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.
| Original language | English |
|---|---|
| Article number | eaav0748 |
| Journal | Science |
| Volume | 364 |
| Issue number | 6436 |
| DOIs | |
| Publication status | Published - Apr 12 2019 |
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Glycosidase and glycan polymorphism control hydrolytic release of immunogenic flagellin peptides. / Buscaill, Pierre; Chandrasekar, Balakumaran; Sanguankiattichai, Nattapong; Kourelis, Jiorgos; Kaschani, Farnusch; Thomas, Emma L.; Morimoto, Kyoko; Kaiser, Markus; Preston, Gail M.; Ichinose, Yuki; Van Der Hoorn, Renier A.L.
In: Science, Vol. 364, No. 6436, eaav0748, 12.04.2019.Research output: Contribution to journal › Article
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TY - JOUR
T1 - Glycosidase and glycan polymorphism control hydrolytic release of immunogenic flagellin peptides
AU - Buscaill, Pierre
AU - Chandrasekar, Balakumaran
AU - Sanguankiattichai, Nattapong
AU - Kourelis, Jiorgos
AU - Kaschani, Farnusch
AU - Thomas, Emma L.
AU - Morimoto, Kyoko
AU - Kaiser, Markus
AU - Preston, Gail M.
AU - Ichinose, Yuki
AU - Van Der Hoorn, Renier A.L.
PY - 2019/4/12
Y1 - 2019/4/12
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85064691008&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85064691008&partnerID=8YFLogxK
U2 - 10.1126/science.aav0748
DO - 10.1126/science.aav0748
M3 - Article
VL - 364
JO - Science
JF - Science
SN - 0036-8075
IS - 6436
M1 - eaav0748
ER -