High Potency of a Bivalent Human VH Domain in SARS-CoV-2 Animal Models

  • Wei Li
  • , Alexandra Schäfer
  • , Swarali S. Kulkarni
  • , Xianglei Liu
  • , David R. Martinez
  • , Chuan Chen
  • , Zehua Sun
  • , Sarah R. Leist
  • , Aleksandra Drelich
  • , Liyong Zhang
  • , Marcin L. Ura
  • , Alison Berezuk
  • , Sagar Chittori
  • , Karoline Leopold
  • , Dhiraj Mannar
  • , Shanti S. Srivastava
  • , Xing Zhu
  • , Eric C. Peterson
  • , Chien Te Tseng
  • , John W. Mellors
  • Darryl Falzarano, Sriram Subramaniam, Ralph S. Baric, Dimiter S. Dimitrov

Research output: Contribution to journalArticlepeer-review

Abstract

A high-affinity human antibody domain, VH ab8, specific for SARS-CoV-2, bound to all three S protomers competing with ACE2. The relatively small size and bivalency of VH-Fc ab8 contributed to its high potency in two animal models of infection.

Original languageEnglish (US)
Pages (from-to)429-441.e16
JournalCell
Volume183
Issue number2
DOIs
StatePublished - Oct 15 2020

Keywords

  • SARS-CoV-2
  • electron microscopy
  • human V antibody domain
  • mouse and hamster models
  • virus neutralization

ASJC Scopus subject areas

  • General Biochemistry, Genetics and Molecular Biology

Fingerprint

Dive into the research topics of 'High Potency of a Bivalent Human VH Domain in SARS-CoV-2 Animal Models'. Together they form a unique fingerprint.

Cite this