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7X7O

SARS-CoV-2 spike RBD in complex with neutralizing antibody UT28K

Summary for 7X7O
Entry DOI10.2210/pdb7x7o/pdb
DescriptorSpike protein S1, UT28K Fab, heavy chain, UT28K Fab, light chain (3 entities in total)
Functional Keywordssars-cov-2, spike, antibody, viral protein
Biological sourceSevere acute respiratory syndrome coronavirus 2
More
Total number of polymer chains12
Total formula weight310251.80
Authors
Primary citationOzawa, T.,Tani, H.,Anraku, Y.,Kita, S.,Igarashi, E.,Saga, Y.,Inasaki, N.,Kawasuji, H.,Yamada, H.,Sasaki, S.I.,Somekawa, M.,Sasaki, J.,Hayakawa, Y.,Yamamoto, Y.,Morinaga, Y.,Kurosawa, N.,Isobe, M.,Fukuhara, H.,Maenaka, K.,Hashiguchi, T.,Kishi, H.,Kitajima, I.,Saito, S.,Niimi, H.
Novel super-neutralizing antibody UT28K is capable of protecting against infection from a wide variety of SARS-CoV-2 variants.
Mabs, 14:2072455-2072455, 2022
Cited by
PubMed Abstract: Many potent neutralizing SARS-CoV-2 antibodies have been developed and used for therapies. However, the effectiveness of many antibodies has been reduced against recently emerging SARS-CoV-2 variants, especially the Omicron variant. We identified a highly potent SARS-CoV-2 neutralizing antibody, UT28K, in COVID-19 convalescent individuals who recovered from a severe condition. UT28K showed efficacy in neutralizing SARS-CoV-2 in an assay and prophylactic treatment, and the reactivity to the Omicron strain was reduced. The structural analyses revealed that antibody UT28K Fab and SARS-CoV-2 RBD protein interactions were mainly chain-dominated antigen-antibody interactions. In addition, a mutation analysis suggested that the emergence of a UT28K neutralization-resistant SARS-CoV-2 variant was unlikely, as this variant would likely lose its competitive advantage over circulating SARS-CoV-2. Our data suggest that UT28K offers potent protection against SARS-CoV-2, including newly emerging variants.
PubMed: 35543180
DOI: 10.1080/19420862.2022.2072455
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.75 Å)
Structure validation

239803

数据于2025-08-06公开中

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