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Review
. 2025 Aug 26;14(17):2667.
doi: 10.3390/plants14172667.

Biotechnological Advances in Sanguinarine and Chelerythrine Production from Plume Poppy (Macleaya cordata): A Gene Editing Perspective

Bilal A Rather  1   2 , Wujun Xu  1   2 , Aadil Yousuf Tantray  3 , Moksh Mahajan  4 , Huapeng Sun  2 , Hanqing Cong  2 , Xuefei Jiang  1 , M Iqbal R Khan  4   5 , Fei Qiao  2
Affiliations
Review

Biotechnological Advances in Sanguinarine and Chelerythrine Production from Plume Poppy (Macleaya cordata): A Gene Editing Perspective

Bilal A Rather et al. Plants (Basel). .

Abstract

Plume poppy (Macleaya cordata), an important member of the Papaveraceae family, is a substantial source of benzylisoquinoline alkaloids (BIAs) such as sanguinarine and chelerythrine. These compounds possess significant therapeutic potential, including anti-inflammatory, anticancer, and antimicrobial activities, along with various industrial applications. However, the yield of these compounds in native plants are minimal and highly variable due to certain ecological factors. Recent advances in transgenic technologies have opened a new avenue for enhancing the biosynthesis of BIAs and optimizing their delivery in plume poppy. This review consolidates recent strategies in gene editing and metabolic modulations aimed at improving alkaloid biosynthesis in plume poppy. It uniquely connects these tools with industrial and therapeutic demands, offering a roadmap for enhanced BIA production. The current review also provides new insights into the overcoming the current limitations, offering potential solutions for stable, high-yield production of BIAs in plume poppy for their therapeutic use.

Keywords: CRISPR/Cas9; chelerythrine; plume poppy; sanguinarine.

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Conflict of interest statement

The authors declare no conflicts of interest.

Figures

Figure 1
Figure 1
(A) Basal rosette of Macleaya cordata (plume poppy) during the vegetative stage. (B) Wild plant showing its aerial parts. Adapted from Lei et al. [10].
Figure 2
Figure 2
The biosynthetic pathway of sanguinarine and chelerythrine in M. cordata (3OHase: tyrosine 3-monooxygenase, 4HPPDC: 4-hydroxyphenylpyruvate decarboxylase, 4OMT: 3′-hydroxy-N-methylcoclaurine 4-O-methyltransferase, 6OMT: 6-O-methyltransferase, BBE: reticuline oxidase, berberine bridge enzyme; CNMT: coclaurine N-methyltransferase, DBOX: dihydrobenzophenanthridine oxidase, MSH: (S)-cis-N-methylstylopine 14-hydroxylase, NCS: norcoclaurine synthase, NMCH: N-methylcoclaurine hydroxylase, P6H: protopine 6-hydroxylase, SPS: stylopine synthase, TDC: (S)-canadine synthase, TNMT: tetrahydroprotoberberine-cis-N-methyltransferase, TYDC: tyrosine decarboxylase, TyrAt: tyrosine aminotransferase).
Figure 3
Figure 3
Mechanistic illustration showing potential approaches for improved sanguinarine and chelerythrine production in M. cordata (6OMT: 6-O-methyltransferase, BBE: reticuline oxidase, berberine bridge enzyme; CFS: cheilanthifoline synthase, DBOX: dihydrobenzophenanthridine oxidase, NCS: norcoclaurine synthase, NMCH: N-methylcoclaurine hydroxylase, P6H: protopine 6-hydroxylase, SMT: (S)-scoulerine 9-O-methyltransferase).
See this image and copyright information in PMC

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