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  Impact of glycan linkage to staphylococcus aureus wall teichoic acid on langerin recognition and Langerhans cell activation

Hendriks, A., van Dalen, R., Ali, S., Gerlach, D., van der Marel, G. A., Fuchsberger, F. F., et al. (2021). Impact of glycan linkage to staphylococcus aureus wall teichoic acid on langerin recognition and Langerhans cell activation. ACS Infectious Diseases, 7(3), 624-635. doi:10.1021/acsinfecdis.0c00822.

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 Creators:
Hendriks, Astrid, Author
van Dalen, Rob, Author
Ali, Sara, Author
Gerlach, David, Author
van der Marel, Gijsbert A., Author
Fuchsberger, Felix F.1, Author           
Aerts, Piet C., Author
de Haas, Carla J.C., Author
Peschel, Andreas, Author
Rademacher, Christoph1, Author           
van Strijp, Jos A.G., Author
Codée, Jeroen D.C., Author
van Sorge, Nina M., Author
Affiliations:
1Christoph Rademacher, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863300              

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Free keywords: Immunology; Peptides and proteins; Bacteria; Genetics; Biopolymers
 Abstract: Staphylococcus aureus is the leading cause of skin and soft tissue infections. It remains incompletely understood how skin-resident immune cells respond to invading S. aureus and contribute to an effective immune response. Langerhans cells (LCs), the only professional antigen-presenting cell type in the epidermis, sense S. aureus through their pattern-recognition receptor langerin, triggering a proinflammatory response. Langerin recognizes the β-1,4-linked N-acetylglucosamine (β1,4-GlcNAc) but not α-1,4-linked GlcNAc (α1,4-GlcNAc) modifications, which are added by dedicated glycosyltransferases TarS and TarM, respectively, on the cell wall glycopolymer wall teichoic acid (WTA). Recently, an alternative WTA glycosyltransferase, TarP, was identified, which also modifies WTA with β-GlcNAc but at the C-3 position (β1,3-GlcNAc) of the WTA ribitol phosphate (RboP) subunit. Here, we aimed to unravel the impact of β-GlcNAc linkage position for langerin binding and LC activation. Using genetically modified S. aureus strains, we observed that langerin similarly recognized bacteria that produce either TarS- or TarP-modified WTA, yet tarP-expressing S. aureus induced increased cytokine production and maturation of in vitro-generated LCs compared to tarS-expressing S. aureus. Chemically synthesized WTA molecules, representative of the different S. aureus WTA glycosylation patterns, were used to identify langerin-WTA binding requirements. We established that β-GlcNAc is sufficient to confer langerin binding, thereby presenting synthetic WTA molecules as a novel glycobiology tool for structure-binding studies and for elucidating S. aureus molecular pathogenesis. Overall, our data suggest that LCs are able to sense all β-GlcNAc-WTA producing S. aureus strains, likely performing an important role as first responders upon S. aureus skin invasion.

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Language(s): eng - English
 Dates: 2021-02-162021
 Publication Status: Issued
 Pages: -
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 Table of Contents: -
 Rev. Type: -
 Identifiers: DOI: 10.1021/acsinfecdis.0c00822
BibTex Citekey: doi:10.1021/acsinfecdis.0c00822
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Title: ACS Infectious Diseases
Source Genre: Journal
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Publ. Info: Washington, D. C. : ACS
Pages: - Volume / Issue: 7 (3) Sequence Number: - Start / End Page: 624 - 635 Identifier: ISSN: 2373-8227