Full-text resources of PSJD and other databases are now available in the new Library of Science.
Visit https://bibliotekanauki.pl

PL EN


Preferences help
enabled [disable] Abstract
Number of results
2004 | 52 | 2 | 104-112

Article title

Leucine-rich repeats in host-pathogen interactions

Title variants

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.

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
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.