ArticlePloS one2015
Mo-CBP3, an antifungal chitin-binding protein from Moringa oleifera seeds, is a member of the 2S albumin family.
Article in PloS one, 2015. 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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Who cites it
10 citing papers in PubMed, 70 citations in OpenAlex.
- Exploring the HNE-inhibitory potential of in silico selected Moringa oleifera defense proteins.Journal of computer-aided molecular design · 2026Article
- Comparison of Different Encapsulation Techniques in Exosomes Obtained from Goat and Bovine Milk.ACS omega · 2025Article
- Protein fromFood science and biotechnology · 2022Article
- Comparative study of flocculation and adsorption behaviour of water treatment proteins from Moringa peregrina and Moringa oleifera seeds.Scientific reports · 2019Article
- Article
- A review of phytochemistry, metabolite changes, and medicinal uses of the common sunflower seed and sprouts (Helianthus annuus L.).Chemistry Central journal · 2017Review
- A Chitin-binding Protein Purified fromFrontiers in microbiology · 2017Article
- Proteomic Profiles Reveal the Function of Different Vegetative Tissues of Moringa oleifera.The protein journal · 2016Article
- Phytochemicals of Moringa oleifera: a review of their nutritional, therapeutic and industrial significance.3 Biotech · 2016Review
- A tripartite approach identifies the major sunflower seed albumins.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2016Article
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mo-CBP3 is a chitin-binding protein from M. oleifera seeds that inhibits the germination and mycelial growth of phytopathogenic fungi. This protein is highly thermostable and resistant to pH changes, and therefore may be useful in the development of new antifungal drugs. However, the relationship of MoCBP3 with the known families of carbohydrate-binding domains has not been established. In the present study, full-length cDNAs encoding 4 isoforms of Mo-CBP3 (Mo-CBP3-1, Mo-CBP3-2, Mo-CBP3-3 and Mo-CBP3-4) were cloned from developing seeds. The polypeptides encoded by the Mo-CBP3 cDNAs were predicted to contain 160 (Mo-CBP3-3) and 163 amino acid residues (Mo-CBP3-1, Mo-CBP3-2 and Mo-CBP3-4) with a signal peptide of 20-residues at the N-terminal region. A comparative analysis of the deduced amino acid sequences revealed that Mo-CBP3 is a typical member of the 2S albumin family, as shown by the presence of an eight-cysteine motif, which is a characteristic feature of the prolamin superfamily. Furthermore, mass spectrometry analysis demonstrated that Mo-CBP3 is a mixture of isoforms that correspond to different mRNA products. The identification of Mo-CBP3 as a genuine member of the 2S albumin family reinforces the hypothesis that these seed storage proteins are involved in plant defense. Moreover, the chitin-binding ability of Mo-CBP3 reveals a novel functionality for a typical 2S albumin.
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