Polybia paulista venom displays phospholipase, hyaluronidase, proteolytic, haemolylic among other activities. Besides, its venom also displays higher myotoxic activity than that from some bothropic venoms. So, it is important that the characterization of the main venom allergens be investigated through the determination of their gene sequence and organization; protein structures and action mechanisms. We determined and analyzed two partial cDNA sequences from the one of the most important venom allergens of the Polybia paulista venom, the enzyme hyaluronidase (HYAL). The cDNA was obtained through the mRNA extraction from the insect abdomens and amplification through RACE-PCR using gene-specific primers. The fragments were cloned, sequenced and the obtained data were analyzed and compared with similar sequences. The two sequences spanned almost the whole gene and exhibited, in gels, ca 800 (HYAL 1) and 600 (HYAL 2) bp. The translated HYAL 1 sequence corresponded to 227 residues and HYAL 2 to 228. High identities with nucleotide sequences (90% for both fragments) and with amino acid sequences (87% for HYAL 1 and 85% for HYAL 2) were observed with the same enzyme from wasp Polished annularis and lower identities with that from wasps Vespula vulgaris, Dolichovespula maculata and from the bees Apis cerana cerana. The HYAL 1 protein fragment was shown to be richer in the amino acids Gly, Asn and Lys, while HYAL 2 in Phe, Ser and Ile amino acids. A common characteristic of the wasp venom allergens is their identity with proteins from other organisms, as it was observed with the cDNA sequences obtained here, which presented 34% identity with a correlated protein of the human bladder cancer progression. These results, although preliminaries indicate that the hyaluronidase is a quite conserved allergen and also they provide important subsidies for the study of the immunological cross reactivity between the bee and wasp venom, which is important for patients with multiple sensibility to the stings from these insects.