Kiwellin, a Novel Protein from Kiwi Fruit. Purification,
Biochemical Characterization and Identification as an Allergen*

Tamburrini, Maurizio; Cerasuolo, Ivana; Carratore, Vito; Stanziola, Anna Agnese; Zofra, S; Romano, Luigi; Camardella, Laura; Ciardiello, Maria Antonietta

doi:10.1007/s10930-005-7638-7

Cited by 73 publications

(78 citation statements)

References 21 publications

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“…Similarities were also found with Barwin-like proteins sharing a structural motif with various wound-induced and other pathogenesis-related proteins from potato, rubber trees, and tobacco [96].…”

Section: Expansinssupporting

confidence: 55%

Molecular Properties of Plant Food Allergens: A Current Classification into Protein Families

Hauser¹,

Egger²,

Wallner³

et al. 2008

TOIJ

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So far the allergen list of the International Union of Immunological Societies (IUIS) allergen nomenclature subcommittee comprises 130 plant-derived food allergens. Based on sequence homology these allergens can be classified into only 27 out of 9,000 known protein families according to the Allfam database. These families comprise the prolamin and cupin superfamilies, pathogenesis related proteins, profilins, thaumatin-like proteins, oleosins, expansins, a number of enzymes and protease inhibitors among others. The classification on structural and thus biochemical and functional similarities will provide a new outlook on the molecules and might contribute to answer the question about allergenicity of different proteins. This will help to define clinical relevant allergenic molecules and explain cross-reactive phenomena between single food allergen sources as well as between food allergens and allergenic molecules of other origins (e.g. pollen).

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Section: Expansinssupporting

confidence: 55%

Molecular Properties of Plant Food Allergens: A Current Classification into Protein Families

Hauser¹,

Egger²,

Wallner³

et al. 2008

TOIJ

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“…In the A. chinensis mapping population, high CP activity segregates as a single dominant Mendelian trait that is associated with the presence of the ACT1A- and kiwellin (Tamburrini et al, 2005) proteins, respectively. B, Western analysis using a chitinase-specific polyclonal antibody.…”

Section: Discussionmentioning

confidence: 99%

Mapping, Complementation, and Targets of the Cysteine Protease Actinidin in Kiwifruit

et al. 2011

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Cysteine proteases (CPs) accumulate to high concentration in many fruit, where they are believed to play a role in fungal and insect defense. The fruit of Actinidia species (kiwifruit) exhibit a range of CP activities (e.g. the Actinidia chinensis variety YellowA shows less than 2% of the activity of Actinidia deliciosa variety Hayward). A major quantitative trait locus for CP activity was mapped to linkage group 16 in a segregating population of A. chinensis. This quantitative trait locus colocated with the gene encoding actinidin, the major acidic CP in ripe Hayward fruit encoded by the ACT1A-1 allele. Sequence analysis indicated that the ACT1A locus in the segregating A. chinensis population contained one functional allele (A-2) and three nonfunctional alleles (a-3, a-4, and a-5) each containing a unique frameshift mutation. YellowA kiwifruit contained two further alleles: a-6, which was nonfunctional because of a large insertion, and a-7, which produced an inactive enzyme. Site-directed mutagenesis of the act1a-7 protein revealed a residue that restored CP activity. Expression of the functional ACT1A-1 cDNA in transgenic plants complemented the natural YellowA mutations and partially restored CP activity in fruit. Two consequences of the increase in CP activity were enhanced degradation of gelatin-based jellies in vitro and an increase in the processing of a class IV chitinase in planta. These results provide new insight into key residues required for CP activity and the in vivo protein targets of actinidin.

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“…It derives from the processing of kiwellin, a wellrepresented novel allergenic protein present in the edible part of the fruit [17]. Its isolation and purification processes and its structural characterization were reported in our previous study [18].…”

Section: Introductionmentioning

confidence: 99%

Studies on the Effect of Salts on the Channel Activity of Kissper, a Kiwi Fruit Peptide

Meleleo¹

2012

TONUTRAJ

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Fruits and vegetables are known to possess health benefits: indeed, they contain a large number of bioactive molecules with a positive impact on human health. Dietary proteins possess specific biological properties which make these components potential ingredients of functional or health-promoting foods. Many of these properties are attributed to physiologically-active peptides encrypted in protein molecules.Kissper, a 39-residue peptide isolated from kiwi fruit (Actinidia deliciosa), derives from the processing of kiwellin, a well-represented novel allergenic protein present in the edible part of the fruit. Kissper has six cysteine residues forming three disulfide bridges. This cysteine pattern is similar, but not identical, to those observed in some plant and animal proteins, including toxins involved in defence mechanisms. We show that kissper forms ion channels in DOPS:DOPE:POPC PLMs in different media, such as KCl, potassium gluconate, potassium citrate and potassium phosphate monobasic. Kissper's channels show a strong voltage dependence in all media used, and an estimated pore diameter in the range from 1.9 to 7.6 Å in KCl medium. Finally, kissper's pores shift selectivity from anions to neutral to cations, depending on the nature of the salt solutions. Therefore we propose the kissper as a novel nutraceutical component of kiwi fruit that may have a positive impact on human health due to its channel-like pathways which modulate membrane permeability. The kissper action might promote the adsorption of substances, in particular, within the gastrointestinal tract, helping digestion, preventing constipation and harmful accumulation of metabolites.

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Kiwellin, a Novel Protein from Kiwi Fruit. Purification, Biochemical Characterization and Identification as an Allergen*

Cited by 73 publications

References 21 publications

Molecular Properties of Plant Food Allergens: A Current Classification into Protein Families

Molecular Properties of Plant Food Allergens: A Current Classification into Protein Families

Mapping, Complementation, and Targets of the Cysteine Protease Actinidin in Kiwifruit

Studies on the Effect of Salts on the Channel Activity of Kissper, a Kiwi Fruit Peptide

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