Cross-reactivity between mammalian proteins

Restani, Patrizia; Beretta, Barbara; Fiocchi, Alessandro; Ballabio, Cinzia; Galli, Corrado L.

doi:10.1016/s1081-1206(10)62116-3

Cited by 137 publications

(90 citation statements)

References 16 publications

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“…In addition to that and according to Restani et al. [17,18] the cross reactions were observed between proteins of milk and meats, such as caseins and albumin, of different species like the cow, goat, ewe and mare and it was explained by the probable resemblance in the sequence of their proteins.…”

Section: Resultsmentioning

confidence: 82%

“…Consequently, cross reactions occur when two different milk proteins can bind the same immunoglobulins (Ig). Thus, there is a risk of cross reactivity between cow's milk and goat's milk [2][3][4] and between mare's milk and ewe's milk [5][6][7][8][9] . The dromedary remains the species taxonomically farthest away from the cow and for which there is little data on the antigenic properties of its milk proteins.…”

Section: Introductionmentioning

confidence: 99%

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Cross Reactivity between Dromedary Whey Proteins and IgG Anti Bovine α-Lactalbumin and Anti Bovine β-Lactoglobulin

Youcef¹,

Saïdi²,

Mezemaze³

et al. 2009

American J. of Applied Sciences

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Problem statement: Our aim was to enhance the data on antigenic properties of dromedary whey proteins. Approach: The identification of the whey proteins was carried by SDS-page and Reversed phase high performance liquid chromatography (RP-HPLC). The cross-reactivity of dromedary whey proteins with IgG anti bovine β-lactoglobulin and anti bovine α-lactalbumin, obtained by immunisation of Balb/c mice, was carried out by ELISA. Results: The SDS-page showed the presence of band corresponding to α-lactalbumin and albumin serum; this was confirmed by the chromatogram obtained by RP-HPLC, where we detected a pick corresponding to α-lactalbumin. There was a cross reaction of dromedary whey proteins with IgG anti bovin α- lactalbumin but it was very weak with IgG anti boin β-lactoglobulin. Conclusion: We detected a cross reactivity between dromedary whey proteins and IgG anti bovin α-lactalbumin.

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Section: Resultsmentioning

confidence: 82%

Section: Introductionmentioning

confidence: 99%

Cross Reactivity between Dromedary Whey Proteins and IgG Anti Bovine α-Lactalbumin and Anti Bovine β-Lactoglobulin

Youcef¹,

Saïdi²,

Mezemaze³

et al. 2009

American J. of Applied Sciences

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“…Conversely, sensitization to BSA is the main predictive marker for the cross-reactivity to cow's milk that is present in 73-93% of patients with beef allergies, despite of the fact that BSA shares 76% identity to its human homolog [27,29].…”

Section: Allergenic Animal Proteinsmentioning

confidence: 99%

Vegetable Proteins: Non-sensitizing Encapsulation Agents for Bioactive Compounds

Quiroz¹,

Durán²,

Ciro-Gómez³

et al. 2017

Allergen

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Plant-derived proteins are remarkable macromolecules of scientific interest because they represent an alternative to the animal-derived proteins and petroleum-derived polymers. Many food proteins especially those derived from animal sources could act as antigens in humans. For instance, milk proteins extracted from cows may cause food intolerance during infancy. Further, soybean, peanuts, tree nuts, fish, crustacean shellfish and egg proteins may act as antigens in 90% of children. Since the GI tract is permeable to intact antigens the oral intake of these proteins may generate gastrointestinal (50-80%), cutane ous (20-40%) and respiratory symptoms (4-25%). Most of these allergens are water-soluble glycoproteins that are resistant to acids and enzymes. Usually, these proteins have a small molecular weight (10,000-60,000 kDa), water solubility, glycosylation residues, and a rela tive resistance to heat and digestion. Allergenicity is less frequent in vegetable proteins due to their less flexible and non-compact structure. Allergenicity is also related to the resistance to proteolysis, post-translational glycosylation, presence of epitopes, and enzy matic proteolysis. Moreover, proteins serve as a coating material if structural modifica tions in the protein, either by physical, chemical or enzymatic mechanisms are conducted. As a result, their allergenicity is reduced, and their functional properties are enhanced.

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“…Occasionally amino acid formulas are indicated if an individual is highly sensitive and reacts to small amounts of residual milk proteins in an extensively hydrolysed formula. Most children with CMA are sensitive to goat and sheep milk due to cross reactivity and should not be recommended 22 . For older subjects who are on a milk free diet, calcium supplementation is recommended.…”

Section: Substitutesmentioning

confidence: 99%

Cow’s milk allergy

Liyanage

2015

Sri Lanka J Child Health

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Cross-reactivity between mammalian proteins

Cited by 137 publications

References 16 publications

Cross Reactivity between Dromedary Whey Proteins and IgG Anti Bovine α-Lactalbumin and Anti Bovine β-Lactoglobulin

Cross Reactivity between Dromedary Whey Proteins and IgG Anti Bovine α-Lactalbumin and Anti Bovine β-Lactoglobulin

Vegetable Proteins: Non-sensitizing Encapsulation Agents for Bioactive Compounds

Cow’s milk allergy

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