Methionine 156 in the immunodominant domain of CD36 contributes to define the epitope recognized by the NL07 MoAb

CD36 is a membrane glycoprotein expressed by several cell types, and play a role as a receptor for different physiological and pathological ligands. An immunodominant domain of CD36 has been described in the amino acidic region 155-183, where many ligands and monoclonal antibodies (MoAbs) react. MoA...

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Bibliographic Details
Published in:Molecular and cellular biochemistry 2000-11, Vol.214 (1-2), p.89-95
Main Authors: Gruarin, P, Ulliers, D, Thorne, R F, Alessio, M
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino Acid Substitution
Animals
Antibodies, Monoclonal
Base Sequence
CD36 Antigens - chemistry
CD36 Antigens - genetics
COS Cells
DNA Primers - genetics
Erythrocytes
Humans
Immunodominant Epitopes - chemistry
Immunodominant Epitopes - genetics
In Vitro Techniques
Malaria
Malaria, Falciparum - immunology
Methionine - chemistry
Mice
Parasites
Plasmodium falciparum
Point Mutation
Protein Structure, Tertiary
Proteins
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - immunology
Transfection
Vector-borne diseases
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Summary:CD36 is a membrane glycoprotein expressed by several cell types, and play a role as a receptor for different physiological and pathological ligands. An immunodominant domain of CD36 has been described in the amino acidic region 155-183, where many ligands and monoclonal antibodies (MoAbs) react. MoAbs against CD36 have proved useful in structural as well as functional studies. One of these antibodies, MoAb NL07, recognizes a conformational epitope that is acquired in the late steps of the CD36 maturation. The NL07 epitope appears to be functionally relevant and blocks CD36-mediated binding to red blood cells infected with the malaria parasite Plasmodium falciparum (IRBC). In this work a mutant COS-7 clone expressing NL07-negative CD36 molecules on the cell surface was investigated. In the mutant, the methionine in position 156 of the wild type CD36 sequence was replaced by a valine. It was determined that methionine 156 was essential for NL07 reactivity, mapping the NL07 epitope to the vicinity of the functionally important immunodominant domain (aa 155-183) of CD36. Although methionine 156 is located in this region, the CD36V156 mutated molecule was apparently functional and able to bind IRBC and oxidized LDL.
ISSN:0300-8177
1573-4919
DOI:10.1023/A:1007147101640