In 2011, simultaneous, widespread outbreaks of food poisoning by contaminated enterohemorrhagic Escherichia coli in beef, which killed four and hospitalized more than 30 people, occurred in Japan. While the press was widely reporting this disaster, two maintenance hemodialysis patients were suffering from Campylobacter bacteremia by eating undercooked meat. One patient was infected with C. upsaliensis and the other with C. fetus. Although these patients could be successfully treated, they led us to consider the characteristics of C. upsaliensis and C. fetus as opportunistic pathogens, as well as changes in dietary behaviors and food markets. Moreover, they emphasized the need for hemodialysis patients to be not only educated in that they should restrict potassium, phosphate and water intake, but also that they should take care of food sanitation.
Neurons express many cell surface proteins as mutually binding key-lock molecules that can create synapses. However, the molecular mechanisms of how neurons make synapses only with preferred targets are not completely understood. Here we identified Side-IV and Beat-IIb, belonging to the Drosophila immunoglobulin superfamily, as a new key-lock combination capable of inducing synapse formation. Side-IV interaction with Beat-IIb transduces bifurcated signaling to Side-IV's co-receptor, Kirre, and a synaptic scaffold protein, Dsyd-1. Localization and genetic interaction analyses revealed that Side-IV localizes subcellularly at synapse formations defined by Beat-IIa/b and anchors Dsyd-1.Our data demonstrate that a complex made up of Side-IV, Beat-IIb, Kirre, and Dsyd-1 not only narrows neuronal binding specificity but also recruits synapse formation factors Kirre and Dsyd-1 to restrict synapse formation loci and inhibit miswiring. We propose a mechanism by which key-lock molecules set a hierarchy of preference among neuronal pairs in a complex circuit in vivo.
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