Journal
JOURNAL OF VIROLOGY
Volume 80, Issue 15, Pages 7775-7780Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.00642-06
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Funding
- NIAID NIH HHS [AI 059355, U54 AI065357, U54 AI 065357, U54 AI065357-01, R21 AI059355] Funding Source: Medline
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The envelope glycoprotein of the arenaviruses (GP-C) is unusual in that the mature complex retains the cleaved, 58-amino-acid signal peptide. Association of this stable signal peptide (SSP) has been shown to be essential for intracellular trafficking and proteolytic maturation of the GP-C complex. We identify here a specific and previously unrecognized role of SSP in pH-dependent membrane fusion. Amino acid substitutions that alter the positive charge at lysine K33 in SSP affect the ability of GP-C to mediate cell-cell fusion and the threshold pH at which membrane fusion is triggered. Based on the presumed location of K33 at or near the luminal domain of SSP, we postulate that SSP interacts with the membrane-proximal or transmembrane regions of the G2 fusion protein. This unique organization of the GP-C complex may suggest novel strategies for intervention in arenavirus infection.
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