Structure and function of a thymic peptide is mimicked by Plasmodium falciparum peptides

Ann Inst Pasteur Immunol. 1988 Sep-Oct;139(5):557-67. doi: 10.1016/0769-2625(88)90100-6.

Abstract

Numerous Plasmodium falciparum antigens contain repetitive amino acid sequences. Two blood stage antigens, Pf11-1 and Pf332, were characterized in our laboratories and present high cross-reactivities, defining a family of cross-reacting antigens. In this report, we show that amino acid sequence homologies might explain these cross-reactivities, but that they extend to polypeptides from the host, namely thymosin-alpha 1 (T alpha 1). An antiserum raised in chickens and Saimiri monkeys against the synthetic Pf11-1 peptide cross-reacts with synthetic T alpha 1. Synthetic Pf11-1 and Pf332 peptides share some of the biological activities of T alpha 1. These results are discussed with respect to the mechanisms devised by malaria parasites for escape from the host immune response.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antigens, Protozoan / immunology*
  • Antigens, Surface / analysis
  • Biological Assay
  • Cross Reactions
  • Enzyme-Linked Immunosorbent Assay
  • Mice
  • Molecular Sequence Data
  • Peptides / chemical synthesis
  • Peptides / immunology
  • Plasmodium falciparum / immunology*
  • Rosette Formation
  • Thy-1 Antigens
  • Thymalfasin
  • Thymosin / analogs & derivatives*
  • Thymosin / immunology

Substances

  • Antigens, Protozoan
  • Antigens, Surface
  • Peptides
  • Thy-1 Antigens
  • Thymosin
  • Thymalfasin