ArticleCell reports2020
Structure-Based Design with Tag-Based Purification and In-Process Biotinylation Enable Streamlined Development of SARS-CoV-2 Spike Molecular Probes.
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Article in Cell reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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55 citing papers in PubMed, 73 citations in OpenAlex.
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Authors and funding
38 authors at 5 institutions in 1 country.
Tongqing ZhouVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
I-Ting TengVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Adam S OliaVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Gabriele CeruttiDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.
Jason GormanVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Alexandra NazzariVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Wei ShiVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Yaroslav TsybovskyElectron Microscopy Laboratory, Cancer Research Technology Program, Leidos Biomedical Research Inc., Frederick National Laboratory for Cancer Research, Frederick, MD 21701, USA.
Lingshu WangVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Shuishu WangVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Baoshan ZhangVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Yi ZhangVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Phinikoula S KatsambaDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.
Yuliya PetrovaVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Bailey B BanachBioengineering Graduate Program, The University of Kansas, Lawrence, KS 66045, USA.
Ahmed S FahadDepartment of Pharmaceutical Chemistry, The University of Kansas, Lawrence, KS 66045, USA.
Lihong LiuAaron Diamond AIDS Research Center, Columbia University Vagelos College of Physicians and Surgeons, New York, NY 10032, USA.
Sheila N Lopez AcevedoDepartment of Pharmaceutical Chemistry, The University of Kansas, Lawrence, KS 66045, USA.
Bharat MadanDepartment of Pharmaceutical Chemistry, The University of Kansas, Lawrence, KS 66045, USA.
Matheus Oliveira de SouzaDepartment of Pharmaceutical Chemistry, The University of Kansas, Lawrence, KS 66045, USA.
Xiaoli PanDepartment of Pharmaceutical Chemistry, The University of Kansas, Lawrence, KS 66045, USA.
Pengfei WangAaron Diamond AIDS Research Center, Columbia University Vagelos College of Physicians and Surgeons, New York, NY 10032, USA.
Jacy R WolfeDepartment of Pharmaceutical Chemistry, The University of Kansas, Lawrence, KS 66045, USA.
Michael YinAaron Diamond AIDS Research Center, Columbia University Vagelos College of Physicians and Surgeons, New York, NY 10032, USA.
David D HoAaron Diamond AIDS Research Center, Columbia University Vagelos College of Physicians and Surgeons, New York, NY 10032, USA.
Emily PhungVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Anthony DiPiazzaVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Lauren A ChangVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Olubukola M AbionaVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Kizzmekia S CorbettVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Brandon J DeKoskyBioengineering Graduate Program, The University of Kansas, Lawrence, KS 66045, USA; Department of Pharmaceutical Chemistry, The University of Kansas, Lawrence, KS 66045, USA; Department of Chemical Engineering, The University of Kansas, Lawrence, KS 66045, USA.
Barney S GrahamVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
John R MascolaVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
John MisasiVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Tracy RuckwardtVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Nancy J SullivanVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Lawrence ShapiroVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA; Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA. Electronic address: lss8@columbia.edu.
Peter D KwongVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA; Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA. Electronic address: pdkwong@nih.gov.
National Institute of Allergy and Infectious Diseases · USNational Institutes of Health · USUniversity of Kansas · USColumbia University · USLeidos (United States) · US
Funding
ZWITTERION SURFACTANT DDMAB FOR IMPROV STABIL OF PROTEINP41RR001209 · NCRR · STANFORD UNIVERSITY · PI SCOTT, EMILY E · 1985 to 2011
$38.9MTRD #3: An automated and streamlined pipeline for in-situ molecular microscopyP41GM103310 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI KIEFT, JEFFREY S · 2012 to 2021
$14.7MComprehensive analysis of human adaptive immune receptors to elucidate correlates of Epstein-Barr virus disease suppressionDP5OD023118 · OD · UNIVERSITY OF KANSAS LAWRENCE · PI DEKOSKY, BRANDON JAMES · 2016 to 2022
$2.2MComprehensive molecular and functional analyses of anti-HIV-1 broadly neutralizing antibody repertoiresR21AI143407 · NIAID · UNIVERSITY OF KANSAS LAWRENCE · PI DEKOSKY, BRANDON JAMES, FORREST, MARCUS LAIRD · 2019 to 2020
$435kProbing antigen specificity and response of autoimmune B cells in Neuromyelitis OpticaR21AI144408 · NIAID · UNIVERSITY OF KANSAS LAWRENCE · PI DEKOSKY, BRANDON JAMES · 2019 to 2020
$417kNCRR NIH HHS P41 RR001209NIAID NIH HHS R21 AI143407NIAID NIH HHS R21 AI144408NIGMS NIH HHS P41 GM103310NIH HHS DP5 OD023118
Abstract
Biotin-labeled molecular probes, comprising specific regions of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike, would be helpful in the isolation and characterization of antibodies targeting this recently emerged pathogen. Here, we design constructs incorporating an N-terminal purification tag, a site-specific protease-cleavage site, the probe region of interest, and a C-terminal sequence targeted by biotin ligase. Probe regions include full-length spike ectodomain as well as various subregions, and we also design mutants that eliminate recognition of the angiotensin-converting enzyme 2 (ACE2) receptor. Yields of biotin-labeled probes from transient transfection range from ∼0.5 mg/L for the complete ectodomain to >5 mg/L for several subregions. Probes are characterized for antigenicity and ACE2 recognition, and the structure of the spike ectodomain probe is determined by cryoelectron microscopy. We also characterize antibody-binding specificities and cell-sorting capabilities of the biotinylated probes. Altogether, structure-based design coupled to efficient purification and biotinylation processes can thus enable streamlined development of SARS-CoV-2 spike ectodomain probes.
Indexed as
Angiotensin-Converting Enzyme 2Antibodies, NeutralizingAntibodies, ViralAntibody SpecificityBinding Sites, AntibodyBiotinylationCoronavirus InfectionsCOVID-19Cryoelectron MicroscopyHumansMolecular ProbesPandemicsPeptidyl-Dipeptidase APneumonia, ViralReceptors, VirusSpike Glycoprotein, CoronavirusACE2 protein, humanAngiotensin-Converting Enzyme 2Antibodies, NeutralizingAntibodies, ViralMolecular ProbesPeptidyl-Dipeptidase AReceptors, VirusSpike Glycoprotein, Coronavirusantibodybiotinylated probecoronavirus disease 2019COVID-19HRV3C proteasehuman rhinovirus 3Csingle-chain Fcstructure-based design
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