Proteolytic processing of the Plasmodium falciparum merozoite surface protein-1 produces a membrane-bound fragment containing two epidermal growth factor-like domains

Mol Biochem Parasitol. 1991 Nov;49(1):29-33. doi: 10.1016/0166-6851(91)90127-r.

Abstract

The amino-terminal sequence has been obtained for 2 fragments of the Plasmodium falciparum T9/94 merozoite surface protein precursor (PfMSP1) and these have been compared with the sequence predicted from the gene. These data define the position of these fragments in the precursor and indicate that the C-terminal sequence which is carried into the red cell during invasion consists of 2 epidermal growth factor (EGF)-like domains. A homologous cleavage sequence and domain structure can be identified in the MSP1 molecules of other malarial species. In addition the results suggest that the smaller fragment is not N-glycosylated.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cell Membrane / metabolism
  • DNA, Protozoan / genetics
  • Epidermal Growth Factor / metabolism
  • Merozoite Surface Protein 1
  • Molecular Sequence Data
  • Peptide Fragments / metabolism
  • Peptide Hydrolases / metabolism
  • Plasmodium falciparum / genetics
  • Plasmodium falciparum / metabolism*
  • Protein Precursors / genetics
  • Protein Precursors / metabolism*
  • Protein Processing, Post-Translational
  • Protozoan Proteins / genetics
  • Protozoan Proteins / metabolism*
  • Sequence Homology, Nucleic Acid

Substances

  • DNA, Protozoan
  • Merozoite Surface Protein 1
  • Peptide Fragments
  • Protein Precursors
  • Protozoan Proteins
  • Epidermal Growth Factor
  • Peptide Hydrolases

Associated data

  • GENBANK/M61207
  • GENBANK/M61208
  • GENBANK/M64681
  • GENBANK/M64715
  • GENBANK/S74964
  • GENBANK/S74965
  • GENBANK/S74966
  • GENBANK/S75016
  • GENBANK/S77612
  • GENBANK/S77767
  • GENBANK/S78950