Staphylococcus aureus Lpl protein triggers human host cell invasion via activation of Hsp90 receptor

Paula M. Tribelli, Arif Luqman, Minh Thu Nguyen, Johannes Madlung, Sook Ha Fan, Boris Macek, Peter Sass, Katharina Bitschar, Birgit Schittek, Dorothee Kretschmer, Friedrich Götz*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

17 Citations (Scopus)

Abstract

Staphylococcus aureus is a facultative intracellular pathogen. Recently, it has been shown that the protein part of the lipoprotein-like lipoproteins (Lpls), encoded by the lpl cluster comprising of 10 lpls paralogue genes, increases pathogenicity, delays the G2/M phase transition, and also triggers host cell invasion. Here, we show that a recombinant Lpl1 protein without the lipid moiety binds directly to the isoforms of the human heat shock proteins Hsp90α and Hsp90ß. Synthetic peptides covering the Lpl1 sequence caused a twofold to fivefold increase of S. aureus invasion in HaCaT cells. Antibodies against Hsp90 decrease S. aureus invasion in HaCaT cells and in primary human keratinocytes. Additionally, inhibition of ATPase function of Hsp90 or silencing Hsp90α expression by siRNA also decreased the S. aureus invasion in HaCaT cells. Although the Hsp90ß is constitutively expressed, the Hsp90α isoform is heat-inducible and appears to play a major role in Lpl1 interaction. Pre-incubation of HaCaT cells at 39°C increased both the Hsp90α expression and S. aureus invasion. Lpl1-Hsp90 interaction induces F-actin formation, thus, triggering an endocytosis-like internalisation. Here, we uncovered a new host cell invasion principle on the basis of Lpl-Hsp90 interaction.

Original languageEnglish
Article numbere13111
JournalCellular Microbiology
Volume22
Issue number1
DOIs
Publication statusPublished - 1 Jan 2020

Keywords

  • F-actin
  • Hsp90 receptor
  • Lpl
  • Staphylococcus aureus
  • invasion

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