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PMID: 7509756 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Plasmodium falciparum: pfalhesin and CD36 form an adhesin/receptor pair that is responsible for the pH-dependent portion of cytoadherence/sequestration.

Experimental parasitology ·Vol. 78 ·No. 2 ·1994-03-00 ·Pages 203-9

Crandall I, Land KM, Sherman IW

Abstract

The cytoadherent behavior of two Plasmodium falciparum (human malaria) cell lines, FCR-3 and ITO4 (a cell line with elevated ICAM-1 adherence), was studied using CHO cells transfected with CD36 or ICAM-1 receptors as target cells. ICAM-1-mediated adherence was found to be relatively pH insensitive, whereas CD36-mediated adherence was pH sensitive and inhibited by monoclonal antibodies and peptides based on a region found in human band 3 protein and named pfalhesin. Immobilized pfalhesin was used as an affinity matrix to purify CD36 from extracts of C32 amelanotic melanoma cells, which have ICAM-1 as well as CD36 receptors, and bind both parasite cell lines. We conclude that pfalhesin and CD36 constitute an adhesin/receptor pair.

MeSH Terms
Amino Acid Sequence Animals Anion Exchange Protein 1, Erythrocyte/physiology Antigens, CD/physiology CD36 Antigens CHO Cells Cell Adhesion Cell Adhesion Molecules/physiology Cricetinae Erythrocytes/parasitology Humans Hydrogen-Ion Concentration Immunoblotting Intercellular Adhesion Molecule-1 Melanoma, Amelanotic Molecular Sequence Data Plasmodium falciparum/physiology Tumor Cells, Cultured
Chemicals
Anion Exchange Protein 1, Erythrocyte Antigens, CD CD36 Antigens Cell Adhesion Molecules pfalhesin Intercellular Adhesion Molecule-1
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Crandall I
Department of Biology, University of California, Riverside 92521.
Land K M
Sherman I W
Article Info
Journal
Experimental parasitology
Abbr.
Exp Parasitol
ISSN
0014-4894
Published
1994-03-00
Pages
203-9
Language
English
Region
United States
NLM ID
0370713
Subset
IM
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