Human metapneumovirus fusion protein triggering: Increasing complexities by analysis of new HMPV fusion proteins

J. Tyler Kinder, Edita M. Klimyte, Andres Chang, John V. Williams, Rebecca Ellis Dutch

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

The human metapneumovirus (HMPV) fusion protein (F) mediates fusion of the viral envelope and cellular membranes to establish infection. HMPV F from some, but not all, viral strains promotes fusion only after exposure to low pH. Previous studies have identified several key residues involved in low pH triggering, including H435 and a proposed requirement for glycine at position 294. We analyzed the different levels of fusion activity, protein expression and cleavage of three HMPV F proteins not previously examined. Interestingly, low pH-triggered fusion in the absence of G294 was identified in one F protein, while a novel histidine residue (H434) was identified that enhanced low pH promoted fusion in another. The third F protein failed to promote cell-to-cell fusion, suggesting other requirements for F protein triggering. Our results demonstrate HMPV F triggering is more complex than previously described and suggest a more intricate mechanism for fusion protein function and activation.

Original languageEnglish
Pages (from-to)248-254
Number of pages7
JournalVirology
Volume531
DOIs
StatePublished - May 2019

Bibliographical note

Publisher Copyright:
© 2019 Elsevier Inc.

Keywords

  • Clade
  • Fusion
  • HMPV
  • Human metapneumovirus
  • Low pH
  • Strains
  • Syncytia

ASJC Scopus subject areas

  • Virology

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