Abstract
Lysins are capable of disrupting mammalian cell membranes by specifically binding to membrane components. Lysin can be a protein, a peptide or a glycoside. Certain lysins, called hemolysins, can disintegrate mammalian erythrocytes. A few of the reported lysins can bind to specific glycan structures. Here we report, for the first time, a glycan‐binding hemolysin (named Hemolysin‐X or HelyX) from a flowering plant. HelyX was purified by ammonium sulfate precipitation, size exclusion chromatography and high performance liquid chromatography (HPLC). Activity and ligand binding properties of HelyX were studied by plate based assays and spectrophotometric analysis. Interactions of HelyX with mammalian and fungal cells were studied through microscopy and flow cytometry. HelyX showed rapid and robust hemolytic activities even at a very low concentration. The molecular weight of this hemolysin is 2 kDa. Hemolysis by HelyX was completely inhibited by serum glycoproteins (Fetuin, asialofetuin, thyroglobulin and fibrinogen) and cholesterol. Interestingly, the hemolysins of cholera bacteria were reported to show similar binding specificities. When tested with colon and breast cancer cell lines, HelyX showed significant apoptotic activities. The hemolysin also inhibited the growth of yeast cells.Support or Funding InformationMichigan Technological University
Published Version
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