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NOD-like proteins (NLR) are a specialized group of intracellular receptors, which constitute an essential component of the host innate immune system. They were discovered more than a decade ago, but research on this particular class of microbial detectors is still ongoing to allow for a better understanding of the mechanisms, recognition of microorganisms, transmission of signals, and carrying out the activation of inflammatory signaling pathways. In this review, we discuss the construction of NOD1 and NOD2 receptors, their functions, and significance in the pathogenesis of inflammatory diseases in humans.
The establishment of the nitrogen-fixing symbiosis between rhizobia and legumes re quires an ex change of sig nals be tween the two part ners. In re sponse to flavonoids ex creted by the host plant, rhizobia syn the size Nod fac tors (NFs) which elicit, at very low con cen tra tions and in a spe cific man ner, var i ous sym bi otic re sponses on the roots of the le gume hosts. NFs from sev eral rhizobial spe cies have been char ac ter ized. They all are lipo-chitooligosaccharides, con sist ing of a back bone of gen er ally four or five glucosamine residues N-acylated at the non-reducing end, and carrying various O-substituents. The N-acyl chain and the other substituents are important determi nants of the rhizobial host spec i fic ity. A num ber of nodulation genes which spec ify the syn the sis of NFs have been iden ti fied. All rhizobia, in spite of their di ver sity, pos sess conserved nodABC genes responsible for the synthesis of the N-acylated oligo­saccharide core of NFs, which sug gests that these genes are of a monophyletic or i gin. Other genes, the host spe cificnod genes, spec ify the sub sti tu tions of NFs. The cen tral role of NFs and nod genes in the Rhizo bium-legume sym bi o sis sug gests that these fac­tors could be used as mo lec u lar mark ers to study the evo lu tion of this sym bi o sis. We have stud ied a num ber of NFs which are N-acylated by α,β-unsaturated fatty ac­ids. We found that the abil ity to syn the size such NFs does not cor re late with tax o- nomic po si tion of the rhizobia. How ever, all rhizobia that pro duce NFs such nodulate plants be long ing to re lated tribes of le gumes, the Trifolieae, Vicieae, and Galegeae, all of them be ing mem bers of the so-called galegoid group. This sug gests that the abil ity to recognize the NFs with α,β-unsaturated fatty acids is limited to this group of le­gumes, and thus might have ap peared only once in the course of le gume evo lu tion, in the galegoid phy lum.
The fucosyltransferase NodZ is involved in the biosynthesis of the nodulation factor in nitrogen-fixing symbiotic bacteria. It catalyzes α1,6 transfer of l-fucose from GDP-fucose to the reducing residue of the synthesized Nod oligosaccharide. We present the structure of the NodZ protein from Bradyrhizobium expressed in Escherichia coli and crystallized in the presence of phosphate ions in two crystal forms. The enzyme is arranged into two domains of nearly equal size. Although NodZ falls in one broad class (GT-B) with other two-domain glycosyltransferases, the topology of its domains deviates from the canonical Rossmann fold, with particularly high distortions in the N-terminal domain. Mutational data combined with structural and sequence alignments indicate residues of potential importance in GDP-fucose binding or in the catalytic mechanism. They are all clustered in three conserved sequence motifs located in the C-terminal domain.
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