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TitleStudies in humanized mice and convalescent humans yield a SARS-CoV-2 antibody cocktail.
Journal, issue, pagesScience, Vol. 369, Issue 6506, Page 1010-1014, Year 2020
Publish dateAug 21, 2020
AuthorsJohanna Hansen / Alina Baum / Kristen E Pascal / Vincenzo Russo / Stephanie Giordano / Elzbieta Wloga / Benjamin O Fulton / Ying Yan / Katrina Koon / Krunal Patel / Kyung Min Chung / Aynur Hermann / Erica Ullman / Jonathan Cruz / Ashique Rafique / Tammy Huang / Jeanette Fairhurst / Christen Libertiny / Marine Malbec / Wen-Yi Lee / Richard Welsh / Glen Farr / Seth Pennington / Dipali Deshpande / Jemmie Cheng / Anke Watty / Pascal Bouffard / Robert Babb / Natasha Levenkova / Calvin Chen / Bojie Zhang / Annabel Romero Hernandez / Kei Saotome / Yi Zhou / Matthew Franklin / Sumathi Sivapalasingam / David Chien Lye / Stuart Weston / James Logue / Robert Haupt / Matthew Frieman / Gang Chen / William Olson / Andrew J Murphy / Neil Stahl / George D Yancopoulos / Christos A Kyratsous /
PubMed AbstractNeutralizing antibodies have become an important tool in treating infectious diseases. Recently, two separate approaches yielded successful antibody treatments for Ebola-one from genetically ...Neutralizing antibodies have become an important tool in treating infectious diseases. Recently, two separate approaches yielded successful antibody treatments for Ebola-one from genetically humanized mice and the other from a human survivor. Here, we describe parallel efforts using both humanized mice and convalescent patients to generate antibodies against the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike protein, which yielded a large collection of fully human antibodies that were characterized for binding, neutralization, and three-dimensional structure. On the basis of these criteria, we selected pairs of highly potent individual antibodies that simultaneously bind the receptor binding domain of the spike protein, thereby providing ideal partners for a therapeutic antibody cocktail that aims to decrease the potential for virus escape mutants that might arise in response to selective pressure from a single-antibody treatment.
External linksScience / PubMed:32540901 / PubMed Central
MethodsEM (single particle)
Resolution3.9 Å
Structure data

22137

6xdg

EMDB-22137, PDB-6xdg:
Complex of SARS-CoV-2 receptor binding domain with the Fab fragments of two neutralizing antibodies
Method: EM (single particle) / Resolution: 3.9 Å

Source
  • severe acute respiratory syndrome coronavirus 2
  • homo sapiens (human)
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / SARS-CoV-2 / therapeutic antibody / antiviral / VIRAL PROTEIN-IMMUNE SYSTEM complex

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