Evolutionary distance from human homologs reflects allergenicity of animal food proteins

Jenkins, John A.; Breiteneder, Heimo; Mills, E. N. Clare

doi:10.1016/j.jaci.2007.08.019

Cited by 203 publications

(144 citation statements)

References 30 publications

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“…In fact, no human IgE response to tropomyosin from birds or fish has been identified. This is expected since these sequences have an identity with human tropomyosins greater than 63%, which is translated in the absence of allergenic activity [27].…”

Section: Allergenic Animal Proteinsmentioning

confidence: 98%

“…Thus, if the protein has a sequence identity from 54 to 63% with respect to human homologues, then it is considered as allergenic. Nevertheless, a higher identity does not implies allergenicity [27,28].…”

Section: Allergenic Animal Proteinsmentioning

confidence: 98%

“…Animal food allergens are classified into three general families such as tropomyosins, EF-hand proteins, and caseins [27]. However, regardless of their family the ability to act as an allergen appears to be related to relative identity with human homologues.…”

Section: Allergenic Animal Proteinsmentioning

confidence: 99%

“…EF proteins form the second family of animal-derived food allergens, and they are composed of parvalbumin [27]. Parvalbumins are divided into α-and β-parvalbumin.…”

Section: Allergenic Animal Proteinsmentioning

confidence: 99%

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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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Section: Allergenic Animal Proteinsmentioning

confidence: 98%

Section: Allergenic Animal Proteinsmentioning

confidence: 98%

Section: Allergenic Animal Proteinsmentioning

confidence: 99%

“…EF proteins form the second family of animal-derived food allergens, and they are composed of parvalbumin [27]. Parvalbumins are divided into α-and β-parvalbumin.…”

Section: Allergenic Animal Proteinsmentioning

confidence: 99%

See 2 more Smart Citations

Vegetable Proteins: Non-sensitizing Encapsulation Agents for Bioactive Compounds

Quiroz¹,

Durán²,

Ciro-Gómez³

et al. 2017

Allergen

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show abstract

“…The precise mechanism of the effects of glycosylation on the allergenic response are not clear. Attempts have been made to develop and evaluate algorithms which predict protein allergenic response based on sequence homology (Aalberse & Stapel, 2001;Jameson & Wolf, 1988), structural identity, and evolutionary relationship (Jenkins et al, 2007), albeit with limited predicting power. The Food and Agriculture Organization (FAO) of the United Nations together with the World Health Organization (WHO) developed a decision tree to assess the allergenic potential of genetically engineered food ingredients based on sequence homology followed by serum screens (FAO/WHO 2001, reviewed by Bernstein et al, 2003).…”

Section: Food Allergy and Intolerancementioning

confidence: 99%