key: cord-0017523-lcs7t2i9 authors: Ramanathan, Muthukumar; Ferguson, Ian D; Miao, Weili; Khavari, Paul A title: SARS-CoV-2 B.1.1.7 and B.1.351 spike variants bind human ACE2 with increased affinity date: 2021-05-19 journal: Lancet Infect Dis DOI: 10.1016/s1473-3099(21)00262-0 sha: 7b80746e1de4c51d20ef9e2633ca8b1176734c3a doc_id: 17523 cord_uid: lcs7t2i9 nan In the initial stage of infection, virions bind lung airway epithelial cells with kinetics governed in part by spike-ACE2 binding affinities. Enhanced affinity likely mediates increased infectivity by lowering the effective concentration of virions required for cell entry and is a convergent feature in more transmissible SARS-CoV-2 variants arising in multiple geographical regions. Finally, characterisation of binding between variant spike proteins and cognate human receptor See Online for appendix ACE2 on the basis of microscale thermophoresis represents a potential surveillance strategy for predicting enhanced transmissibility of emerging SARS-CoV-2 variants harbouring novel spike mutations. We declare no competing interests. SARS-CoV-2 variants of concern in the United Stateschallenges and opportunities Spike mutation D614G alters SARS-CoV-2 fitness Emergence and rapid spread of a new severe acute respiratory syndrome-related coronavirus 2 (SARS-CoV-2) lineage with multiple spike mutations in South Africa Neutralizing activity of BNT162b2-elicited serum Loss of furin cleavage site attenuates SARS-CoV-2 pathogenesis Higher infectivity of the SARS-CoV-2 new variants is associated with K417N/T, E484K, and N501Y mutants: an insight from structural data