Differential features of fusion activation within the paramyxoviridae

Kristopher D. Azarm, Benhur Lee

Research output: Contribution to journalReview articlepeer-review

22 Scopus citations

Abstract

Paramyxovirus (PMV) entry requires the coordinated action of two envelope glycoproteins, the receptor binding protein (RBP) and fusion protein (F). The sequence of events that occurs during the PMV entry process is tightly regulated. This regulation ensures entry will only initiate when the virion is in the vicinity of a target cell membrane. Here, we review recent structural and mechanistic studies to delineate the entry features that are shared and distinct amongst the Paramyxoviridae. In general, we observe overarching distinctions between the proteinusing RBPs and the sialic acid? (SA?) using RBPs, including how their stalk domains differentially trigger F. Moreover, through sequence comparisons, we identify greater structural and functional conservation amongst the PMV fusion proteins, as compared to the RBPs. When examining the relative contributions to sequence conservation of the globular head versus stalk domains of the RBP, we observe that, for the protein?using PMVs, the stalk domains exhibit higher conservation and find the opposite trend is true for SA?using PMVs. A better understanding of conserved and distinct features that govern the entry of protein?using versus SA?using PMVs will inform the rational design of broader spectrum therapeutics that impede this process.

Original languageEnglish
Article numberv12020161
JournalViruses
Volume12
Issue number2
DOIs
StatePublished - 2020

Keywords

  • Henipavirus
  • Parainfluenza virus
  • Paramyxovirus
  • Rubulavirus
  • Structure
  • Type I fusion protein
  • Viral envelope proteins
  • Viral transmission
  • Virus entry

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