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AQP4\u2010M23 is the OAP\u2010forming isoform, whereas AQP4\u2010M1 alone is unable to form OAPs. The function of AQP4 organization into OAPs in normal physiology is unknown; however, alteration in OAP assemblies is reported for several CNS pathological states. In this study, we demonstrate that in the CNS, NMO\u2010IgG is able to pull down both M1\u2010 and M23\u2010AQP4 but experiments performed using cells selectively transfected with M1\u2010 or M23\u2010AQP4 and native tissues show NMO\u2010IgG epitope to be intrinsic in AQP4 assemblies into OAPs. Other OAP\u2010forming water\u2010channel proteins, such as the lens Aquaporin\u20100 and the insect Aquaporin\u2010cic, were not recognized by NMO\u2010IgG, indicating an epitope characteristic of AQP4\u2010OAPs. Finally, water transport measurements show that NMO\u2010IgG treatment does not significantly affect AQP4 function. In conclusion, our results suggest for the first time that OAP assemblies are required for NMO\u2010IgG to recognize AQP4. \u00a9 2009 Wiley\u2010Liss, Inc.,<\/jats:p>","DOI":"10.1002\/glia.20855","type":"journal-article","created":{"date-parts":[[2009,2,19]],"date-time":"2009-02-19T19:14:11Z","timestamp":1235070851000},"page":"1363-1373","source":"Crossref","is-referenced-by-count":143,"title":["Aquaporin\u20104 orthogonal arrays of particles are the target for neuromyelitis optica autoantibodies"],"prefix":"10.1002","volume":"57","author":[{"given":"Grazia 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