[Identification of the binding site on ICAM-1 for red blood cells infected by Plasmodium falciparum]

Zhongguo Ji Sheng Chong Xue Yu Ji Sheng Chong Bing Za Zhi. 2002;20(3):129-32.
[Article in Chinese]

Abstract

Objective: To identify the binding site on ICAM-1 to PRBCs in order to explore anti-adhesive agent against cerebral malaria.

Methods: Monoclonal antibody 15.2 against ICAM-1 domain 1 was chosen as target molecule to screen mimetic peptides of ICAM-1 from a 12-mer random peptide library. Three rounds of biopanning were carried out and then ELISA, competitive ELISA, dot-ELISA and Western blotting were used to evaluate the binding character between phage-borne peptides and McAb 15.2. The insert DNA sequences of positive clones were determined and their amino acid sequences were deduced.

Results: Thirty clones from the third round were randomly selected, and 26 of them were found positive by sandwich ELISA. The competitive ELISA test proved that most phage-borne peptides could competitively inhibit the binding of antibody (15.2 McAb) with ICAM-1. Analysis of DNA and amino acid sequences indicated that over a half positive phage clones expressed 12-mer peptide KLYLIAEGSVAA. Comparison of peptide K(XX) L(XXX) GSV with the 64-73 aa of primary sequence of ICAM-1 showed a 50% homogeneity.

Conclusion: These peptides displayed by phage may be analogs of ICAM-1, K..L...GSV probably plays a significant role on the binding reaction of ICAM-1 and PRBCs.

Publication types

  • English Abstract
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antibodies, Monoclonal
  • Binding Sites
  • Epitopes
  • Erythrocytes / parasitology
  • Erythrocytes / physiology*
  • Intercellular Adhesion Molecule-1 / physiology*
  • Peptide Library
  • Peptides / chemistry
  • Plasmodium falciparum / physiology*
  • Sequence Homology, Amino Acid

Substances

  • Antibodies, Monoclonal
  • Epitopes
  • Peptide Library
  • Peptides
  • Intercellular Adhesion Molecule-1