A major continuous allergenic epitope of bovine β‐lactoglobulin recognized by human IgE binding

Ball, G.; Shelton, Michael J.; Walsh, Bradley J.; Hill, David; Hosking, C. S.; Howden, M.E.H.

doi:10.1111/j.1365-2222.1994.tb00987.x

Cited by 121 publications

(81 citation statements)

References 17 publications

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“…This assumption was tested using an allergen in milk, ␤-lactoglobulin (BLG). BLG contains two disulfides (19) that, when disrupted by site-directed mutagenesis, changed its structure (20) and the accessibility of IgGand IgE-binding epitopes (21,22). The disruption of disulfide bonds in BLG also had an impact on the sensitivity of this protein to digestion with pepsin and its overall allergenicity with respect to skin test responses and GI symptoms in a sensitized dog model of food allergy (12).…”

Section: Discussionmentioning

confidence: 99%

Protein Structure Plays a Critical Role in Peanut Allergen Stability and May Determine Immunodominant IgE-Binding Epitopes

Sen¹,

Kopper²,

Pons³

et al. 2002

The Journal of Immunology

208

191

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Hypersensitivity to peanuts is a reaction mediated by IgE Abs in response to several peanut protein allergens. Among these allergenic proteins, Ara h 2 is one of the most commonly recognized allergens. Ara h 2 is a 17-kDa protein that has eight cysteine residues that could form up to four disulfide bonds. Circular dichroism studies showed substantial changes in the secondary and tertiary structures of the reduced Ara h 2 as compared with the native protein. Upon treatment with trypsin, chymotrypsin, or pepsin, a number of relatively large fragments are produced that are resistant to further enzymatic digestion. These resistant Ara h 2 peptide fragments contain intact IgE-binding epitopes and several potential enzyme cut sites that are protected from the enzymes by the compact structure of the protein. The enzyme-treated allergen remains essentially intact despite the action of proteases until the fragments are dissociated when the disulfide linkages are reduced. Amino acid sequence analysis of the resistant protein fragments indicates that they contain most of the immunodominant IgE-binding eptiopes. These results provide a link between allergen structure and the immunodominant IgE-binding epitopes within a population of food-allergic individuals.

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Section: Discussionmentioning

confidence: 99%

Protein Structure Plays a Critical Role in Peanut Allergen Stability and May Determine Immunodominant IgE-Binding Epitopes

Sen¹,

Kopper²,

Pons³

et al. 2002

The Journal of Immunology

208

191

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“…Caseins and b-lactoglobulin (b-Lg) have been described as the main antigenic and allergenic components for human beings [3,4], although immunoglobulins, a-lactalbumin (a-La), and bovine serum albumin (BSA) were also found to be reactive with different isotypes of human antibodies [5,6]. Several immunoreactive epitopes have been identified in caseins [7,8] and b-Lg [9]. Most of the epitopes present in the casein molecules are sequential since the high number of proline and hydrophobic residues (45%) in these proteins determine an undefined secondary and tertiary structure [10].…”

Section: Introductionmentioning

confidence: 99%

Detection and identification of a soy protein component that cross-reacts with caseins from cow's milk

Rozenfeld

Docena

Añón

et al. 2002

Clinical and Experimental Immunology

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Food allergy is becoming a medical, economical and social problem. Soybean, together with milk, peanuts and eggs, are the major allergenic foods. This pathology affects the infant population, when the gut barrier is immature and the immune system is still refining its ability to tolerate food proteins. In our country, cow's milk allergy (CMA) constitutes the main food allergy in infancy, but soy allergy has become exacerbated because of the increased utilization of soy-based formulas as cow's milk (CM) substitutes and the inclusion of soy-proteins in many processed foods. Once a food allergy is diagnosed, the only proven therapy is the strict elimination of the offending allergens from the diet. Available substitutes for CM include milks from different mammalian animals, soy-based formulas, hydrolysed cow's milk proteins (CMP) and amino acid-based formulas. Furthermore, there is evidence that soy proteins may trigger allergic reactions in CMA patients, as assessed by a double-blind placebo controlled food challenge (DBPCFC) [1].Milk contains more than 50 proteins and the major ones are implicated in a number of immunologically mediated reactions [2]. Caseins and b-lactoglobulin (b-Lg) have been described as the main antigenic and allergenic components for human beings [3,4], although immunoglobulins, a-lactalbumin (a-La), and bovine serum albumin (BSA) were also found to be reactive with different isotypes of human antibodies [5,6]. Several immunoreactive epitopes have been identified in caseins [7,. Most of the epitopes present in the casein molecules are sequential since the high number of proline and hydrophobic residues (45%) in these proteins determine an undefined secondary and tertiary structure [10]. Besides, caseins tend to aggregate as a result of hydrophobic interactions to give quaternary structures [11], and this may create conformational epitopes buried in the hydrophobic interior of the micelle [7]. These epitopes are only exposed and accessible to the immune system after denaturation of the complex by digestion.A number of soy proteins that bind antibodies, especially IgE, have been identified [12,13]. The main fractions of storage globulins from seed proteins are the complexes 7S or b-conglycinin, and 11S or glycinin. The 7S complex is generally a trimer with MW 150-200 kD, whereas 11S is a hexamer with MW 300-400 kD [14]. In the 7S fraction, or b-conglycinin, several IgE-binding proteins have been identified and some of them have been purified and characterized: Gly m Bd 28K, Gly m Bd 30K, Gly m Bd 60K [15,16]. Sequence homology has been reported between these allergens and the thiol proteinase family SUMMARYSoy-based formulas are the most employed cow's milk substitutes in the treatment of cow's milk allergy in our country. Since adverse reactions have been reported in allergic patients as a consequence of exposure to soy proteins, we have investigated the possible cross-reactivity between components from soybean and cow's milk. A cow's milk specific polyclonal antiserum and casein specific m...

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“…In addition, lipocalins have a highly conserved structure that confers a resistance to degradation. For example, ␤lg is able to resist acidic treatment and to pass the stomach intact (5). It has been suggested that this resistance may be important for immunogenicity.…”

Section: Cdna Cloning and Sequencing Of The Major Horse Allergen Equ C1mentioning

confidence: 99%

cDNA Cloning and Sequencing Reveal the Major Horse Allergen Equ c1 to Be a Glycoprotein Member of the Lipocalin Superfamily

Grégoire¹,

Rosinski‐Chupin

Rabillon³

et al. 1996

Journal of Biological Chemistry

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The gene encoding the major horse allergen, designated Equus caballus allergen 1 (Equ c1), was cloned from total cDNA of sublingual salivary glands by reverse transcription-polymerase chain reaction using synthetic degenerate oligonucleotides deduced from N-terminal and internal peptide sequences of the glycosylated hair dandruff protein. A recombinant form of the protein, with a polyhistidine tail, was expressed in Escherichia coli and purified by immobilized metal affinity chromatography. The recombinant protein is able to induce a passive cutaneous anaphylaxis reaction in rat, and it behaves similarly to the native Equ c1 in several immunological tests with allergic patients' IgE antibodies, mouse monoclonal antibodies, or rabbit polyclonal IgG antibodies. Amino acid sequence identity of 49 -51% with rodent urinary proteins from mice and rats suggests that Equ c1 is a new member of the lipocalin superfamily of hydrophobic ligand-binding proteins that includes several other major allergens. An RNA blot analysis demonstrates the expression of mRNA Equ c1 in liver and in sublingual and submaxillary salivary glands.

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A major continuous allergenic epitope of bovine β‐lactoglobulin recognized by human IgE binding

Cited by 121 publications

References 17 publications

Protein Structure Plays a Critical Role in Peanut Allergen Stability and May Determine Immunodominant IgE-Binding Epitopes

Protein Structure Plays a Critical Role in Peanut Allergen Stability and May Determine Immunodominant IgE-Binding Epitopes

Detection and identification of a soy protein component that cross-reacts with caseins from cow's milk

cDNA Cloning and Sequencing Reveal the Major Horse Allergen Equ c1 to Be a Glycoprotein Member of the Lipocalin Superfamily

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