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  Bacterial lectin BambL acts as a B cell superantigen

Frensch, M., Jäger, C., Müller, P. F., Tadić, A., Wilhelm, I., Wehrum, S., et al. (2021). Bacterial lectin BambL acts as a B cell superantigen. Cellular and Molecular Life Sciences, 78, 8165-8186. doi:10.1007/s00018-021-04009-z.

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Item Permalink: https://hdl.handle.net/21.11116/0000-000D-BD8B-2 Version Permalink: https://hdl.handle.net/21.11116/0000-000D-BD8C-1
Genre: Journal Article

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 Creators:
Frensch, Marco1, Author
Jäger, Christina2, Author
Müller, Peter F2, Author
Tadić, Annamaria2, Author
Wilhelm, Isabel2, Author
Wehrum, Sarah2, Author
Diedrich, Britta2, Author
Fischer, Beate2, Author
Meléndez, Ana Valeria2, Author
Dengjel, Joern2, Author
Eibel, Hermann2, Author
Römer, Winfried1, Author
Affiliations:
1IMPRS-MCB, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society, ou_persistent22              
2External Organizations, ou_persistent22              

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Free keywords: Adaptive immunity; Apoptosis; Bacterial pathogens; Immunoglobulin glycosylation; Multivalent lectins; β-Propeller lectins.
 Abstract: B cell superantigens crosslink conserved domains of B cell receptors (BCRs) and cause dysregulated, polyclonal B cell activation irrespective of normal BCR-antigen complementarity. The cells typically succumb to activation-induced cell death, which can impede the adaptive immune response and favor infection. In the present study, we demonstrate that the fucose-binding lectin of Burkholderia ambifaria, BambL, bears functional resemblance to B cell superantigens. By engaging surface glycans, the bacterial lectin activated human peripheral blood B cells, which manifested in the surface expression of CD69, CD54 and CD86 but became increasingly cytotoxic at higher concentrations. The effects were sensitive to BCR pathway inhibitors and excess fucose, which corroborates a glycan-driven mode of action. Interactome analyses in a model cell line suggest BambL binds directly to glycans of the BCR and regulatory coreceptors. In vitro, BambL triggered BCR signaling and induced CD19 internalization and degradation. Owing to the lectin's six binding sites, we propose a BCR activation model in which BambL functions as a clustering hub for receptor glycans, modulates normal BCR regulation, and induces cell death through exhaustive activation.

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Language(s): eng - English
 Dates: 2021-11-03
 Publication Status: Published online
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1007/s00018-021-04009-z
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Title: Cellular and Molecular Life Sciences
  Abbreviation : Cell. Mol. Life Sci.
Source Genre: Journal
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Publ. Info: Springer (Birkhäuser Verlag)
Pages: - Volume / Issue: 78 Sequence Number: - Start / End Page: 8165 - 8186 Identifier: Other: 1420-9071
ISSN: 1420-682X
CoNE: https://pure.mpg.de/cone/journals/resource/954926942730