Heterologous expression and mutagenesis of recombinant Vespa affinis hyaluronidase protein (rVesA2).

ABSTRACT:

Background

Crude venom of the banded tiger waspVespa affinis contains a variety of enzymes including hyaluronidases, commonly known as spreading factors.

Methods

The cDNA cloning, sequence analysis and structural modelling of V. affinis venom hyaluronidase (VesA2) were herein described. Moreover, heterologous expression and mutagenesis of rVesA2 were performed.

Results

V. affinis venom hyaluronidase full sequence is composed of 331 amino acids, with four predicted N-glycosylation sites. It was classified into the glycoside hydrolase family 56. The homology modelling exhibited a central core (α/β)₇ composed of Asp107 and Glu109, acting as the catalytic residues. The recombinant protein was successfully expressed in E. coli

SUBMITTER: Rungsa P 

PROVIDER: S-EPMC6892566 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature