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oai:figshare.com:article/34047331 2026-10-01T17:22:38Z category_8 category_12 category_24 category_272 category_39 category_46 category_734 category_64 category_132 category_134 portal_5 item_type_1 month_year_10_2026

Comparison of RhGB07 with other sarbecoviruses. Nazia Thakur (9904162) Joseph Newman (5638340) Dongchun Ni (15188356) Jeffrey Seow (9415776) Abigail L. Hay (25157576) Yeonjae Lee (12256119) Ayush Upadhyay (25157573) Babatunde E. Ekundayo (25157578) John A. Hammond (7431785) Thomas P. Peacock (6536120) Kelvin Lau (1847764) Katie J. Doores (346210) Dalan Bailey (193037) Microbiology Cell Biology Evolutionary Biology Environmental Sciences not elsewhere classified Ecology Immunology Biological Sciences not elsewhere classified Cancer Infectious Diseases Virology multiple bat coronaviruses g ., rc g ., civet clade 1 viruses restricted ace2 usage mammalian ace2 proteins g ., rhgb07 using monoclonal antibodies clade 1 sarbecoviruses div >< p determined host range converting enzyme 2 2 convalescent individuals ace2 ), via using binding assays antigenicity using sera related bat sarbecoviruses using sarbecoviruses host range clade 3 pangolin ), neutralising antibodies entry assays binding domain sarbecoviruses interact sarbecoviruses exhibited rodent ace2 like rhgb07 generalist ace2 related antigenicity zoonotic potential vitally important still evidence specialist </ shifting pattern robust evidence research indicates racoon dog novel structure largely maintained including human immunodominant target human primate generalist phenotypes generalist </ especially omicron entry phenotypes diverse panel continued evolution breakthrough infections (A) The C- α trace of the RBD of RhGB07 rendered as balls-and-sticks superimposed with the RBD apostructures of PRD-0038 (PDB 8U29), Khosta-1 (PDB 9J6G), Khosta-2 (PDB: 9J5U) and BtKY72 (PDB 8ZY0). The insets highlight regions of interest of the RBD that are either involved in binding of ACE2 or have presented structural changes across clades. (B) The C-α trace of the RBD of RhGB07 rendered as balls-and-sticks superimposed with the RBD of PRD-0038 apo or PRD-0038 bound to R. Alcyone ACE2 (PDB: 8U0T). The insets show a zoomed-in view of two regions of the RBD that show the greatest changes in the position of the C-α of the RBD. The region containing the ins1-loop and Δ4-loop coincides with putative ACE2-interacting residues based on mapping the equivalent residues. (C) RBD (top) and NTD (bottom) of RhGB07 cartoon depicted with the cryo-EM density contoured in this region. Residues comprising a putative fatty acid binding pocket as seen in SARS-CoV-2 RBD [<a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003944#pbio.3003944.ref039" target="_blank">39</a>] or a putative biliverdin binding pocket as seen in other coronavirus NTD [<a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003944#pbio.3003944.ref040" target="_blank">40</a>] are highlighted. No density was present in either of these pockets corresponding to a fatty acid or biliverdin, respectively. (D) Sequence conservation of selected sarbecoviruses were mapped onto the RhGB07 spike. Areas least conserved are in red and most conserved are blue. The least conserved regions are at the top of the RBD, the NTD and close to a putative polybasic site. (TIF) 2026-10-01T17:40:07Z Image Figure 10.1371/journal.pbio.3003944.s007 https://figshare.com/articles/figure/_p_Comparison_of_RhGB07_with_other_sarbecoviruses_p_/34047331 CC BY 4.0