Journal
GENE
Volume 547, Issue 2, Pages 338-345Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.gene.2014.06.045
Keywords
Hyaluronidases; Cloning and molecular characterization; Noncoding isoforms; Buthus martensi
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Funding
- National Natural Science Foundation of Henan [12B35002]
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Hyaluronidase is a common component of scorpion venom and has been considered as spreading factor that promotes a fast penetration of the venom in the anaphylactic reaction. In the current study, a novel full-length of hyaluronidase BmHYI and three noncoding isoforms of BmHYII, BmHYIII and BmHYIV were cloned by using a combined strategy based on peptide sequencing and Rapid Amplification of cDNA Ends (RACE). BmHYI has 410 amino acid residues containing the catalytic, positional and five potential N-glycosylation sites. The deduced protein sequence of BmHYI shares significant identity with venom hyaluronidases from bees and snakes. The phylogenetic analysis showed early divergence and independent evolution of BmHYI from other hyaluronidases. An extraordinarily high level of sequence similarity was detected among four sequences. But, BmHYII BmHYIII and BmHYIV were short of stop-codon in the open reading frame and poly(A) signal in the 3' end. (C) 2014 Elsevier B.V. All rights reserved.
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