%0 Journal Article %A Mansur, Fariha Jasin %A Takahara, Sari %A Yamamoto, Mihoko %A Shimatani, Masafumi %A Karim, Mohammad Minnatul %A Noiri, Yuichiro %A Ebisu, Shigeyuki %A Azakami, Hiroyuki %D 2017 %T Purification and characterization of hemolysin from periodontopathogenic bacterium Eikenella corrodens strain 1073 %U https://tandf.figshare.com/articles/journal_contribution/Purification_and_characterization_of_hemolysin_from_periodontopathogenic_bacterium_i_Eikenella_corrodens_i_strain_1073/4986347 %R 10.6084/m9.figshare.4986347.v1 %2 https://ndownloader.figshare.com/files/8393840 %K Eikenella corrodens %K hemolysis %K purification %K virulence, periodontal disease %X

Eikenella corrodens 1073 was found to show hemolytic activity when grown on sheep blood agar. A high and dose-dependent hemolytic activity was detected in the cell envelope fraction, which was further purified by ion-exchange and gel-filtration chromatography. Consequently, a 65-kDa protein with hemolytic activity was obtained, suggesting that this protein might be a hemolysin. Its N-terminal amino acid sequence was nearly identical to that of X-prolyl aminopeptidase from E. corrodens ATCC 23834. To confirm that X-prolyl aminopeptidase functions as a hemolytic factor, we expressed the hlyA gene, encoding X-prolyl aminopeptidase, in Escherichia coli. After induction with isopropyl β-D-1-thiogalactopyranoside, a protein of about 65 kDa was purified on a Ni column, and its hemolytic activity was confirmed. Meanwhile, a strain with a disrupted hlyA gene, which was constructed by homologous recombination, did not show any hemolytic activity. These results suggested that X-prolyl aminopeptidase might function as a hemolysin in E. corrodens.

Eikenella corrodens 1073 showed hemolytic activity when grown on sheep blood agar. We purified and identified the hemolytic factor.

%I Taylor & Francis