Serotypic evolution of measles virus is constrained by multiple co-dominant B cell epitopes on its surface glycoproteins

Miguel Ángel Muñoz-Alía, Rebecca A. Nace, Lianwen Zhang, Stephen J. Russell

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

After centuries of pestilence and decades of global vaccination, measles virus (MeV) genotypes capable of evading vaccine-induced immunity have not emerged. Here, by systematically building mutations into the hemagglutinin (H) glycoprotein of an attenuated measles virus strain and assaying for serum neutralization, we show that virus evolution is severely constrained by the existence of numerous co-dominant H glycoprotein antigenic sites, some critical for binding to the pathogenicity receptors SLAMF1 and nectin-4. We further demonstrate the existence in serum of protective neutralizing antibodies targeting co-dominant fusion (F) glycoprotein epitopes. Lack of a substantial reduction in serum neutralization of mutant measles viruses that retain even one of the co-dominant antigenic sites makes evolution of pathogenic measles viruses capable of escaping serum neutralization in vaccinated individuals extremely unlikely.

Original languageEnglish (US)
Article number100225
JournalCell Reports Medicine
Volume2
Issue number4
DOIs
StatePublished - Apr 20 2021

Keywords

  • antibody escape
  • antigenic evolution
  • measles virus fusion
  • measles virus hemagglutinin

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Medicine(all)

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