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TitleStructural and biochemical mechanism for increased infectivity and immune evasion of Omicron BA.2 variant compared to BA.1 and their possible mouse origins.
Journal, issue, pagesCell Res, Vol. 32, Issue 7, Page 609-620, Year 2022
Publish dateMay 31, 2022
AuthorsYouwei Xu / Canrong Wu / Xiaodan Cao / Chunyin Gu / Heng Liu / Mengting Jiang / Xiaoxi Wang / Qingning Yuan / Kai Wu / Jia Liu / Deyi Wang / Xianqing He / Xueping Wang / Su-Jun Deng / H Eric Xu / Wanchao Yin /
PubMed AbstractThe Omicron BA.2 variant has become a dominant infective strain worldwide. Receptor binding studies show that the Omicron BA.2 spike trimer exhibits 11-fold and 2-fold higher potency in binding to ...The Omicron BA.2 variant has become a dominant infective strain worldwide. Receptor binding studies show that the Omicron BA.2 spike trimer exhibits 11-fold and 2-fold higher potency in binding to human ACE2 than the spike trimer from the wildtype (WT) and Omicron BA.1 strains. The structure of the BA.2 spike trimer complexed with human ACE2 reveals that all three receptor-binding domains (RBDs) in the spike trimer are in open conformation, ready for ACE2 binding, thus providing a basis for the increased infectivity of the BA.2 strain. JMB2002, a therapeutic antibody that was shown to efficiently inhibit Omicron BA.1, also shows potent neutralization activities against Omicron BA.2. In addition, both BA.1 and BA.2 spike trimers are able to bind to mouse ACE2 with high potency. In contrast, the WT spike trimer binds well to cat ACE2 but not to mouse ACE2. The structures of both BA.1 and BA.2 spike trimer bound to mouse ACE2 reveal the basis for their high affinity interactions. Together, these results suggest a possible evolution pathway for Omicron BA.1 and BA.2 variants via a human-cat-mouse-human circle, which could have important implications in establishing an effective strategy for combating SARS-CoV-2 viral infections.
External linksCell Res / PubMed:35641567 / PubMed Central
MethodsEM (single particle)
Resolution2.6 - 3.48 Å
Structure data

33336

7xo4

EMDB-33336, PDB-7xo4:
SARS-CoV-2 Omicron BA.1 Variant Spike Trimer with two mouse ACE2 Bound
Method: EM (single particle) / Resolution: 3.24 Å

33337

7xo5

EMDB-33337, PDB-7xo5:
SARS-CoV-2 Omicron BA.1 Variant Spike Trimer with one mouse ACE2 Bound
Method: EM (single particle) / Resolution: 3.13 Å

33338

7xo6

EMDB-33338, PDB-7xo6:
SARS-CoV-2 Omicron BA.1 Variant RBD with mouse ACE2 Bound
Method: EM (single particle) / Resolution: 2.6 Å

33339

7xo7

EMDB-33339, PDB-7xo7:
SARS-CoV-2 Omicron BA.2 Variant Spike Trimer with two human ACE2 Bound
Method: EM (single particle) / Resolution: 3.38 Å

33340

7xo8

EMDB-33340, PDB-7xo8:
SARS-CoV-2 Omicron BA.2 Variant Spike Trimer with three human ACE2 Bound
Method: EM (single particle) / Resolution: 3.48 Å

33341

7xo9

EMDB-33341, PDB-7xo9:
SARS-CoV-2 Omicron BA.2 Variant RBD complexed with human ACE2
Method: EM (single particle) / Resolution: 3.0 Å

33342

7xoa

EMDB-33342, PDB-7xoa:
SARS-CoV-2 Omicron BA.2 Variant Spike Trimer with one mouse ACE2 Bound
Method: EM (single particle) / Resolution: 3.2 Å

33343

7xob

EMDB-33343, PDB-7xob:
SARS-CoV-2 Omicron BA.2 Variant Spike Trimer with two mouse ACE2 Bound
Method: EM (single particle) / Resolution: 3.3 Å

33344

7xoc

EMDB-33344, PDB-7xoc:
SARS-CoV-2 Omicron BA.2 Variant RBD complexed with mouse ACE2
Method: EM (single particle) / Resolution: 3.0 Å

33345

7xod

EMDB-33345, PDB-7xod:
SARS-CoV-2 Omicron BA.2 Variant Spike Trimer with three JMB2002 Fab Bound
Method: EM (single particle) / Resolution: 3.27 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

ChemComp-ZN:
Unknown entry

ChemComp-CL:
Unknown entry / Chloride

Source
  • severe acute respiratory syndrome coronavirus 2
  • mus musculus (house mouse)
  • homo sapiens (human)
  • lama glama (llama)
KeywordsVIRAL PROTEIN / SARS-CoV-2 / Omicron / Spike / mouse ACE2 / VIRAL PROTEIN/HYDROLASE / VIRAL PROTEIN-HYDROLASE COMPLEX / VIRAL PROTEIN/IMMUNE SYSTEM / VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX

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