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Purified monomeric ligand.MD-2 complexes reveal molecular and structural requirements for activation and antagonism of TLR4 by Gram-negative bacterial endotoxins
Journal article   Peer reviewed

Purified monomeric ligand.MD-2 complexes reveal molecular and structural requirements for activation and antagonism of TLR4 by Gram-negative bacterial endotoxins

Theresa L. Gioannini, Athmane Teghanemt, DeSheng Zhang, Gregory Esparza, Liping Yu and Jerrold Weiss
Immunologic research, Vol.59(1-3), pp.3-11
08/01/2014
DOI: 10.1007/s12026-014-8543-y
PMCID: PMC4125468
PMID: 24895101

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Abstract

A major focus of work in our laboratory concerns the molecular mechanisms and structural bases of Gram-negative bacterial endotoxin recognition by host (e.g., human) endotoxin-recognition proteins that mediate and/or regulate activation of Toll-like receptor (TLR) 4. Here, we review studies of wild-type and variant monomeric endotoxin.MD-2 complexes first produced and characterized in our laboratories. These purified complexes have provided unique experimental reagents, revealing both quantitative and qualitative determinants of TLR4 activation and antagonism. This review is dedicated to the memory of Dr. Theresa L. Gioannini (1949-2014) who played a central role in many of the studies and discoveries that are reviewed.
Immunology Life Sciences & Biomedicine Science & Technology

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