Parainfluenza virus 5 fusion protein maintains pre-fusion stability but not fusogenic activity following mutation of a transmembrane leucine/isoleucine domain

Jean Mawuena Branttie, Rebecca Ellis Dutch

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

Abstract

The paramyxoviruses Hendra virus (HeV) and parainfluenza virus 5 (PIV5) require the fusion (F) protein to efficiently infect cells. For fusion to occur, F undergoes dramatic, essentially irreversible conformational changes to merge the viral and cell membranes into a continuous bilayer. Recently, a transmembrane (TM) domain leucine/isoleucine (L/I) zipper was shown to be critical in maintaining the expression, stability and pre-fusion conformation of HeV F, allowing for fine-Tuned timing of membrane fusion. To analyse the effect of the TM domain L/I zipper in another paramyxovirus, we created alanine mutations to the TM domain of PIV5 F, a paramyxovirus model system. Our data show that while the PIV5 F TM L/I zipper does not significantly affect total expression and only modestly affects surface expression and pre-fusion stability, it is critical for fusogenic activity. These results suggest that the roles of TM L/I zipper motifs differ among members of the family Paramyxoviridae.

Original languageEnglish
Pages (from-to)467-472
Number of pages6
JournalJournal of General Virology
Volume101
Issue number5
DOIs
StatePublished - 2020

Bibliographical note

Funding Information:
This work was supported by NIAID grant R01AI051517 and NIH grant 2P20 RR02017 to R. E. D.

Publisher Copyright:
© 2020 Microbiology Society. All rights reserved.

Keywords

  • fusogenic activity
  • leucine/isoleucine zipper
  • pre-fusion stability
  • transmembrane domain.

ASJC Scopus subject areas

  • Virology

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