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The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.

High-affinity salicylic acid-binding protein 2 is required for plant innate immunity and has salicylic acid-stimulated lipase activity

Open access
Kumar, Dhirendra, Klessig, Daniel F.·2003·Proceedings of the National Academy of Sciences

Abstract

Salicylic acid (SA) is a critical hormone for signaling innate immunity in plants. Here we present the purification and characterization of SA-binding protein 2 (SABP2), a tobacco protein that is present in low abundance and specifically binds SA with high affinity. Sequence analysis predicted that SABP2 is a lipase belonging to the α/β fold hydrolase super family. Confirming this prediction, recombinant SABP2 exhibited lipase activity against several synthetic substrates. Moreover, this lipase activity was stimulated by SA binding and may generate a lipid-derived signal. Silencing of SABP2 expression suppressed local resistance to tobacco mosaic virus, induction of pathogenesis-related 1 ( PR-1 ) gene expression by SA, and development of systemic acquired resistance. Together, these results suggest that SABP2 is an SA receptor that is required for the plant immune response. We further propose that SABP2 belongs to a large class of ligand-stimulated hydrolases involved in stress hormone-mediated signal transduction.

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Metadata

Authors
Kumar, D., & Klessig, D. F.
Venue
Proceedings of the National Academy of Sciences
Published
2003-12-12
Volume
100
Issue
26
Pages
16101-16106
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2039656448
Cited by
320
References
41
FWCI
20.65
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: High-affinity salicylic acid-binding protein 2 is required for plant innate immunity and has salicylic acid-stimulated lipase activity. https://app.cochat.ai/papers/10.1073/pnas.0307162100
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Kumar, D., & Klessig, D. F. (2003). High-affinity salicylic acid-binding protein 2 is required for plant innate immunity and has salicylic acid-stimulated lipase activity. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0307162100

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