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Parasitophorous vacuole membrane of Plasmodium knowlesi

Conference · · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:6943182

The authors have evaluated the occurrence of host cell membrane protein and parasite protein in the vacuolar membrane (VM) of isolated parasites. Parasites were labeled by incorporation of (/sup 35/S)methionine and by lactoperoxidase-catalyzed /sup 125/I iodination. Of the two prominent /sup 125/I-labeled components, one, not detected by metabolic labeling corresponded in M/sub r/ to erythrocyte band 3 (90 kDa). Trypsinization of radioiodinated parasites for 5' or 20' yield a 35 kDa fragment, not seen in untreated samples and compatible with the trypsin degradation of band 3 from the cytoplasmic side. Tryptic peptide maps of the 35 kDa revealed a very acidic peptide corresponding to the highly anionic tryptic peptide of band 3 showed by others. The second prominent /sup 125/I-labeled VM protein had an M/sub r/ 74,000 corresponding to a protein metabolically labeled with (/sup 35/S)methionine, suggesting it is inserted into the VM by the parasites. Several less prominent proteins labeling with both (/sup 35/S)methionine and /sup 125/I were also detected (140 kDa, 55 kDa, 45 kDa). A faint /sup 125/I-labeled triple (220-230 kDa) is compatible with a trace amounts of spectrin, usually a prominent component of red cell membrane. The results indicate that host cell band 3 is a prominent component of the VM, but that this membrane also contains several parasite-synthesized proteins.

Research Organization:
Tufts-New England Medical Center, Boston, MA
OSTI ID:
6943182
Report Number(s):
CONF-8606151-
Journal Information:
Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States), Journal Name: Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States) Vol. 45:6; ISSN FEPRA
Country of Publication:
United States
Language:
English