A functional analysis of a natural variant of intercellular adhesion molecule-1 (ICAM-1Kilifi)

被引：55

作者：

Craig, A

Fernandez-Reyes, D

Mesri, M

McDowell, A

Altieri, DC

Hogg, N

Newbold, C

机构：

[1] Molecular Parasitology Group, Institute of Molecular Medicine, John Radcliffe Hospital

[2] Boyer Center for Molecular Medicine, Yale University School of Medicine, New Haven, CT 06536-0812

[3] Leukocyte Adhesion Laboratory, Imp. Cancer Res. Fund Laboratories, London WC2A 3PX, Lincoln's Inn Fields

来源：

HUMAN MOLECULAR GENETICS | 2000年 / 9卷 / 04期

关键词：

D O I：

10.1093/hmg/9.4.525

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Intercellular adhesion molecule-1 (ICAM-1) is involved in a range of interactions both within the host and between the host and a number of pathogens. Recently we described a mutation within the coding region of the first N-terminal immunoglobulin-like domain of ICAM-1, present at high frequency within African populations, which increased the risk of cerebral malaria. To understand the mechanism by which such a polymorphism might be maintained despite counterselection by malaria, we have carried out functional assays using both forms of ICAM-1 as soluble Fc chimeric fusion proteins. ICAM-1(Kilifi) has reduced avidity for LFA-1 compared with ICAM-1(ref) and binding to soluble fibrinogen was completely abolished with the Kilifi variant. In Plasmodium falciparum adhesion assays, ITO4-A4u binding to ICAM-1(Kilifi) was reduced compared with binding to the reference form. These results allow for the possibility of balanced selection between the reference and Kilifi forms of ICAM-1 through modulation of inflammatory responses and indicate the existence of differences within ICAM-1-binding P.falciparum isolates which may be relevant to pathogenesis.

引用

页码：525 / 530

页数：6

共 41 条

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