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2004 | 52 | 2 | 104-112
Article title

Leucine-rich repeats in host-pathogen interactions

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Languages of publication
EN
Abstracts
EN
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

Year
Volume
52
Issue
2
Pages
104-112
Physical description
Contributors
author
author
author
author
References
Document Type
ARTICLE
Publication order reference
Emanuela Handman, Division of Infection and Immunity, The Walter and Eliza Hall Institute of Medical Research, 1G Royal Pde, Parkville 3050, Victoria, Australia
Identifiers
YADDA identifier
bwmeta1.element.element-from-psjc-94532455-019d-3b68-a876-09d12e8ee642
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