Plasmodium berghei and Plasmodium chabaudi: A neutral endopeptidase in parasite extracts and plasma of infected animals |
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| Institution: | 1. Laboratoire de Biologie Cellulaire, U.A. CNRS No. 290, Université de Poitiers, 40 Avenue du Recteur Pineau, 86022 Poitiers Cédex, France;2. Laboratoire de Biochimie Cellulaire et Moléculaire des Glycoconjugués, Centre de Biophysique Moléculaire, CNRS et Université d''Orléans, 1 rue Haute, 45071 Orléans Cédex 2, France;1. Princess of Wales Hospital, Coity Road, Bridgend CF31 1RQ, UK;2. Neath Port Talbot Hospital, Port Talbot SA12 8YL, UK;1. Department of Civil Engineering, Sharda University, Greater Noida 201310, India;2. Department of Architecture, Axis institute of Architecture, Kanpur 209402, India;1. Department of Medicine, Yong Loo Lin School of Medicine, National University of Singapore, Singapore;2. Christchurch Heart Institute, University of Otago, New Zealand;3. Heart Failure and Cardiac Regeneration (ICREC) Research Program, Health Science Research Institute Germans Trias i Pujol (IGTP), Badalona, Spain;4. Centro de Investigación Biomédica en Red Enfermedades Cardiovasculares (CIBERCV), Spain;5. Heart Failure Clinic, Cardiology Service, Hospital Universitari Germans Trias i Pujol Badalona, Barcelona, Spain;6. Biochemistry Service, Hospital Universitari Germans Trias I Pujol, Badalona, Spain;7. Cardiovascular Research Institute, National University Health System, Singapore;8. Department of Biological Sciences, National University of Singapore, Singapore;1. Bioactive Natural Products Laboratory, Department of Biochemistry, Biological Sciences Institute, Federal University of Juiz de Fora, Juiz de Fora, MG Brazil;2. Department of Parasitology, Microbiology and Immunology, Biological Sciences Institute, Federal University of Juiz de Fora, Juiz de Fora, MG Brazil |
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| Abstract: | By using a sensitive fluorometric method with Val-Leu-Gly-Arg-3-amino-9-ethylcarbazole (VLGR-AEC) as a substrate, two endopeptidase activities were identified in two fractions of Sephacryl S-200 gel filtration from soluble P. berghei and P. chabaudi extracts. Controls with normal mouse erythrocytes, with leukocytes, and with reticulocyte enriched blood and different washing procedures during the preparation of soluble P. berghei extracts showed that the MW >200 kDa fraction was a contaminant from erythrocytes and exhibited an optimal pH activity of 8.2. In contrast, the fraction 130 kDa was related to P. berghei and P. chabaudi and exhibited an optimal pH activity of 7.4. The two enzyme activities were compared with eight different substrates. The parasite endopeptidase showed a strong activity with Val-Leu-Gly-Lys-AEC (VLGK-AEC) and Ser-Gly-Lys-AEC (SGK-AEC) as substrates; in contrast, the mouse host endopeptidase poorly cleaved the VLGK-AEC and did not cleave SGK-AEC. Presence of the hydrophobic benzyl group on serine reduced the hydrolizing properties of P. berghei endopeptidase: the reverse was observed with host endopeptidase. The hydrolysis of the N-polyhydroxyalcanoyl-VLGK-AEC substrate by the parasite neutral endopeptidase strongly increased with the schizogonic stage, as shown with synchronized P. chabaudi in mice. By its physiological pH and specificity the release of this enzyme in mouse plasma during the infection could be of interest in a peptidyl-drug Strategy. |
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