Rxivist logo

Complete mapping of viral escape from neutralizing antibodies

By Michael B. Doud, Scott E. Hensley, Jesse Bloom

Posted 09 Nov 2016
bioRxiv DOI: 10.1101/086611 (published DOI: 10.1371/journal.ppat.1006271)

Identifying viral mutations that confer escape from antibodies is crucial for understanding the interplay between immunity and viral evolution. Here we quantify how every amino-acid mutation to influenza hemagglutinin affects neutralization by monoclonal antibodies targeting several antigenic regions. Our approach involves creating all replication-competent protein variants of the virus, selecting these variants with antibody, and using deep sequencing to identify enriched mutations. These high-throughput measurements are predictive of the effects of individual mutations in traditional neutralization assays. At many residues, only some of the possible mutations escape from an antibody. For instance, at a single residue targeted by two different antibodies, we identify some mutations that escape both antibodies and other mutations that escape only one or the other. Therefore, our approach maps how viruses can escape antibodies with mutation-level sensitivity, and shows that only some mutations at antigenic residues actually alter antigenicity.

Download data

  • Downloaded 697 times
  • Download rankings, all-time:
    • Site-wide: 32,511
    • In microbiology: 1,915
  • Year to date:
    • Site-wide: None
  • Since beginning of last month:
    • Site-wide: None

Altmetric data


Downloads over time

Distribution of downloads per paper, site-wide


PanLingua

Sign up for the Rxivist weekly newsletter! (Click here for more details.)


News