Mo-CBP3, a 2S albumin from Moringa oleifera, is a complex mixture of isoforms that arise from different post-translational modifications

Freire, José Ednésio da Cruz; Moreno, Frederico Bruno Mendes Batista; Monteiro-Júnior, José E.; Sousa, Antônio J.S.; Vasconcelos, Ilka M.; Oliveira, José T.A.; Monteiro-Moreira, Ana C.O.; Rocha, B.A.M.; Grangeiro, Thalles Barbosa

doi:10.1016/j.plaphy.2019.05.003

Cited by 7 publications

(4 citation statements)

References 58 publications

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“…This observation suggests that, depending on the purification procedure, different 2S albumin isoforms can be purified from an allergenic source, as observed here for pomegranate. Actually, in each species, 2S albumins represent a multigenic family [40][41][42][43] coding for a group of isoforms characterized by a few common features and several structural and physicochemical differences. In fact, similar to other 2S albumins [44][45][46][47], the pomegranate homologs have a blocked N-terminal residue and are rich in arginine and glutamine, representing a great source of nitrogen, and methionine, which is essential for sulfur storage.…”

Section: Discussionmentioning

confidence: 99%

“…It is reported that 2S albumins are synthesized as a single polypeptide with a theoretical molecular mass ranging from 18 to 24 kDa, that undergoes several post-translational modifications, including proteolysis, signal peptide removal and the formation of disulfide bridges [48,49]. In most 2S albumins, the precursor, or protein proform, is further cleaved into two subunits by an aspartic protease, thus forming a heterodimer which comprises a small subunit of about 3-4 kDa and a large one of about 8-10 kDa, kept together by two disulfide bonds [43,47,50]. A few monomeric 2S albumins have also been reported [41,51].…”

Section: Discussionmentioning

confidence: 99%

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Isolation, Characterization and IgE Binding of Two 2S Albumins of Pomegranate Seeds

Tuppo,

Alessandri,

Zaccaro

et al. 2024

Foods

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Literature reports suggest that the presence of proteins in pomegranate seeds is responsible for sensitization and IgE-mediated allergic reactions. The objective of this study was the analysis of a pomegranate seed extract and the isolation and characterization of proteins contained in high amounts. The extract characterization showed a protein profile with main bands at about 18 kDa and below 10 kDa upon SDS-PAGE, and molecules were recognized by specific IgEs upon immunoblotting. Then, two new 2S albumins, a monomeric and a heterodimeric one, were isolated by using classical biochemical methods. They were identified via direct protein sequencing and mass spectrometry, and their primary structure was analyzed and compared with homologous allergenic proteins via bioinformatics. In an Italian population of 703 suspected allergic patients, analyzed by using the FABER® test, the frequency of sensitization to the monomeric and heterodimeric 2S albumins was 1.7% and 0.28%, respectively. This study reports for the first time the isolation and characterization of two 2S albumins from pomegranate seeds. The clinical relevance of these molecules needs further investigation, for instance in populations having different exposures and allergy profiles.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Isolation, Characterization and IgE Binding of Two 2S Albumins of Pomegranate Seeds

Tuppo,

Alessandri,

Zaccaro

et al. 2024

Foods

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“…Additionally, a mixture of isoenzymes is produced by the M. oleifera seeds. The Mo-CBP 3 protein is a compact, thermoresistant (melting temperature of 98 • C), cationic protein, with antifungal activity [29].…”

Section: Characterization Of Seed Cake Extractsmentioning

confidence: 99%

Green Synthesis and Antibacterial Activity of Silver Nanoparticles Obtained from Moringa oleifera Seed Cake

et al. 2023

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In the present work, we report a simple, cost-efficient, and eco-friendly green method to synthesize silver nanoparticles with antimicrobial activity. An ethanolic extract from Moringa oleifera seed residue was used as a reducing and stabilizing agent in an aqueous solution of silver nitrate. The synthesized silver nanoparticles’ hydrodynamic radius, polydispersity index, and zeta-potential were evaluated by Dynamic Light Scattering. Scanning Electron Microscopy was employed to confirm the size and morphology of the nanoparticles. Synthesis of spherical particles with 127 ± 24 nm was confirmed. After sintering, the product of the synthesis was analyzed by X-ray diffraction. The X-ray diffraction pattern attributed to reflections of the (111), (200), (220), and (311) planes, which are characteristic of silver nanoparticles, confirms the successful synthesis of crystalline face-centered cubic nanoparticles. The antimicrobial activity of the bionanoparticles was tested against Escherichia coli BL21(DE3) cells and compared with the effect of a Moringa oleifera seed cake extract. Herein, we show that the growth of Escherichia coli is significantly affected by the addition of the synthesized bionanoparticles. Addition of the bionanoparticles inhibited the growth and lengthened the lag phase of the bacterial culture.

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“…Phosphorylation (Tables A1 and A2) is common and reversible in proteins, and generally fulfil a regulatory activity of the function of the protein (activate or inhibit its function) in processes such as growth, development of immunity, and responses to stress [28], so it regulate the nsLTPs functional roles. Furthermore, it has previously been observed that Ser and/or Thr residues in seed storage proteins are extensively phosphorylated improving the transport mechanism of these storage proteins [28].…”

Section: Nsltps Functional Motifs and Post-translational Modification...mentioning

confidence: 99%

Molecular and Functional Characterisation of Allergenic Non-specific Lipid Transfer Proteins of Sweet Lupin Seed Species

Rodrigo-Garcia¹,

Haro²,

Priego-Poyato³

et al. 2022

Legumes Research - Volume 1

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Non-specific lipid transfer proteins (nsLTPs) are small proteins abundant in plants, which function in transferring phospholipids and galactolipids across the membrane. nsLTPs also play a key role in plant resistance to biotic and abiotic stresses, growth and development, as well as in sexual reproduction, seed development, and germination. In addition, these proteins have previously been identified as food allergens. In the present study, we carried out a molecular and functional comparative characterisation of 25 sequences of nsLTPs of lupin legumes and other species. Extensive analysis was carried out; including comparison of databases, phylogeny, physical–chemical properties, functional properties of post-translational modifications, protein structure conservation, 2-D and 3D modelling, functional interaction analysis, and allergenicity including identification of IgE, T-cell, and B-cell binding epitopes. The results indicated that particular structural features of nsLTPs are essential to the functionality of these proteins, high level of structural stability and conservation. Information about different functional interactions between nsLTPs and ligands showed that nsLTPs can accommodate several of them with different structure; and that the relationship between structure and allergenicity was investigated through the identification of epitopes susceptible of being involved in cross-reactivity between species of the Fabaceae family.

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Mo-CBP3, a 2S albumin from Moringa oleifera, is a complex mixture of isoforms that arise from different post-translational modifications

Cited by 7 publications

References 58 publications

Isolation, Characterization and IgE Binding of Two 2S Albumins of Pomegranate Seeds

Isolation, Characterization and IgE Binding of Two 2S Albumins of Pomegranate Seeds

Green Synthesis and Antibacterial Activity of Silver Nanoparticles Obtained from Moringa oleifera Seed Cake

Molecular and Functional Characterisation of Allergenic Non-specific Lipid Transfer Proteins of Sweet Lupin Seed Species

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