The aim of this study was to clone, express the gene of Hgp44 in adhesin domains of gingipains from Porphyromonas gingivalis and purify the protein. Furthermore, the effect of Hgp44 from P. gingivalis on inducing HUVECs to secrete IL-6 and IL-8 was evaluated. The Hgp44 gene fragment was amplified by polymerase chain reaction, and then inserted into the cloning vector pMD18-T and linked with a prokaryotic expression vector pET22b to construct the recombinant expression plasmid pET22b-Hgp44.
Escherichia coli is the most widely used host for the production of recombinant proteins. However, most eukaryotic proteins are typically obtained as insoluble, misfolded inclusion bodies that need solubilization and refolding. The interactions between human FHL2 protein and many types of proteins, including structural proteins, kinases, and several classes of transcription factor, have been found to have important roles in a variety of fundamental processes, including arrhythmia, hypertrophy, atherosclerosis, and angiogenesis.