ArticleMolecules (Basel, Switzerland)2014
Functional properties of a cysteine proteinase from pineapple fruit with improved resistance to fungal pathogens in Arabidopsis thaliana.
Article in Molecules (Basel, Switzerland), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 26 citations in OpenAlex.
- Antifungal Effect of the Proteolytic Fraction P1G10 Stabilized by Alginate-Chitosan Polyelectrolyte Complexation AgainstFoods (Basel, Switzerland) · 2026Article
- Genome-Wide Analysis of theBiology · 2025Article
- Identification and characterization of HVA22 genes in pineapple (Ananas comosus L.) revealed their potential roles in development regulation and cold stress response.BMC plant biology · 2025Article
- Comparative transcriptome analysis reveals candidate genes for cold stress response and early flowering in pineapple.Scientific reports · 2023Article
- Identification of bromelain subfamily proteases encoded in the pineapple genome.Scientific reports · 2023Article
- Bromelain and Nisin: The Natural Antimicrobials with High Potential in Biomedicine.Pharmaceutics · 2021Review
- Papain-Like Cysteine Protease Gene Family in Fig (Frontiers in plant science · 2021Article
- Genome-Wide Identification and Expression Profiling of ATP-Binding Cassette (ABC) Transporter Gene Family in Pineapple (Frontiers in plant science · 2017Article
- HvPap-1 C1A Protease Participates Differentially in the Barley Response to a Pathogen and an Herbivore.Frontiers in plant science · 2017Article
- Inhibitory properties of cysteine protease pro-peptides from barley confer resistance to spider mite feeding.PloS one · 2015Article
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7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In plant cells, many cysteine proteinases (CPs) are synthesized as precursors in the endoplasmic reticulum, and then are subject to post-translational modifications to form the active mature proteinases. They participate in various cellular and physiological functions. Here, AcCP2, a CP from pineapple fruit (Ananas comosus L.) belonging to the C1A subfamily is analyzed based on the molecular modeling and homology alignment. Transcripts of AcCP2 can be detected in the different parts of fruits (particularly outer sarcocarps), and gradually increased during fruit development until maturity. To analyze the substrate specificity of AcCP2, the recombinant protein was overexpressed and purified from Pichia pastoris. The precursor of purified AcCP2 can be processed to a 25 kDa active form after acid treatment (pH 4.3). Its optimum proteolytic activity to Bz-Phe-Val-Arg-NH-Mec is at neutral pH. In addition, the overexpression of AcCP2 gene in Arabidopsis thaliana can improve the resistance to fungal pathogen of Botrytis cinerea. These data indicate that AcCP2 is a multifunctional proteinase, and its expression could cause fruit developmental characteristics of pineapple and resistance responses in transgenic Arabidopsis plants.
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