Expression of functional D299G.T399I polymorphic variant of TLR4 depends more on coexpression of MD-2 than does wild-type TLR4

J Immunol. 2010 Apr 15;184(8):4362-7. doi: 10.4049/jimmunol.0903142. Epub 2010 Mar 8.

Abstract

Two missense variants (D299G and T399I) of TLR4 are cosegregated in individuals of European descent and, in a number of test systems, result in reduced responsiveness to endotoxin. How these changes within the ectodomain (ecd) of TLR4 affect TLR4 function is unclear. For both wild-type and D299G.T399I TLR4, we used endotoxinCD14 and endotoxinMD-2 complexes of high specific radioactivity to measure: 1) interaction of recombinant MD-2TLR4 with endotoxinCD14 and TLR4 with endotoxinMD-2; 2) expression of functional MD-2TLR4 and TLR4; and 3) MD-2TLR4 and TLR4-dependent cellular endotoxin responsiveness. Both wild-type and D299G.T399I TLR4(ecd) demonstrated high affinity (K(d) approximately 200 pM) interaction of endotoxinCD14 with MD-2TLR4(ecd) and endotoxinMD-2 with TLR4(ecd). However, levels of functional TLR4 were reduced up to 2-fold when D299G.T399I TLR4 was coexpressed with MD-2 and >10-fold when expressed without MD-2, paralleling differences in cellular endotoxin responsiveness. The dramatic effect of the D299G.T399I haplotype on expression of functional TLR4 without MD-2 suggests that cells expressing TLR4 without MD-2 are most affected by these polymorphisms.

Publication types

  • Comparative Study
  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Substitution / genetics
  • Amino Acid Substitution / immunology
  • Cell Line
  • Dose-Response Relationship, Immunologic
  • Endotoxins / metabolism
  • Endotoxins / pharmacology
  • Genetic Variation* / immunology
  • Haplotypes
  • Humans
  • Lipopolysaccharides / metabolism
  • Lipopolysaccharides / pharmacology
  • Lymphocyte Antigen 96 / biosynthesis
  • Lymphocyte Antigen 96 / genetics*
  • Lymphocyte Antigen 96 / metabolism
  • Mutation, Missense* / immunology
  • Polymorphism, Genetic* / immunology
  • Protein Binding / genetics
  • Protein Binding / immunology
  • Protein Structure, Tertiary / genetics
  • Toll-Like Receptor 4 / agonists
  • Toll-Like Receptor 4 / biosynthesis
  • Toll-Like Receptor 4 / genetics*
  • Toll-Like Receptor 4 / metabolism

Substances

  • Endotoxins
  • LY96 protein, human
  • Lipopolysaccharides
  • Lymphocyte Antigen 96
  • TLR4 protein, human
  • Toll-Like Receptor 4
  • lipid-linked oligosaccharides