Arginine aminopeptidase, an integral membrane protein of the Cryptosporidium parvum sporozoite.
AUTOR(ES)
Okhuysen, P C
RESUMO
Cryptosporidium parvum oocysts were studied for the expression of aminopeptidase by using amino acids bound to the synthetic fluorescent substrate 7-amino-4-trifluoromethyl coumarin. After 1 h of incubation, intact oocysts showed no activity; however, homogenization and solubilization with Triton X-114 followed by phase separation yielded a 22-fold increase in aminopeptidase activity in the detergent fraction. With arginyl-6-amino-2-styrylquinoline as a substrate, aminopeptidase activity was observed in permeabilized oocysts and freshly excysted sporozoites but not on intact oocysts or empty oocyst membranes after excystation. These results suggest that C. parvum expresses an arginine aminopeptidase that is an integral protein of the sporozoite membrane.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=303163Documentos Relacionados
- Characterization of an Intestinal Epithelial Cell Receptor Recognized by the Cryptosporidium parvum Sporozoite Ligand CSL
- Identification and initial characterization of five Cryptosporidium parvum sporozoite antigen genes.
- Identification of isolate-specific sporozoite proteins of Cryptosporidium parvum by two-dimensional gel electrophoresis.
- Cryptosporidium parvum (Apicomplexa: Cryptosporidiidae) oocyst and sporozoite antigens recognized by bovine colostral antibodies.
- Cryptosporidium parvum Apical Complex Glycoprotein CSL Contains a Sporozoite Ligand for Intestinal Epithelial Cells