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  A lipid zipper triggers bacterial invasion

Eierhoff, T., Bastian, B., Thuenauer, R., Madl, J., Audfray, A., Aigal, S., et al. (2014). A lipid zipper triggers bacterial invasion. Proceedings of the National Academy of Sciences, USA, 12895-12900.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-002B-8847-6 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-002B-98B7-7
Genre: Journal Article

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 Creators:
Eierhoff, Thorsten, Author
Bastian, Björn, Author
Thuenauer, Roland, Author
Madl, Josef, Author
Audfray, Aymeric, Author
Aigal, Sahaja1, Author
Juillot, Samuel, Author
Rydell, Gustaf E., Author
Müller, Stefan, Author
de Bentzmann, Sophie, Author
Imberty, Anne, Author
Fleck, Christian, Author
Römer, Winfried, Author
Affiliations:
1Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society, 79108 Freiburg, DE, ou_2243640              

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Free keywords: membrane curvature; glycolipid; infection
 Abstract: Glycosphingolipids are important structural constituents of cellular membranes. They are involved in the formation of nanodomains ("lipid rafts"), which serve as important signaling platforms. Invasive bacterial pathogens exploit these signaling domains to trigger actin polymerization for the bending of the plasma membrane and the engulfment of the bacterium--a key process in bacterial uptake. However, it is unknown whether glycosphingolipids directly take part in the membrane invagination process. Here, we demonstrate that a "lipid zipper," which is formed by the interaction between the bacterial surface lectin LecA and its cellular receptor, the glycosphingolipid Gb3, triggers plasma membrane bending during host cell invasion of the bacterium Pseudomonas aeruginosa. In vitro experiments with Gb3-containing giant unilamellar vesicles revealed that LecA/Gb3-mediated lipid zippering was sufficient to achieve complete membrane engulfment of the bacterium. In addition, theoretical modeling elucidated that the adhesion energy of the LecA-Gb3 interaction is adequate to drive the engulfment process. In cellulo experiments demonstrated that inhibition of the LecA/Gb3 lipid zipper by either lecA knockout, Gb3 depletion, or application of soluble sugars that interfere with LecA binding to Gb3 significantly lowered P. aeruginosa uptake by host cells. Of note, membrane engulfment of P. aeruginosa occurred independently of actin polymerization, thus corroborating that lipid zippering alone is sufficient for this crucial first step of bacterial host-cell entry. Our study sheds new light on the impact of glycosphingolipids in the cellular invasion of bacterial pathogens and provides a mechanistic explication of the initial uptake processes.

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Language(s): eng - English
 Dates: 2014-09-02
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 701133
 Degree: -

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Title: Proceedings of the National Academy of Sciences, USA
  Alternative Title : PNAS
Source Genre: Journal
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Affiliations:
Publ. Info: -
Pages: - Volume / Issue: - Sequence Number: - Start / End Page: 12895 - 12900 Identifier: -