Structural Basis for Potent Neutralization of Betacoronaviruses by Single-Domain Camelid Antibodies

• Published in: Cell Vol. 181; no. 5; pp. 1004 - 1015.e15
• Main Authors: Wrapp, Daniel, De Vlieger, Dorien, Corbett, Kizzmekia S., Torres, Gretel M., Wang, Nianshuang, Van Breedam, Wander, Roose, Kenny, van Schie, Loes, Hoffmann, Markus, Pöhlmann, Stefan, Graham, Barney S., Callewaert, Nico, Schepens, Bert, Saelens, Xavier, McLellan, Jason S.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 28.05.2020
• Subjects: Animals; antibodies; Antibodies, Neutralizing - chemistry; Antibodies, Neutralizing - immunology; Antibodies, Neutralizing - isolation & purification; Betacoronavirus - immunology; Camelidae; Camelids, New World - immunology; Coronavirus infections; Coronavirus Infections - therapy; COVID-19; cross reaction; Cross Reactions; crystal structure; epitopes; humans; immunoglobulin G; Immunoglobulin G - chemistry; Immunoglobulin G - immunology; llamas; membrane fusion; MERS; Middle East respiratory syndrome coronavirus; Models, Molecular; nanobody; neutralization; Pandemics; Pneumonia, Viral - therapy; Protein Domains; receptors; Receptors, Virus - chemistry; SARS; SARS-CoV-2; Single-Domain Antibodies - chemistry; Single-Domain Antibodies - immunology; Single-Domain Antibodies - isolation & purification; Spike Glycoprotein, Coronavirus - chemistry; Spike Glycoprotein, Coronavirus - immunology; therapeutics; viruses; COVID-19; SARS; SARS-CoV-2; nanobody; MERS

Coronaviruses make use of a large envelope protein called spike (S) to engage host cell receptors and catalyze membrane fusion. Because of the vital role that these S proteins play, they represent a vulnerable target for the development of therapeutics. Here, we describe the isolation of single-doma...