho, G., Valdez, R., Stoneman, E., Gordon, A., Wang, H. H., Ho, D. D., & Liu, L. (2024). SARS-CoV-2 omicron BA.2.87.1 exhibits higher susceptibility to serum neutralization than EG.5.1 and JN.1. Emerging Microbes & Infections, 13(1). https://doi.org/10.1080/22221751.2024.2359004

Wang, Q., Mellis, I. A., Ho, J., Bowen, A., Kowalski-Dobson, T., Valdez, R., Katsamba, P. S., Wu, M., Lee, C., Shapiro, L., Gordon, A., Guo, Y., Ho, D. D., & Liu, L. (2024). Recurrent SARS-CoV-2 spike mutations confer growth advantages to select JN.1 sublineages. Emerging Microbes & Infections, 13(1). https://doi.org/10.1080/22221751.2024.2402880

Wang, Q., Guo, Y., Liu, L., Schwanz, L. T., Li, Z., Nair, M. S., Ho, J., Zhang, R. M., Iketani, S., Yu, J., Huang, Y., Qu, Y., Valdez, R., Lauring, A. S., Huang, Y., Gordon, A., Wang, H. H., Liu, L., & Ho, D. D. (2023). Antigenicity and receptor affinity of SARS-CoV-2 BA.2.86 spike. Nature, 624(7992), 639–644. https://doi.org/10.1038/s41586-023-06750-w

Wilks, S. H., Mühlemann, B., Shen, X., Türeli, S., LeGresley, E. B., Netzl, A., Caniza, M. A., Chacaltana-Huarcaya, J. N., Corman, V. M., Daniell, X., Datto, M. B., Dawood, F. S., Denny, T. N., Drosten, C., Fouchier, R. A. M., Garcia, P. J., Halfmann, P. J., Jassem, A., Jeworowski, L. M., … Smith, D. J. (2023). Mapping SARS-CoV-2 antigenic relationships and serological responses. Science, 382(6666). https://doi.org/10.1126/science.adj0070

Liu, L., Casner, R. G., Guo, Y., Wang, Q., Iketani, S., Chan, J. F.-Woo., Yu, J., Dadonaite, B., Nair, M. S., Mohri, H., Reddem, E. R., Yuan, S., Poon, V. K.-M., Chan, C. C.-S., Yuen, K.-Y., Sheng, Z., Huang, Y., Bloom, J. D., Shapiro, L., & Ho, D. D. (2023). Antibodies targeting a quaternary site on SARS-CoV-2 spike glycoprotein prevent viral receptor engagement by conformational locking. Immunity, 56(10), 2442-2455.e8. https://doi.org/10.1016/j.immuni.2023.09.003

Sergeeva, A. P., Katsamba, P. S., Liao, J., Sampson, J. M., Bahna, F., Mannepalli, S., Morano, N. C., Shapiro, L., Friesner, R. A., & Honig, B. (2023). Free Energy Perturbation Calculations of Mutation Effects on SARS-CoV-2 RBD::ACE2 Binding Affinity. Journal of Molecular Biology, 435(15), 168187. https://doi.org/10.1016/j.jmb.2023.168187

Khan, K., Karim, F., Ganga, Y., Bernstein, M., Jule, Z., Reedoy, K., Cele, S., Lustig, G., Amoako, D., Wolter, N., Samsunder, N., Sivro, A., San, J. E., Giandhari, J., Tegally, H., Pillay, S., Naidoo, Y., Mazibuko, M., Miya, Y., … Sigal, A. (2022). Omicron BA.4/BA.5 escape neutralizing immunity elicited by BA.1 infection. Nature Communications, 13(1). https://doi.org/10.1038/s41467-022-32396-9

Marcink, T. C., Kicmal, T., Armbruster, E., Zhang, Z., Zipursky, G., Golub, K. L., Idris, M., Khao, J., Drew-Bear, J., McGill, G., Gallagher, T., Porotto, M., des Georges, A., & Moscona, A. (2022). Intermediates in SARS-CoV-2 spike–mediated cell entry. Science Advances, 8(33). https://doi.org/10.1126/sciadv.abo3153

Cerutti, G., Guo, Y., Liu, L., Liu, L., Zhang, Z., Luo, Y., Huang, Y., Wang, H. H., Ho, D. D., Sheng, Z., & Shapiro, L. (2022). Cryo-EM structure of the SARS-CoV-2 Omicron spike. Cell Reports, 38(9), 110428. https://doi.org/10.1016/j.celrep.2022.110428