Leucine-rich repeats in host-pathogen interactions
- Author(s)
- Kedzierski, L; Montgomery, J; Curtis, J; Handman, E;
- Details
- Publication Year 2004-03-01,Volume 52,Issue #2,Page 104-112
- Journal Title
- ARCHIVUM IMMUNOLOGIAE ET THERAPIAE EXPERIMENTALIS
- Publication Type
- Journal Article
- Abstract
- Leucine-rich repeats (LRRs) are versatile binding motifs found in a variety of proteins and are involved in protein-protein interactions. The LRR domain is composed of repeats forming a characteristic solenoid horse-shoe structure, which provides a scaffold for numerous insertions involved in binding to pathogen-associated molecular patterns and surface receptors. LRRs have been shown to be involved in the host defense systems of both plants (resistance genes) and mammals (Toll-like receptors and nucleotide-binding oligomerisation domain proteins), where they sense specific pathogen-associated molecules and activate the innate immune system. Paradoxically, LRRs have also been shown to be part of microbial virulence factors involved in the interaction with host cells and establishment of infection. The potential of LRRs to bind a vast array of structurally unrelated ligands and their well-documented involvement in microbial pathogenesis make them a potential target for vaccines and new drugs. The recent identification of LRRs in the obligate intracellular protozoan parasite Leishmania and their participation in the macrophage-parasite interaction have added new insight into the role of LRRs in the host cell invasion.
- Publisher
- INST IMMUNOLOGY & EXPERIMENTAL THERAPY
- Keywords
- TOLL-LIKE RECEPTORS; LEISHMANIA-MAJOR PROTEOPHOSPHOGLYCAN; INTEGRIN MAC-1 CD11B/CD18; GLYCOPROTEIN IB-ALPHA; LAMBLIA CYST WALL; LISTERIA-MONOCYTOGENES; INNATE IMMUNITY; YERSINIA-PESTIS; EXPRESSION SITE; RIBONUCLEASE INHIBITOR
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- Refer to copyright notice on published article.
Creation Date: 2004-03-01 12:00:00