Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 101, Issue 25, Pages 9217-9222Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0403339101
Keywords
membrane fusion; fusion activation; paramyxoviruses; class 1 fusion protein
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Funding
- NIAID NIH HHS [R01 AI023173, AI-23173] Funding Source: Medline
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Many viruses have evolved fusion-mediating glycoproteins that couple the energy released from irreversible protein refolding to the work of membrane fusion. The viral fusion proteins require a triggering event to undergo a cascade of tightly regulated conformational changes. Different isolates of the paramyxovirus SV5 fusion (F) protein have either a short (20-residue) or long (42-residue) cytoplasmic tail (CT), and a long CT suppresses fusion activity in a sequence-specific manner. Addition of a domain to the F protein CT, which has the propensity to form a three-helix bundle, stabilizes the F protein and increases the energy required for fusion activation. Quantitative cell-cell fusion assays and measurement of ectodomain conformation by monoclonal antibody reactivity indicate that this suppression of fusion by the long CT or addition of a three-helix bundle occurs at a step preceding initial membrane merger. The data suggest that F protein activation involves CT signaling to the ectodomain.
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