7KM5

Crystal structure of SARS-CoV-2 RBD complexed with Nanosota-1

Summary for 7KM5

• Entry DOI: 10.2210/pdb7km5/pdb
• Descriptor: Spike protein S1, nanobody, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• Functional Keywords: rbd, nanobody, viral protein, viral protein-immune system complex, viral protein/immune system
• Biological source: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2, COVID-19 virus); More
• Total number of polymer chains: 4
• Total formula weight: 79089.59

Authors

Ye, G.,Shi, K.,Aihara, H.,Li, F. (deposition date: 2020-11-02, release date: 2021-08-04, Last modification date: 2024-11-13)

Primary citation

Ye, G.,Gallant, J.,Zheng, J.,Massey, C.,Shi, K.,Tai, W.,Odle, A.,Vickers, M.,Shang, J.,Wan, Y.,Du, L.,Aihara, H.,Perlman, S.,LeBeau, A.,Li, F.
The development of Nanosota - 1 as anti-SARS-CoV-2 nanobody drug candidates.
Elife, 10:-, 2021

PubMed Abstract: Combating the COVID-19 pandemic requires potent and low-cost therapeutics. We identified a series of single-domain antibodies (i.e., nanobody), , from a camelid nanobody phage display library. Structural data showed that bound to the oft-hidden receptor-binding domain (RBD) of SARS-CoV-2 spike protein, blocking viral receptor angiotensin-converting enzyme 2 (ACE2). The lead drug candidate possessing an Fc tag () bound to SARS-CoV-2 RBD ~3000 times more tightly than ACE2 did and inhibited SARS-CoV-2 pseudovirus ~160 times more efficiently than ACE2 did. Administered at a single dose, demonstrated preventive and therapeutic efficacy against live SARS-CoV-2 infection in both hamster and mouse models. Unlike conventional antibodies, was produced at high yields in bacteria and had exceptional thermostability. Pharmacokinetic analysis of c documented an excellent in vivo stability and a high tissue bioavailability. As effective and inexpensive drug candidates, may contribute to the battle against COVID-19.

PubMed: 34338634
DOI: 10.7554/eLife.64815

Experimental method

X-RAY DIFFRACTION (3.19 Å)