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Both sera of the patient and chicken contained anti\u2010ganglioside antibodies and anti\u2010Lipid A (anti\u2010Kdo2\u2010Lipid A) antibodies directed against the lipid A portion of the bacterial lipooligosaccharide. The anti\u2010Kdo2\u2010Lipid A activities inhibited voltage\u2010gated Na (Nav) channel of NSC\u201034 cells in culture. We hypothesized that anti\u2010Kdo2\u2010Lipid A antibody acts on the functional inhibition of Nav1.4. To test this possibility, a rabbit peptide antibody (anti\u2010Nav1.4 pAb) against a 19\u2010mer peptide (KELKDNHILNHVGLTDGPR) on the \u03b1 subunit of Nav1.4 was produced. Anti\u2010Nav1.4 pAb was cross\u2010reactive to Kdo2\u2010Lipid A. Anti\u2010Kdo2\u2010lipid A antibody activity in the chicken serum was tested for the Na<jats:sup>+<\/jats:sup> current inhibition in NSC\u201034 cells in combination with \u03bc\u2010Conotoxin and tetrodotoxin. Contrary to our expectations, the anti\u2010Kdo2\u2010Lipid A antibody activity was extended to Nav channels other than Nav1.4. By overlapping structural analysis, it was found that there might be multiple peptide epitopes containing certain dipeptides showing a structural similarity with v\u2010Lipid A. Thus, our study suggests the possibility that there are multiple epitopic peptides on the extracellular domains of Nav1.1 to 1.9, and some of them may represent target sites for anti\u2010Kdo2\u2010Lipid A antibody, to induce neurophysiological changes in GBS by disrupting the normal function of the Nav channels. \u00a9 2008 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/jnr.21781","type":"journal-article","created":{"date-parts":[[2008,7,14]],"date-time":"2008-07-14T22:12:21Z","timestamp":1216073541000},"page":"3359-3374","source":"Crossref","is-referenced-by-count":5,"title":["Topology and patch\u2010clamp analysis of the sodium channel in relationship to the anti\u2010lipid a antibody in 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