Journal of advanced research · 2026
Psyllid glycine-rich antimicrobial peptides oligomerize to directly cleave zinc transporter ZnuA on the membranes of citrus Huanglongbing pathogen.
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Peng Hongyan, Bin Yu, Li You, Du Yu, Wang Chuang, Wang Shuai, Wei Taiyun
Аннотация
INTRODUCTION: Huanglongbing (HLB), the most devastating citrus disease worldwide, is caused by Candidatus Liberibacter asiaticus (CLas) and transmitted by Asian citrus psyllid, Diaphorina citri. Currently, the potential role of the insect vector's innate immunity against CLas remains poorly understood.
OBJECTIVES: This study aimed to identify and characterize a 41-amino acid glycine-rich antimicrobial peptide from D. citri (DcGrAMP1), elucidate its molecular mechanism against CLas and related α-proteobacteria, and evaluate its efficacy in suppressing CLas in HLB-affected citrus under greenhouse and field conditions.
METHODS: Through genomic screening and CLas-induced expression validation, we obtained DcGrAMP1; combined with structural prediction, site-directed mutagenesis, molecular interaction techniques, and RNA interference, we elucidated its mechanism against CLas and regulatory pathway; through transgenic citrus construction and protein injection assays, we validated its CLas-suppressive efficacy under greenhouse and field conditions.
RESULTS: DcGrAMP1 exhibits remarkable thermal stability. It oligomerizes through Arg26/Arg31 for bacterial membrane penetration, and Arg21 engages in binding-associated cleavage upon interacting with Asp153 of zinc transporter ZnuA on CLas membranes, thereby cleaving the adjacent peptide bond and triggering ZnuA degradation. CLas infection activates the c-Jun N-terminal kinase-activator protein 1 (JNK-AP1) signaling pathway in the psyllid, thereby upregulating DcGrAMP1 expression. Overexpression or injection of DcGrAMP1 in citrus significantly reduced CLas titers and alleviated HLB symptoms.
CONCLUSION: This work provides the evidence that insect AMPs can oligomerize to penetrate CLas membranes, and then directly cleave zinc transporter ZnuA on the membranes of citrus Huanglongbing pathogen.
OBJECTIVES: This study aimed to identify and characterize a 41-amino acid glycine-rich antimicrobial peptide from D. citri (DcGrAMP1), elucidate its molecular mechanism against CLas and related α-proteobacteria, and evaluate its efficacy in suppressing CLas in HLB-affected citrus under greenhouse and field conditions.
METHODS: Through genomic screening and CLas-induced expression validation, we obtained DcGrAMP1; combined with structural prediction, site-directed mutagenesis, molecular interaction techniques, and RNA interference, we elucidated its mechanism against CLas and regulatory pathway; through transgenic citrus construction and protein injection assays, we validated its CLas-suppressive efficacy under greenhouse and field conditions.
RESULTS: DcGrAMP1 exhibits remarkable thermal stability. It oligomerizes through Arg26/Arg31 for bacterial membrane penetration, and Arg21 engages in binding-associated cleavage upon interacting with Asp153 of zinc transporter ZnuA on CLas membranes, thereby cleaving the adjacent peptide bond and triggering ZnuA degradation. CLas infection activates the c-Jun N-terminal kinase-activator protein 1 (JNK-AP1) signaling pathway in the psyllid, thereby upregulating DcGrAMP1 expression. Overexpression or injection of DcGrAMP1 in citrus significantly reduced CLas titers and alleviated HLB symptoms.
CONCLUSION: This work provides the evidence that insect AMPs can oligomerize to penetrate CLas membranes, and then directly cleave zinc transporter ZnuA on the membranes of citrus Huanglongbing pathogen.