A highly membrane-active peptide in Flock House virus: implications for the mechanism of nodavirus infection
1999 | journal article; research paper. A publication with affiliation to the University of Göttingen.
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A highly membrane-active peptide in Flock House virus: implications for the mechanism of nodavirus infection
Bong, D. T.; Steinem, C. ; Janshoff, A. ; Johnson, J. S. & Ghadiri, M. R. (1999)
Chemistry & Biology, 6(7) pp. 473-481. DOI: https://doi.org/10.1016/S1074-5521(99)80065-9
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- Authors
- Bong, Dennis T.; Steinem, Claudia ; Janshoff, Andreas ; Johnson, John S.; Ghadiri, M. Reza
- Abstract
- Background: Nodaviruses are among the simplest animal viruses, and are therefore attractive systems for deconvoluting core viral processes such as assembly, infection and uncoating. Membrane translocation of the single-stranded RNA genome of nodaviruses has been proposed to be mediated by direct lipid-protein interactions between a past-assembly autocatalytic cleavage product from the capsomere and the target membrane. To probe the validity of this hypothesis, we have synthesized a 21-residue Met-->Nle (norleucine) variant of the amino-terminal helical domain (denoted here as gamma(1)) of the cleavage peptide in Flock House nodavirus (FHV) and studied its ability to alter membrane structure and function. Results: The synthetic peptide gamma(1) increases membrane permeability to hydrophilic solutes, as judged by fluorescence experiments with liposome-encapsulated dyes and ion-conductance measurements. Furthermore, peptide orientation and location within lipid bilayers was determined using tryptophan-fluorescence-quenching experiments and attenuated total reflectance infrared spectroscopy. Conclusions: The helical domain of the FHV cleavage product partitions spontaneously into lipid bilayers and increases membrane permeability, consistent with the postulated mechanism for viral genome translocation. The existence of a membrane-binding domain in the FHV cleavage sequence suggests peptide-triggered disruption of the endosomal membrane as a prelude to viral uncoating in the host cytoplasm, A model for this interaction is proposed.
- Issue Date
- 1999
- Journal
- Chemistry & Biology
- ISSN
- 1074-5521
- Language
- English