Specific high affinity interactions of monomeric endotoxin.protein complexes with Toll-like receptor 4 ectodomain.

Specific high affinity interactions of monomeric endotoxin.protein complexes with Toll-like receptor 4 ectodomain. Research Abstract Details 

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Specific high affinity interactions of monomeric endotoxin.protein complexes with Toll-like receptor 4 ectodomain. Abstract Text:

Polonca Prohinar,Fabio Re,Richard Widstrom,DeSheng Zhang,Athmane Teghanemt,Jerrold P Weiss,Theresa L Gioannini,

Potent Toll-like receptor 4 (TLR4) activation by endotoxin has been intensely studied, but the molecular requirements for endotoxin interaction with TLR4 are still incompletely defined. Ligand-receptor interactions involving endotoxin and TLR4 were characterized using monomeric endotoxin.protein complexes of high specific radioactivity. The binding of endotoxin.MD-2 to the TLR4 ectodomain (TLR4ECD) and transfer of endotoxin from CD14 to MD-2/TLR4ECD were demonstrated using HEK293T-conditioned medium containing TLR4ECD+/-MD-2. These interactions are specific, of high affinity (KD<300 pm), and consistent with the molecular requirements for potent cell activation by endotoxin. Both reactions result in the formation of a Mr approximately 190,000 complex composed of endotoxin, MD-2, and TLR4ECD. CD14 facilitates transfer of endotoxin to MD-2 (TLR4) but is not a stable component of the endotoxin.MD-2/TLR4 complex. The ability to assay specific high affinity interactions of monomeric endotoxin.protein complexes with TLR4ECD should allow better definition of the structural requirements for endotoxin-induced TLR4 activation.

Specific high affinity interactions of monomeric endotoxin.protein complexes with Toll-like receptor 4 ectodomain. Publishing Authors By Initials

P Prohinar,F Re,R Widstrom,D Zhang,A Teghanemt,JP Weiss,TL Gioannini,

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Specific high affinity interactions of monomeric endotoxin.protein complexes with Toll-like receptor 4 ectodomain. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: The Journal of biological chemistry

VOLUME: 282

Page Numbers: 1010-7

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 22

MONTH: 11

YEAR: 2006

Specific high affinity interactions of monomeric endotoxin.protein complexes with Toll-like receptor 4 ectodomain. Information

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LANGUAGE: eng

NlmUniqueID: 2985121

Specific high affinity interactions of monomeric endotoxin.protein complexes with Toll-like receptor 4 ectodomain. Keywords Mesh Terms:

KEYWORDS: Tritium

MESH TERMS: diagnostic use

Chemical & Substance for Abstract: Specific high affinity interactions of monomeric endotoxin.protein complexes with Toll-like receptor 4 ectodomain. Information

Substance Name: Tritium

Registry Number: 10028-17-8

Grant and Affiliation Information for Specific high affinity interactions of monomeric endotoxin.protein complexes with Toll-like receptor 4 ectodomain.

AFFILIATION: Inflammation Program, Department of Internal Medicine, Roy J. and Lucille A. Carver College of Medicine, University of Iowa, and Veterans Affairs Medical Center, Iowa City, Iowa 52242, USA.

Country: United States

AGENCY: United States NIAID

GRANT: R21 AI54665

ACRONYM: AI

MEDLINETA: J Biol Chem

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