Molecular modelling of epitope presentation using membrane protein OmpC

Abstract

<span style="font-size:12.0pt;font-family: " times="" new="" roman";mso-fareast-font-family:"times="" roman";mso-ansi-language:="" en-in;mso-fareast-language:en-in;mso-bidi-language:ar-sa"="" lang="EN-IN">Three-dimensional models of the chimeric <i>S. typhi </i>OmpC protein carrying an epitope from rotavirus VP4 capsid protein on either of two exposed loops ( fourth and sixth) were constructed separately, using computer-aided homology modelling. The theoretical model of <i>S. typhi </i>OmpC was used as a template. The monomers were initially energy minimized. The trimers were generated for both ihe chimeric <i>S. typhi</i> OmpC proteins and the structures were optimized after several cycles of minimization. The surface accessibility calculations for the resulting models show that epitope recognition should be more effective in the fourth loop than in the sixth loop. in accordance with the experimental results on the immunogenic nature of the rotaviral epitope inserted into the two putative loops of <i>S. typhi </i>OmpC.</span>