Objective: To explore the invading mechanism of amebae in lamina porpria and observe the interaction between the cysteine proteinase (CP) of Entamoeba histolytica and laminin.
Methods: CP was identified by laminin-sepharose affinity chromatography, followed by isolation, purification and inhibitor experiment. The hydrolytic activity was measured by gelatin electrophoresis.
Results: Purified CP of E. histolytica showed a strong affinity with laminin. The molecular weight of CP is 27 kDa. It can be inhibited by EC-64 and exhibited a protein hydrolytic activity.
Conclusion: The specific affinity and hydrolytic activity of CP might play an important role in its invasion to the basement membrane of intestinal mucosa.