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nature immunology volume 10 number 12 december 2009 1267 The mammalian nucleotide-binding oligomerization domain
 

Summary: nature immunology volume 10 number 12 december 2009 1267
The mammalian nucleotide-binding oligomerization domain
(Nod)-like receptor (NLR) proteins function as intracellular pattern-
recognition receptors and as regulators of host immunity by detecting
microbial products1. The prototypic NLR members, Nod1 and Nod2,
sense fragments of peptidoglycan from bacteria. Nod1 activity is trig-
gered by -d-glutamyl-meso-diaminopimelic acid, which is unique
to peptidoglycan structures in all Gram-negative bacteria and certain
Gram-positive bacteria, including the genera Listeria and Bacillus1. In
contrast, Nod2 is activated by muramyl dipeptide (MDP), a peptido-
glycan motif present in all Gram-positive and Gram-negative bacte-
ria1. The importance of NLRs in detecting specific microbial products
is underscored by the susceptibility of mice with targeted deletion
of various NLR genes2. However, the role of NLRs in sensing intra-
cellular parasites is unclear at present.
Toxoplasma gondii is an obligate intracellular protozoan pathogen
able to infect various animal species. Infection with T. gondii can
cause severe disease, such as pneumonia and encephalitis, in immuno-
compromised hosts.One major determinant of the outcome of T.gondii
infection is the ability of the host to elicit robust cellular immunity to

  

Source: Arnold, Jonathan - Nanoscale Science and Engineering Center & Department of Genetics, University of Georgia

 

Collections: Biotechnology