Spike Glycoprotein, Coronavirus

Displaying 1 - 14 of 14CSV
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
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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
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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
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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
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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
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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
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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
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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
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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
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Hastie, K. M., Li, H., Bedinger, D., Schendel, S. L., Dennison, S. M., Li, K., Rayaprolu, V., Yu, X., Mann, C., Zandonatti, M., Diaz Avalos, R., Zyla, D., Buck, T., Hui, S., Shaffer, K., Hariharan, C., Yin, J., Olmedillas, E., Enriquez, A., … Saphire, E. O. (2021). Defining variant-resistant epitopes targeted by SARS-CoV-2 antibodies: A global consortium study. Science, 374(6566), 472–478. https://doi.org/10.1126/science.abh2315
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Banach, B. B., Cerutti, G., Fahad, A. S., Shen, C.-H., Oliveira De Souza, M., Katsamba, P. S., Tsybovsky, Y., Wang, P., Nair, M. S., Huang, Y., Francino-Urdániz, I. M., Steiner, P. J., Gutiérrez-González, M., Liu, L., López Acevedo, S. N., Nazzari, A. F., Wolfe, J. R., Luo, Y., Olia, A. S., … DeKosky, B. J. (2021). Paired heavy- and light-chain signatures contribute to potent SARS-CoV-2 neutralization in public antibody responses. Cell Reports, 37(1), 109771. https://doi.org/10.1016/j.celrep.2021.109771
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Sztain, T., Ahn, S.-H., Bogetti, A. T., Casalino, L., Goldsmith, J. A., Seitz, E., McCool, R. S., Kearns, F. L., Acosta-Reyes, F., Maji, S., Mashayekhi, G., McCammon, J. A., Ourmazd, A., Frank, J., McLellan, J. S., Chong, L. T., & Amaro, R. E. (2021). A glycan gate controls opening of the SARS-CoV-2 spike protein. Nature Chemistry, 13(10), 963–968. https://doi.org/10.1038/s41557-021-00758-3
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