Amino acid sequence of ragweed pollen allergen Ra5

Le, Mole; Goodfriend, L.; Cb, Lapkoff; Jm, Kehoe; Jd, Capra

doi:10.1021/bi00677a019

Cited by 81 publications

(33 citation statements)

References 19 publications

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“…Ra3 (34) 88-Cys-Thr-Lys-Asp-Gln-Lys Ra5 (35) 40-Ser-Lys-Lys-Cys-Gly-Lys Lys-Pro-Thr-Asp-Gly-Asn-aAbu-Thr-aAbu (aAbu = a-amino butyric acid, replacing Cys) corresponding to residues 138-149 of the hepatitis B surface antigen (HBsAg) protein, and tested it for antigenic activity. The peptide side chains were deprotected under conditions where the peptide remained attached to the polystyrene beads (21).…”

Section: Ragweed Allergensmentioning

confidence: 99%

Prediction of protein antigenic determinants from amino acid sequences.

Hopp¹,

Woods²

1981

Proc. Natl. Acad. Sci. U.S.A.

3,265

1,549

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A method is presented for locating protein antigenic determinants by analyzing amino acid sequences in order to find the point of greatest local hydrophilicity. This is accomplished by assigning each amino acid a numerical value (hydrophilicity value) and then repetitively averaging these values along the peptide chain. The point ofhighest local average hydrophilicity is invariably located in, or immediately adjacent to, an antigenic determinant. It was found that the prediction success rate depended on averaging group length, with hexapeptide averages yielding optimal results. The method was developed using 12 proteins for which extensive immunochemical analysis has been carried out and subsequently was used to predict antigenic determinants for the following proteins: hepatitis B surface antigen, influenza hemagglutinins, fowl plague virus hemagglutinin, human histocompatibility antigen HLA-B7, human interferons, Escherichia coli and cholera enterotoxins, ragweed allergens Ra3 and Ra5, and streptococcal M protein. The and indicate that they are frequently found on regions of a molecule that have an unusually high degree of exposure to solvent-i. e., regions which project into the medium (for reviews, see refs. 1 and 3). This, together with the fact that charged, hydrophilic amino acid side chains are common features of antigenic determinants, led us to investigate the possibility that at least some antigenic determinants might be associated with stretches of amino acid sequence that contain a large number of charged and polar residues and are lacking in large hydrophobic residues. A suitable means of methodically searching for such regions was found by combining a method like that of Chou and Fasman (5), in which numerical values for amino acids are repetitively averaged over the length ofa polypeptide chain, with a set ofvalues expressing the relative hydrophilicity of each amino acid. Suitable values were available in the solvent parameters assigned by Levitt (6), which are derivatives ofthe hydrophobicity values ofNozaki and Tanford (9).In Table 1 are listed the numerical values (hydrophilicity values) assigned to the 20 amino acids commonly found in proteins. In the first column, the values of Levitt (6) are listed, whereas the second column lists the values that were finally chosen for our hydrophilicity calculations. The values were generally retained as expressed by Levitt; however, changes in the values for proline, asparatic acid, and glutamic acid improve the prediction results, as explained later. Hydrophilicity analysis of a protein is carried out by the following method.Each amino acid in the sequence of the protein is assigned its hydrophilicity value, then these values are repetitively averaged down the length of the polypeptide chain, generating a series of local hydrophilicity values. The number of hydrophilicity values that are averaged at each repetition is arbitrary, and we chose groups of six for our initial studies because this is the approximate size ofan antigenic determinant...

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Section: Ragweed Allergensmentioning

confidence: 99%

Prediction of protein antigenic determinants from amino acid sequences.

Hopp¹,

Woods²

1981

Proc. Natl. Acad. Sci. U.S.A.

3,265

1,549

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“…The purification of the allergens allowed determination of several partial N-terminal sequences, and two complete protein sequences (AmbaV: Mole et al 1975; AmbalII: Klapper et al, 1988 (Kaplan, 1985). Pollen of grasses, trees and weeds, spores of moulds as well as other airborn particles such as faeces from mites and dander from pets and other domestic animals serve as a source of allergenic proteins (Marsh et al, 1986 (Kaplan, 1985 major allergens of the house dust mite Dermatophagoides pteronyssinus (Chua et al, 1988a).…”

mentioning

confidence: 99%

The gene coding for the major birch pollen allergen Betv1, is highly homologous to a pea disease resistance response gene.

et al. 1989

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Pollen of the white birch (Betula verrucosa) is one of the main causes of Type I allergic reactions (allergic rhinoconjunctivitis, allergic bronchial asthma) in Middle and Northern Europe, North America and the USSR. Type I allergies are a major threat to public health in these countries, since 10‐15% of the population suffer from these diseases. BetvI, an allergenic protein with an Mr of 17 kd is a constituent of the pollen of white birch and is responsible for IgE binding in more than 95% of birch pollen allergic patients. Here, we report the complete nucleotide sequence and deduced amino acid sequence of a cDNA clone coding for the major pollen allergen (BetvI) of white birch. It is similar to the N‐terminal peptide sequences of the allergens of hazel, alder and hornbeam (close relatives) but it has no significant sequence homology to any other known allergens. However, it shows 55% sequence identity with a pea disease resistance response gene, indicating that BetvI may be involved in pathogen resistance of pollen.

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“…This allergen has a known primary structure consisting of 45 amino acids and a molecular weight of 5,000 (11,12). We also found a significant association between IgE mediated sensitivity to the more complex allergen, rye group I (molecular weight, 27,000), and antigens of the HL-A 8 cross-reacting group (10, 13), which is especially striking in allergic subjects having low levels of total IgE in their serums.…”

mentioning

confidence: 52%