Abstract:
:Amebic cysteine protease 2 (EhCP2) was purified from ethyl ether extracts of axenically grown trophozoites of Entamoeba histolytica strain HM1-IMSS. The purification procedure involved molecular filtration and electroelution. Sequence analysis of the purified product revealed EhCP2 and ubiquitin(s). Electrophoretic migration patterns, isoelectric point determination and Western blot studies failed to reveal other EhCP molecules. Polyclonal antibodies against the purified EhCP2 prepared in rabbits either stabilized or enhanced the enzyme activity in a dose-response manner. Purified EhCP2 was enclosed within inert resin microspheres (22-44 microm in diameter) and injected into the portal vein of normal hamsters. In the liver, the microspheres caused mild acute inflammation and occasional minimal necrosis of short duration. Sections of the liver were immunohistochemically stained with the anti-EhCP2 antibody and the microspheres were positive for only a very short period (1 h) after injection. Sections of experimental acute (1 day, 5 days) amebic liver abscess produced in hamsters were also stained with the anti-EhCP2 antibody; and amebas were intensely positive but no staining was observed at any time in the surrounding necrotic structures. It is suggested that EhCP2 plays either a minor or no role in the causation of tissue damage in experimental acute liver amebiasis.
journal_name
Parasitol Resjournal_title
Parasitology researchauthors
Olivos-García A,González-Canto A,López-Vancell R,García de León Mdel C,Tello E,Nequiz-Avendaño M,Montfort I,Pérez-Tamayo Rdoi
10.1007/s00436-002-0763-8subject
Has Abstractpub_date
2003-06-01 00:00:00pages
212-20issue
3eissn
0932-0113issn
1432-1955journal_volume
90pub_type
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