Rapid clearance of malaria circumsporozoite protein (CS) by hepatocytes.

Abstract

The circumsporozoite protein (CS) covers uniformly the plasma membrane of malaria sporozoites. In vitro, CS multimers bind specifically to regions of the hepatocyte plasma membrane that are exposed to circulating blood in the Disse space. The ligand is in the region II-plus of CS, an evolutionarily conserved stretch of the protein that has amino acid sequence homology to a cell adhesive motif of thrombospondin. We have now found that intravenously injected CS constructs bind rapidly to the basolateral surface of hepatocytes, provided that the recombinant proteins contain region II-plus, and that they are aggregated. Significant amounts of CS were not retained in any other organ. The striking parallelism between these in vitro and in vivo findings with the target specificity of malaria sporozoites, reinforces the hypothesis that the attachment of the parasites to hepatocytes is via region II-plus of CS.

• Authors: C Cerami, U Frevert, P Sinnis, B Takacs, V Nussenzweig
• Journal: The Journal of experimental medicine (J Exp Med) Vol. 179 Issue 2 Pg. 695-701 (Feb 01 1994) ISSN: 0022-1007 [Print] United States
• PMID: 8294876 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, Non-P.H.S., Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Protozoan Proteins
• Recombinant Proteins
• circumsporozoite protein, Protozoan

Topics

• Amino Acid Sequence
• Animals
• Cells, Cultured
• Chromatography, Affinity
• Injections, Intravenous
• Liver (cytology, metabolism)
• Male
• Mice
• Mice, Inbred BALB C
• Microvilli (metabolism)
• Molecular Sequence Data
• Protozoan Proteins (administration & dosage, metabolism)
• Recombinant Proteins (administration & dosage, metabolism)