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Glycosidase and glycan polymorphism control hydrolytic release of immunogenic flagellin peptides
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 understoo...
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Published in: | Science (American Association for the Advancement of Science) 2019-04, Vol.364 (6436) |
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Main Authors: | , , , , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | 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 β-galactosidase 1 (BGAL1) of
promotes hydrolytic elicitor release and acts in immunity against pathogenic
strains only when they carry a terminal modified viosamine (mVio) in the flagellin
-glycan. In counter defense,
pathovars evade host immunity by using BGAL1-resistant
-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. |
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ISSN: | 0036-8075 1095-9203 |
DOI: | 10.1126/science.aav0748 |