Glycosidase and glycan polymorphism control hydrolytic release of immunogenic flagellin peptides

Buscaill, Pierre, Chandrasekar, Balakumaran, Sanguankiattichai, Nattapong, Kourelis, Jiorgos ORCID: https://orcid.org/0000-0002-9007-1333, Kaschani, Farnusch, Thomas, Emma L., Morimoto, Kyoko, Kaiser, Markus, Preston, Gail M., Ichinose, Yuki and van der Hoorn, Renier A. L. (2019) Glycosidase and glycan polymorphism control hydrolytic release of immunogenic flagellin peptides. Science, 364 (6436). ISSN 0036-8075

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Abstract

Plants and animals recognize conserved flagellin fragments as a signature of bacterial invasion. These immunogenic elicitor peptides are embedded in the flagellin polymer and require hydrolytic release before they can activate cell surface receptors. Although much of flagellin signaling is understood, little is known about the release of immunogenic fragments. We discovered that plant-secreted b-galactosidase 1 (BGAL1) of Nicotiana benthamiana promotes hydrolytic elicitor release and acts in immunity against pathogenic Pseudomonas syringae strains only when they carry a terminal modified viosamine (mVio) in the flagellin O-glycan. In counter defense, P. syringae pathovars evade host immunity by using BGAL1-resistant O-glycans or by producing a BGAL1 inhibitor. Polymorphic glycans on flagella are common to plant and animal pathogenic bacteria and represent an important determinant of host immunity to bacterial pathogens.

Item Type: Article
Additional Information: Funding Information: We thank M. Joosten and A. Gust for providing seeds of Arabidopsis mutants; H. Overkleeft for providing glycosidase probes; I. Somssich for providing flg22; C. Zipfel for helpful strategic suggestions and providing fls2c seeds; A. Collmer for providing PtoDC3000 mutants; U. Pyzio for plant care; J. Baker for photography; J. Jones, S. Kamoun, and S. Marillonnet for providing plasmids via AddGene; and R. Tóth and D. Sueldo for critically reading the manuscript. This work was supported by ERC Consolidator grant 616449 “GreenProteases” (to P.B., K.M., R.A.L.v.d.H.), BBSRC grant BB/R017913/1 (to P.B., R.A.L.v.d.H.), a Royal Thai Government Scholarship (to N.S.), the Clarendon Foundation (to J.K.), and the Oxford Interdisciplinary Bioscience DTP (BB/M011224/1 to N.S., E.L.T., G.M.P.). Publisher Copyright: © 2019 American Association for the Advancement of Science. All rights reserved.
Uncontrolled Keywords: general ,/dk/atira/pure/subjectarea/asjc/1000
Faculty \ School: Faculty of Science > The Sainsbury Laboratory
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Depositing User: LivePure Connector
Date Deposited: 07 Dec 2023 01:46
Last Modified: 01 Feb 2024 03:08
URI: https://ueaeprints.uea.ac.uk/id/eprint/93899
DOI: 10.1126/science.aav0748

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