Cyclic ADP ribose isomers: Production, chemical structures, and immune signaling-Reference-Cited by-同舟云学术

Cyclic ADP ribose isomers: Production, chemical structures, and immune signaling

Published:2022-09-30 Issue:6614 Volume:377 Page:
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Manik Mohammad K.¹²^ORCID,Shi Yun³^ORCID,Li Sulin¹²^ORCID,Zaydman Mark A.⁴^ORCID,Damaraju Neha⁵⁶,Eastman Samuel⁷^ORCID,Smith Thomas G.⁸^ORCID,Gu Weixi¹²^ORCID,Masic Veronika³,Mosaiab Tamim³^ORCID,Weagley James S.⁹^ORCID,Hancock Steven J.¹²,Vasquez Eduardo³^ORCID,Hartley-Tassell Lauren³^ORCID,Kargios Nestoras¹⁰^ORCID,Maruta Natsumi¹²^ORCID,Lim Bryan Y. J.¹²^ORCID,Burdett Hayden¹²^ORCID,Landsberg Michael J.¹²^ORCID,Schembri Mark A.¹²^ORCID,Prokes Ivan¹¹^ORCID,Song Lijiang¹¹^ORCID,Grant Murray¹⁰^ORCID,DiAntonio Aaron⁴⁵^ORCID,Nanson Jeffrey D.¹²^ORCID,Guo Ming¹²,Milbrandt Jeffrey⁴^ORCID,Ve Thomas³^ORCID,Kobe Bostjan¹²¹³^ORCID

Affiliation:

1. School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, QLD 4072, Australia.

2. Australian Infectious Diseases Research Centre, The University of Queensland, Brisbane, QLD 4072, Australia.

3. Institute for Glycomics, Griffith University, Southport, QLD 4222, Australia.

4. Department of Pathology and Immunology, Washington University School of Medicine in St. Louis, St. Louis, MO 63100, USA.

5. Department of Developmental Biology, Washington University School of Medicine in St. Louis, St. Louis, MO 63100, USA.

6. Department of Genetics, Washington University School of Medicine in St. Louis, St. Louis, MO 63100, USA.

7. Department of Plant Pathology, University of Nebraska–Lincoln, Lincoln, NE 68583, USA.

8. Department of Chemistry, University of Nebraska–Lincoln, Lincoln, NE 68588, USA.

9. Edison Family Center for Genome Sciences and Systems Biology, Washington University School of Medicine in St. Louis, St. Louis, MO 63110, USA.

10. School of Life Sciences, University of Warwick, Coventry CV4 7AL, UK.

11. Department of Chemistry, University of Warwick, Coventry CV4 7AL, UK.

12. Department of Agronomy and Horticulture, University of Nebraska–Lincoln, Lincoln, NE 68583, USA.

13. The University of Queensland, Institute for Molecular Bioscience, Brisbane, QLD 4072, Australia.

Abstract

Cyclic adenosine diphosphate (ADP)–ribose (cADPR) isomers are signaling molecules produced by bacterial and plant Toll/interleukin-1 receptor (TIR) domains via nicotinamide adenine dinucleotide (oxidized form) (NAD + ) hydrolysis. We show that v-cADPR (2′cADPR) and v2-cADPR (3′cADPR) isomers are cyclized by O-glycosidic bond formation between the ribose moieties in ADPR. Structures of 2′cADPR-producing TIR domains reveal conformational changes that lead to an active assembly that resembles those of Toll-like receptor adaptor TIR domains. Mutagenesis reveals a conserved tryptophan that is essential for cyclization. We show that 3′cADPR is an activator of ThsA effector proteins from the bacterial antiphage defense system termed Thoeris and a suppressor of plant immunity when produced by the effector HopAM1. Collectively, our results reveal the molecular basis of cADPR isomer production and establish 3′cADPR in bacteria as an antiviral and plant immunity–suppressing signaling molecule.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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