Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 89-95 |
| Number of pages | 7 |
| Journal | Molecular and Cellular Biochemistry |
| Volume | 214 |
| Issue number | 1-2 |
| Publication status | Published - 2000 |
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Keywords
- CD36
- Malaria
- MoAb epitope
ASJC Scopus subject areas
- Clinical Biochemistry
- Molecular Biology
- Genetics
- Cell Biology
Cite this
Methionine 156 in the immunodominant domain of CD36 contributes to define the epitope recognized by the NL07 MoAb. / Gruarin, P.; Ulliers, D.; Thome, R. F.; Alessio, M.
In: Molecular and Cellular Biochemistry, Vol. 214, No. 1-2, 2000, p. 89-95.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Methionine 156 in the immunodominant domain of CD36 contributes to define the epitope recognized by the NL07 MoAb
AU - Gruarin, P.
AU - Ulliers, D.
AU - Thome, R. F.
AU - Alessio, M.
PY - 2000
Y1 - 2000
N2 - 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.
AB - 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.
KW - CD36
KW - Malaria
KW - MoAb epitope
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UR - http://www.scopus.com/inward/citedby.url?scp=0034541606&partnerID=8YFLogxK
M3 - Article
C2 - 11195795
AN - SCOPUS:0034541606
VL - 214
SP - 89
EP - 95
JO - Molecular and Cellular Biochemistry
JF - Molecular and Cellular Biochemistry
SN - 0300-8177
IS - 1-2
ER -