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8D5A

Middle state of SARS-CoV-2 BA.2 variant spike protein

This is a non-PDB format compatible entry.
Summary for 8D5A
Entry DOI10.2210/pdb8d5a/pdb
EMDB information27207
DescriptorSpike glycoprotein, alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
Functional Keywordsviral protein
Biological sourceSevere acute respiratory syndrome coronavirus 2
Total number of polymer chains3
Total formula weight454153.22
Authors
Zhang, J.,Tang, W.C.,Gao, H.L.,Shi, W.,Peng, H.Q.,Volloch, S.R.,Xiao, T.S.,Chen, B. (deposition date: 2022-06-04, release date: 2023-06-07, Last modification date: 2024-11-06)
Primary citationZhang, J.,Tang, W.,Gao, H.,Lavine, C.L.,Shi, W.,Peng, H.,Zhu, H.,Anand, K.,Kosikova, M.,Kwon, H.J.,Tong, P.,Gautam, A.,Rits-Volloch, S.,Wang, S.,Mayer, M.L.,Wesemann, D.R.,Seaman, M.S.,Lu, J.,Xiao, T.,Xie, H.,Chen, B.
Structural and functional characteristics of the SARS-CoV-2 Omicron subvariant BA.2 spike protein.
Nat.Struct.Mol.Biol., 30:980-990, 2023
Cited by
PubMed Abstract: The Omicron subvariant BA.2 has become the dominant circulating strain of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) in many countries. Here, we have characterized structural, functional and antigenic properties of the full-length BA.2 spike (S) protein and compared replication of the authentic virus in cell culture and an animal model with previously prevalent variants. BA.2 S can fuse membranes slightly more efficiently than Omicron BA.1, but still less efficiently than other previous variants. Both BA.1 and BA.2 viruses replicated substantially faster in animal lungs than the early G614 (B.1) strain in the absence of pre-existing immunity, possibly explaining the increased transmissibility despite their functionally compromised spikes. As in BA.1, mutations in the BA.2 S remodel its antigenic surfaces, leading to strong resistance to neutralizing antibodies. These results suggest that both immune evasion and replicative advantage may contribute to the heightened transmissibility of the Omicron subvariants.
PubMed: 37430064
DOI: 10.1038/s41594-023-01023-6
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.1 Å)
Structure validation

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