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A secreted citrus protease cleaves an outer membrane protein of the Huanglongbing pathogen

Abstract:
Plants secrete a variety of proteases as a defense response during infection by microbial pathogens. However, the relationship between their catalytic activities and antimicrobial functions remains largely unknown. Particularly, few biologically relevant substrates of these proteases have been identified. Huanglongbing (HLB) has been a major threat to the citrus industry worldwide. The HLB-associated bacterium, “Candidatus Liberibacter asiaticus” (Las), was previously shown to deploy an inhibitor of papain-like cysteine proteases (PLCPs) to promote disease in citrus. In this study, we identified an outer membrane protein (OMP) of Las, LasOMP1, as a substrate of the citrus PLCP CsRD21a. LasOMP1 is one of the most highly expressed genes in Las. CsRD21a cleaves LasOMP1 and produces cleaved peptide products, which could be detected in vitro and in HLB-diseased citrus plants. We found that CsRD21a targets the N-terminal portion of LasOMP1, potentially at an extracellular loop region. Importantly, transgenic sweet orange overexpressing CsRD21a showed reduced Las populations and improved plant growth, highlighting that engineering this protease is a promising strategy to enhance HLB resistance in citrus. Together, our work reveals a pathogen-derived substrate of plant PLCPs and suggests bacterial OMPs may be direct targets of plant defense.
Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1073/pnas.2528641123

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Role:
Author
ORCID:
0000-0003-1908-2643
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Role:
Author
ORCID:
0000-0003-3890-8973


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Funder identifier:
10.13039/501100001809
Grant:
32525008
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Funder identifier:
10.13039/501100000324
Grant:
WMA
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Funder identifier:
10.13039/100007565
Grant:
FLA-CRC-005979
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Funder identifier:
10.13039/100005825
Grant:
2020-70029-33197


Publisher:
National Academy of Sciences
Journal:
Proceedings of the National Academy of Sciences More from this journal
Volume:
123
Issue:
15
Article number:
e2528641123
Publication date:
2026-04-07
Acceptance date:
2026-03-03
DOI:
EISSN:
1091-6490
ISSN:
0027-8424


Language:
English
Keywords:
Pubs id:
2403398
Local pid:
pubs:2403398
Source identifiers:
3925394
Deposit date:
2026-04-07
ARK identifier:
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