TAILIEUCHUNG - Báo cáo khoa học: The N-glycans of yellow jacket venom hyaluronidases and the protein sequence of its major isoform in Vespula vulgaris

Hyaluronidase (. ), one of the three major allergens of yellow jacket venom, is a glycoprotein of 45 kDa that is largely responsible for the cross-reactivity of wasp and bee venoms with sera of allergic patients. The asparagine-linked carbohydrate often appears to constitute the com-mon IgE-binding determinant. | iFEBS Journal The N-glycans of yellow jacket venom hyaluronidases and the protein sequence of its major isoform in Vespula vulgaris Daniel Kolarich1 Renaud Leonard1 Wolfgang Hemmer2 and Friedrich Altmann1 1 Department of Chemistry University of NaturalResources and Applied Life Sciences BOKU Vienna Austria 2 Floridsdorf Allergy Center FAZ Vienna Austria Keywords cross-reactive carbohydrate determinant hyaluronidase Hymenoptera insect sting allergy Vespula Correspondence F. Altmann Department of Chemistry BOKU Muthgasse 18 A-1190 Vienna Austria Fax 43 136006 6059 Tel 43 136006 6062 E-mail Note The nucleotide sequence of Ves v 2b can be found at EMBL AJ920395 The protein sequence for Ves v 2b fragment can be found at ExPASy Q5D7H4. Received 11 May 2005 revised 22 June 2005 accepted 1 July 2005 Hyaluronidase . one of the three major allergens of yellow jacket venom is a glycoprotein of 45 kDa that is largely responsible for the cross-reactivity of wasp and bee venoms with sera of allergic patients. The asparagine-linked carbohydrate often appears to constitute the common IgE-binding determinant. Using a combination of MALDI MS and HPLC of 2-aminopyridine-labelled glycans we found core-difucosylated paucimannosidic glycans to be the major species in the 43-45 kDa band of Vespula vulgaris and also in the corresponding bands of venoms from five other wasp species V. germanica V. maculifrons V. pensylvanica V. flavopilosa and V. squamosa . Concomitant peptide mapping of the V. vulgaris 43 kDa band identified the known hyaluronidase Ves v 2 SwissProt P49370 but only as a minor component. De novo sequencing by tandem MS revealed the predominating peptides to resemble a different yet homologous sequence. cDNA cloning retrieved a sequence with 58 and 59 homology to the previously known isoform and to the Dolichovespula maculata and Polistes annularis hyaluronidases. Close homologues of this new putative hyaluronidase b Ves v 2b were .

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