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Carbohydrate recognition is fundamental to a wide variety of interkingdom interactions. For example, bacterial peptidoglycan, an N-acetyl-D-glucosamine (GlcNAc)–N-acetylmuramic acid (MurNAc) polymer [1], and fungal chitin, a GlcNAc polymer [2, 3], are both immunostimulatory to vertebrates. In addition, bacterially produced Nodulation (Nod) factors, which consist of a modified GlcNAc, play a key role in symbiotic interactions with plants [4]. The structural similarity of these GlcNAc-containing molecules (Fig 1) suggests possible overlap in their physiological action, although many of the mechanisms underlying the detection of these molecules in different organisms appear unrelated. However, a single phylogenetically conserved domain, called Lysin (LysM), is found in specific receptors in signaling pathways responsive to one or more of these three related carbohydrates in bacteria, plants, and fungi and possibly mammalian systems. Thus, promiscuous activation could occur when a structurally similar but physiologically inappropriate ligand binds and thereby aberrantly activates an incorrect LysM domain-containing receptor. Here, I will discuss this possibility and its implications for immune pathologies such as asthma in which chitin is relevant.       Open in a separate window   Fig 1  Bacterial and fungal carbohydrates. A. Monomer of L-Lys containing peptidoglycan from Staphlycoccus aureus. B. Fungal chitin. C. Sinorhizobium meliloti Nod factor NodSmIV. Lys, Lysin; Nod, Nodulation.

Detection of fungal and bacterial carbohydrates: Do the similar structures of chitin and peptidoglycan play a role in immune dysfunction?