Abstract - Structural analysis of the glycoprotein allergen Hev b 4 from natural rubber latex by mass spectrometry


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	Publications of MRB Latest Publications MRB Digest Journal of Rubber Research 4^th Qtr 2008 Vol 11(4) 3^rd Qtr 2008 Vol 11(3) 2^nd Qtr 2008 Vol 11(2) 1^st Qtr 2008 Vol 11(1) 4^th Qtr 2007 Vol 10(4) 3^rd Qtr 2007 Vol 10(3) 2^nd Qtr 2007 Vol 10(2) 1^st Qtr 2007 Vol 10(1) 1^st Qtr 2006 Vol 9(1) 2^nd Qtr 2006 Vol 9(2) 3^rd Qtr 2006 Vol 9(3) 4^th Qtr 2006 Vol 9(4) Submit paper/article Order Form	Abstract Structural analysis of the glycoprotein allergen Hev b 4 from natural rubber latex by mass spectrometry D. Kolarich, F. Altmann, and E. Sunderasan Biochimica et Biophysica Acta, 1760(4),715-20 The lecithinase homolog (Hev b 4) from Hevea brasiliensis (Q6T4P0_HEVBR) is an important natural rubber latex allergen. Hev b 4 is a highly glycosylated protein and its carbohydrate moiety has been implicated in the binding of IgE from natural rubber latex allergic patients. The cDNA for Hev b 4 has recently been cloned and sequenced. Here, we have analyzed the post-translational modifications of natural Hev b 4 by liquid chromatography/ electrospray ionization-mass spectrometry of tryptic peptides. Seven of the eight potential glycosylation sites were found to be occupied. One site, however, was only partially glycosylated. Asn224 was substituted by complex type N-glycans with fucose and xylose, whereas all other sites carried either oligomannose glycans or a mixture of oligomannose and complex N-glycans. Glycosylation site Asn308, the most C-terminal one of the eight sites, was only found in the non-glycosylated form. The complex type N-glycans apparently form the molecular basis for the immune reaction with patients' sera. A large fraction of Hev b 4 molecules contains two or more complex N-glycans and thus a physiological reaction against these polyvalent allergens on the basis of the carbohydrate is in theory possible. Aside from allowing glycosylation analysis, the mass spectrometric data defined the N-terminal cleavage site of Hev b 4. This study once more demonstrates the outstanding analytical potential of electrospray ionization-mass spectrometry coupled with liquid chromatographic separation. back
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