Complete amino acid sequence determination of the major allergen of peach (Prunus persica) Pru p 1
Academic Article
Publication Date:
1999
abstract:
The major protein allergen of peach (Prunus persica), Pru p 1, has recently been identified as a lipid transfer protein (LTP). The complete primary structure of Pru p 1, obtained by direct amino acid sequence and liquid chromatography-mass spectrometry (LC-MS) analyses with the purified protein, is described here. The protein consists of 91 amino acids with a calculated molecular mass of 9178 Da. The amino acid sequence contains eight strictly conserved cysteines, as do all known LTPs, but secondary structure predictions failed to classify the peach 9 kDa protein as an 'all-alpha type', due to the high frequency of amino acids (nine prolines) disrupting alpha helices. Although the sequence similarity with maize LTP is only 63%, out of the 25 amino acids forming the inner surface of the tunnel-like hydrophobic cavity in maize ns-LTP 16 are identical and 7 similar in the peach homolog, supporting the hypothesis of a similar function.
Iris type:
01.01 Articolo in rivista
Keywords:
allergen; lipid transfer protein; proline; vegetable protein; amino acid sequence; article; fruit; genetic con; liquid chromatography; maize; mass spectrometry; molecular weight; nonhuman; nucleotide sequence; priority journal; protein secondary structure; sequence homology; Allergens; Amino Acid Sequence; Amino Acids; Antigens; Plant; Carrier Proteins; Endopeptidases; Mass Spectrometry; Metalloendopeptidases; Molecular Sequence Data; Plant Proteins; Rosales; Sequence Analysis; Protein; Sequence Homology; Amino Acid; Prunus persica; Rosaceae; Zea mays
List of contributors:
Conti, Amedeo; Giuffrida, MARIA GABRIELLA; Fortunato, Donatella; Napolitano, Lorenzo
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