tetano
Editor, Senior Moderator
Cell Rep Med
. 2024 May 2:101553.
doi: 10.1016/j.xcrm.2024.101553. Online ahead of print. A structure-function analysis shows SARS-CoV-2 BA.2.86 balances antibody escape and ACE2 affinity
Chang Liu[SUP] 1 [/SUP], Daming Zhou[SUP] 2 [/SUP], Aiste Dijokaite-Guraliuc[SUP] 3 [/SUP], Piyada Supasa[SUP] 4 [/SUP], Helen M E Duyvesteyn[SUP] 5 [/SUP], Helen M Ginn[SUP] 6 [/SUP], Muneeswaran Selvaraj[SUP] 4 [/SUP], Alexander J Mentzer[SUP] 7 [/SUP], Raksha Das[SUP] 4 [/SUP], Thushan I de Silva[SUP] 8 [/SUP], Thomas G Ritter[SUP] 9 [/SUP], Megan Plowright[SUP] 10 [/SUP], Thomas A H Newman[SUP] 10 [/SUP], Lizzie Stafford[SUP] 9 [/SUP], Barbara Kronsteiner[SUP] 11 [/SUP], Nigel Temperton[SUP] 12 [/SUP], Yuan Lui[SUP] 13 [/SUP], Martin Fellermeyer[SUP] 13 [/SUP], Philip Goulder[SUP] 14 [/SUP], Paul Klenerman[SUP] 15 [/SUP], Susanna J Dunachie[SUP] 16 [/SUP], Michael I Barton[SUP] 17 [/SUP], Mikhail A Kutuzov[SUP] 17 [/SUP], Omer Dushek[SUP] 17 [/SUP]; OPTIC Consortium; Elizabeth E Fry[SUP] 18 [/SUP], Juthathip Mongkolsapaya[SUP] 19 [/SUP], Jingshan Ren[SUP] 20 [/SUP], David I Stuart[SUP] 21 [/SUP], Gavin R Screaton[SUP] 22 [/SUP]
Affiliations
BA.2.86, a recently described sublineage of SARS-CoV-2 Omicron, contains many mutations in the spike gene. It appears to have originated from BA.2 and is distinct from the XBB variants responsible for many infections in 2023. The global spread and plethora of mutations in BA.2.86 has caused concern that it may possess greater immune-evasive potential, leading to a new wave of infection. Here, we examine the ability of BA.2.86 to evade the antibody response to infection using a panel of vaccinated or naturally infected sera and find that it shows marginally less immune evasion than XBB.1.5. We locate BA.2.86 in the antigenic landscape of recent variants and look at its ability to escape panels of potent monoclonal antibodies generated against contemporary SARS-CoV-2 infections. We demonstrate, and provide a structural explanation for, increased affinity of BA.2.86 to ACE2, which may increase transmissibility.
Keywords: ACE2 binding; BA.2.65; SARS-CoV-2; antigenic escape; coronavirus; receptor binding; virus evolution; virus structure.
. 2024 May 2:101553.
doi: 10.1016/j.xcrm.2024.101553. Online ahead of print. A structure-function analysis shows SARS-CoV-2 BA.2.86 balances antibody escape and ACE2 affinity
Chang Liu[SUP] 1 [/SUP], Daming Zhou[SUP] 2 [/SUP], Aiste Dijokaite-Guraliuc[SUP] 3 [/SUP], Piyada Supasa[SUP] 4 [/SUP], Helen M E Duyvesteyn[SUP] 5 [/SUP], Helen M Ginn[SUP] 6 [/SUP], Muneeswaran Selvaraj[SUP] 4 [/SUP], Alexander J Mentzer[SUP] 7 [/SUP], Raksha Das[SUP] 4 [/SUP], Thushan I de Silva[SUP] 8 [/SUP], Thomas G Ritter[SUP] 9 [/SUP], Megan Plowright[SUP] 10 [/SUP], Thomas A H Newman[SUP] 10 [/SUP], Lizzie Stafford[SUP] 9 [/SUP], Barbara Kronsteiner[SUP] 11 [/SUP], Nigel Temperton[SUP] 12 [/SUP], Yuan Lui[SUP] 13 [/SUP], Martin Fellermeyer[SUP] 13 [/SUP], Philip Goulder[SUP] 14 [/SUP], Paul Klenerman[SUP] 15 [/SUP], Susanna J Dunachie[SUP] 16 [/SUP], Michael I Barton[SUP] 17 [/SUP], Mikhail A Kutuzov[SUP] 17 [/SUP], Omer Dushek[SUP] 17 [/SUP]; OPTIC Consortium; Elizabeth E Fry[SUP] 18 [/SUP], Juthathip Mongkolsapaya[SUP] 19 [/SUP], Jingshan Ren[SUP] 20 [/SUP], David I Stuart[SUP] 21 [/SUP], Gavin R Screaton[SUP] 22 [/SUP]
Affiliations
- PMID: 38723626
- DOI: 10.1016/j.xcrm.2024.101553
BA.2.86, a recently described sublineage of SARS-CoV-2 Omicron, contains many mutations in the spike gene. It appears to have originated from BA.2 and is distinct from the XBB variants responsible for many infections in 2023. The global spread and plethora of mutations in BA.2.86 has caused concern that it may possess greater immune-evasive potential, leading to a new wave of infection. Here, we examine the ability of BA.2.86 to evade the antibody response to infection using a panel of vaccinated or naturally infected sera and find that it shows marginally less immune evasion than XBB.1.5. We locate BA.2.86 in the antigenic landscape of recent variants and look at its ability to escape panels of potent monoclonal antibodies generated against contemporary SARS-CoV-2 infections. We demonstrate, and provide a structural explanation for, increased affinity of BA.2.86 to ACE2, which may increase transmissibility.
Keywords: ACE2 binding; BA.2.65; SARS-CoV-2; antigenic escape; coronavirus; receptor binding; virus evolution; virus structure.