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Cited by 956

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

Toll-like receptors 9 and 3 as essential components of innate immune defense against mouse cytomegalovirus infection

Open access
Tabeta, Koichi, Georgel, Philippe, Janssen, Edith, Du, Xin, Hoebe, Kasper, Crozat, Karine, Mudd, Suzanne, Shamel, Louis, Sovath, Sosathya, Goode, Jason, Alexopoulou, Lena, Flavell, Richard A., Beutler, Bruce·2004·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.0400525101
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Abstract

Several subsets of dendritic cells have been shown to produce type I IFN in response to viral infections, thereby assisting the natural killer cell-dependent response that eliminates the pathogen. Type I IFN production can be induced both by unmethylated CpG-oligodeoxynucleotide and by double-stranded RNA. Here, we describe a codominant CpG-ODN unresponsive phenotype that results from an N-ethyl-N-nitrosourea-induced missense mutation in the Tlr9 gene (Tlr9 CpG1). Mice homozygous for the Tlr9 CpG1allele are highly susceptible to mouse cytomegalovirus infection and show impaired infection-induced secretion of IFN-α/β and natural killer cell activation. We also demonstrate that both the Toll-like receptor (TLR) 9 → MyD88 and TLR3 → Trif signaling pathways are activated in vivo on viral inoculation, and that each pathway contributes to innate defense against systemic viral infection. Whereas both pathways lead to type I IFN production, neither pathway offers full protection against mouse cytomegalovirus infection in the absence of the other. The Tlr9 CpG1mutation alters a leucine-rich repeat motif and lies within a receptor domain that is conserved within the evolutionary cluster encompassing TLRs 7, 8, and 9. In other TLRs, including three mouse-specific TLRs described in this paper, the affected region is not represented. The phenotypic effect of the Tlr9 CpG1allele thus points to a critical role for TLR9 in viral sensing and identifies a vulnerable amino acid within the ectodomain of three TLR proteins, essential for a ligand response.

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Metadata

Authors
Tabeta, K., Georgel, P., Janssen, E., Du, X., Hoebe, K., Crozat, K., Mudd, S., Shamel, L., Sovath, S., Goode, J., Alexopoulou, L., Flavell, R. A., & Beutler, B.
Venue
Proceedings of the National Academy of Sciences
Publisher
Proceedings of the National Academy of Sciences
Published
2004-03
Volume
101
Issue
10
Pages
3516-3521
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
DOI
10.1073/pnas.0400525101
OpenAlex
W2030611349
Cited by
956
References
3
FWCI
32.03
Type
journal article
Language
en
Open access
green

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