The Pseudomonas aeruginosa Lectin LecB Causes Integrin Internalization and Inhibits Epithelial Wound Healing.

MBio
R. ThuenauerWinfried Römer

Abstract

The opportunistic bacterium Pseudomonas aeruginosa produces the fucose-specific lectin LecB, which has been identified as a virulence factor. LecB has a tetrameric structure with four opposing binding sites and has been shown to act as a cross-linker. Here, we demonstrate that LecB strongly binds to the glycosylated moieties of β1-integrins on the basolateral plasma membrane of epithelial cells and causes rapid integrin endocytosis. Whereas internalized integrins were degraded via a lysosomal pathway, washout of LecB restored integrin cell surface localization, thus indicating a specific and direct action of LecB on integrins to bring about their endocytosis. Interestingly, LecB was able to trigger uptake of active and inactive β1-integrins and also of complete α3β1-integrin-laminin complexes. We provide a mechanistic explanation for this unique endocytic process by showing that LecB has the additional ability to recognize fucose-bearing glycosphingolipids and causes the formation of membrane invaginations on giant unilamellar vesicles. In cells, LecB recruited integrins to these invaginations by cross-linking integrins and glycosphingolipids. In epithelial wound healing assays, LecB specifically cleared integrins from the surf...Continue Reading

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Citations

Jan 26, 2021·Current Opinion in Infectious Diseases·Nikolaos SpernovasilisGaryfallia Poulakou
Jul 3, 2021·Biomolecules·Patrycja BurzyńskaEwa Jaśkiewicz
Jun 29, 2021·Virulence·Charles D MorinGee W Lau
Aug 21, 2021·Future Microbiology·Anjali WarrierThokur Sreepathy Murali
Aug 15, 2021·Glycoconjugate Journal·Fulvio ReggioriEeva-Liisa Eskelinen
Nov 4, 2021·Cellular and Molecular Life Sciences : CMLS·Marco FrenschWinfried Römer

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Methods Mentioned

BETA
glycosylation
immunoprecipitation
pull down
confocal microscopy
myristoylation
PCR
electrophoresis
acetylation

Software Mentioned

GraphPad Prism

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