An 88-kDa protein of Plasmodium falciparum is related to the band-3-binding domain of human erythrocyte ankyrin

Eur J Biochem. 1992 Jul 15;207(2):455-61. doi: 10.1111/j.1432-1033.1992.tb17071.x.

Abstract

Three tryptic-peptide sequences of an 88-kDa pair of phosphoproteins of the malaria parasite Plasmodium falciparum were determined. They exhibit a striking similarity to corresponding sequences of the 89-kDa domain of human erythrocyte ankyrin. [35S]Methionine labeling of the two proteins demonstrated their parasitic origin. Using an appropriate oligonucleotide probe, Southern-blot analysis of genomic malaria DNA and Northern-blot analysis of malaria RNA suggest the existence of ankyrin-related sequences in the parasite genome and the presence of an ankyrin-related transcript of about 3.2 kb. Our studies provide further evidence of malaria-specific analogues of host-cell proteins, implying an unusual kind of parasite/host interaction.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Anion Exchange Protein 1, Erythrocyte / metabolism*
  • Ankyrins
  • Base Sequence
  • Blood Proteins / metabolism*
  • Gene Expression
  • Genes
  • Membrane Proteins / metabolism*
  • Molecular Sequence Data
  • Molecular Weight
  • Oligonucleotide Probes / chemistry
  • Peptide Mapping
  • Phosphoproteins / chemistry*
  • Phosphoproteins / metabolism
  • Plasmodium falciparum / chemistry*
  • Protein Processing, Post-Translational
  • Protozoan Proteins / chemistry*
  • Protozoan Proteins / metabolism
  • RNA, Messenger / genetics
  • Sequence Alignment

Substances

  • Anion Exchange Protein 1, Erythrocyte
  • Ankyrins
  • Blood Proteins
  • Membrane Proteins
  • Oligonucleotide Probes
  • Phosphoproteins
  • Protozoan Proteins
  • RNA, Messenger