Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2015 May;180(2):165-77.
doi: 10.1111/cei.12578.

Single nucleotide polymorphisms of Toll-like receptors and susceptibility to infectious diseases

Affiliations
Review

Single nucleotide polymorphisms of Toll-like receptors and susceptibility to infectious diseases

C Skevaki et al. Clin Exp Immunol. 2015 May.

Abstract

Toll-like receptors (TLRs) are the best-studied family of pattern-recognition receptors (PRRs), whose task is to rapidly recognize evolutionarily conserved structures on the invading microorganisms. Through binding to these patterns, TLRs trigger a number of proinflammatory and anti-microbial responses, playing a key role in the first line of defence against the pathogens also promoting adaptive immunity responses. Growing amounts of data suggest that single nucleotide polymorphisms (SNPs) on the various human TLR proteins are associated with altered susceptibility to infection. This review summarizes the role of TLRs in innate immunity, their ligands and signalling and focuses on the TLR SNPs which have been linked to infectious disease susceptibility.

Keywords: SNPs; TLR proteins; infection; innate immunity.

PubMed Disclaimer

Figures

Fig 1
Fig 1
Toll-like receptor (TLR) proteins. GeneBank Accession numbers, chromosomal locations, number of amino acids and molecular weight for each of the TLR proteins are provided. The pictures above the TLRs depict their main known ligands.
Fig 2
Fig 2
Three-dimensional structure of Toll-like receptor (TLR) proteins. Block arrows show the main ligand for each TLR protein (single protein, homo- or heterodimer of two TLR proteins) as positioned on the protein. Dashed arrows show the positions of amino acids which change as a result of common single nucleotide polymorphisms (SNPs). The cell membrane and the intracellular domain is also depicted in the TLR-1/TLR-6 heterodimer.

References

    1. Medzhitov R, Janeway CA., Jr Innate immunity: the virtues of a nonclonal system of recognition. Cell. 1997;91:295–298. - PubMed
    1. Medzhitov R, Janeway C., Jr Innate immune recognition: mechanisms and pathways. Immunol Rev. 2000;173:89–97. - PubMed
    1. Hill AV. The genomics and genetics of human infectious disease susceptibility. Annu Rev Genomics Hum Genet. 2001;2:373–400. - PubMed
    1. Medzhitov R, Preston-Hurlburt P, Janeway CA., Jr A human homologue of the Drosophila Toll protein signals activation of adaptive immunity. Nature. 1997;388:394–397. - PubMed
    1. Lemaitre B, Nicolas E, Michaut L, Reichhart JM, Hoffmann JA. The dorsoventral regulatory gene cassette spatzle/Toll/cactus controls the potent antifungal response in Drosophila adults. Cell. 1996;86:973–983. - PubMed

MeSH terms

Substances