Inhibition by cellular vacuolar atpase impairs human papillomavirus uncoating and infection

Konstantin H. MÜller, Gilles A. Spoden, Konstanze D. Scheffer, Regina Brunnhöfer, Jef K. De Brabander, Martin E. Maier, Luise Florin*, Claude P. Muller

*Corresponding author for this work

Research output: Contribution to journalArticleResearchpeer-review

25 Citations (Scopus)

Abstract

Several viruses, including human papillomaviruses, depend on endosomal acidification for successful infection. Hence, the multisubunit enzyme vacuolar ATPase (V-ATPase), which is mainly responsible for endosome acidification in the cell, represents an attractive target for antiviral strategies. In the present study, we show that V-ATPase is required for human papillomavirus (HPV) infection and that uncoating/disassembly but not endocytosis is affected by V-ATPase inhibition. The infection inhibitory potencies of saliphenylhalamide, a proven V-ATPase inhibitor, and its derivatives, as well as those of other V-ATPase inhibitors, were analyzed on different HPV types in relevant cell lines. Variation in the selectivity indices among V-ATPase inhibitors was high, while variation for the same inhibitor against different HPV subtypes was low, indicating that broad-spectrum anti-HPV activity can be provided.

Original languageEnglish
Pages (from-to)2905-2911
Number of pages7
JournalAntimicrobial Agents and Chemotherapy
Volume58
Issue number5
DOIs
Publication statusPublished - May 2014

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