The major protein allergen of peach (Prunus persica), Pru p1, has recently been identified as a lipid transfer protein (LTP), The complete primary structure of Pru p1, 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.

Complete amino acid sequence determination of the major allergen of peach (Prunus persica) Pru p 1 / E.A. Pastorello, C. Ortolani, C. Baroglio, V. Pravettoni, M. Ispano, M.G. Giuffrida, D. Fortunato, L. Farioli, M. Monza, L. Napolitano, M. Sacco, E. Scibola, A. Conti. - In: BIOLOGICAL CHEMISTRY. - ISSN 1431-6730. - 380:11(1999), pp. 1315-1320.

Complete amino acid sequence determination of the major allergen of peach (Prunus persica) Pru p 1

E.A. Pastorello
Primo
;
1999

Abstract

The major protein allergen of peach (Prunus persica), Pru p1, has recently been identified as a lipid transfer protein (LTP), The complete primary structure of Pru p1, 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.
lipid transfer protein ; primary structure ; rosaceae
Settore MED/09 - Medicina Interna
1999
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/207872
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