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Профиль

Bloom lab

Профиль Vively

Lab studying molecular evolution of proteins and viruses. Affiliated with Fred Hutch & HHMI. Opinions are my own and do not reflect those of my employer. https://jbloomlab.org/

14,4 тыс. подписчиков847 подписок362 публикаций
⟳ Репост от Bloom lab
Hensley Lab

Our preprint examining the specificity of human antibodies that cross-react with subclade K H3N2 viruses was posted this morning on medRxiv. These studies have implications on what vaccine strains should be selected for next year’s influenza season. 1/ www.medrxiv.org/content/10.6...

Mapping the specificity of H3N2 strain-specific and cross-reactive human neutralizing antibodies elicited by the 2025-2026 influenza vaccineAn H3N2 variant, named subclade K, continues to circulate widely during the 2025-2026 influenza season. This virus possesses a hemagglutinin (HA) protein that has eleven substitutions relative to the ...www.medrxiv.org
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⟳ Репост от Bloom lab
Tim Yu

In new work by @jahn0.bsky.social and I in @jbloomlab.bsky.social, we investigate how sequence constraints differ across influenza HA subtypes. We find ~50% of sites in HA display substantially different amino-acid preferences across H3, H5, and H7. doi.org/10.64898/202...

Influenza hemagglutinin subtypes have different sequence constraints despite sharing extremely similar structuresHemagglutinins (HA) from different influenza A virus subtypes share as little as ∼40% amino acid identity, yet their protein structure and cell entry function are highly conserved. Here we examine the extent that sequence constraints on HA differ across three subtypes. To do this, we first use pseudovirus deep mutational scanning to measure how all amino-acid mutations to an H7 HA affect its cell entry function. We then compare these new measurements to previously described measurements of how all mutations to H3 and H5 HAs affect cell entry function. We find that ∼50% of HA sites display substantially diverged preferences for different amino acids across the HA subtypes. The sites with the most divergent amino-acid preferences tend to be buried and have biochemically distinct wildtype amino acids in the different HA subtypes. We provide an example of how rewiring the interactions among contacting residues has dramatically shifted which amino acids are tolerated at specific sites. Overall, our results show how proteins with the same structure and function can become subject to very different site-specific evolutionary constraints as their sequences diverge. ### Competing Interest Statement JDB consults for Apriori Bio, Invivyd, Pfizer, GSK, and the Vaccine Company. JDB and BD are inventors on Fred Hutch licensed patents related to the deep mutational scanning of viral proteins. National Institute of Allergy and Infectious Diseases, R01AI165821, 75N93021C00015 U.S. National Science Foundation, DGE-2140004 Howard Hughes Medical Institute, https://ror.org/006w34k90doi.org
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⟳ Репост от Bloom lab
Masaru Kanekiyo

Just out📢 Our new paper published in @natmicrobiol.nature.com describes highly potent cross-neutralizing human monoclonal antibodies against H5Nx influenza viruses. Close collaboration with Sara Andrews lab and Tongqing Zhou lab at the VRC. Link to the article: rdcu.be/eKV9T 1/2

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