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First, the impact of synonymous codon usage bias was examined and an optimized\n                    <jats:styled-content style=\"fixed-case\">RABV<\/jats:styled-content>\n                    \u2010G gene was synthesized. Nevertheless, data showed that the secretion of the optimized\n                    <jats:styled-content style=\"fixed-case\">RABV<\/jats:styled-content>\n                    \u2010G gene was not tremendously increased as compared with the non\u2010optimized one. In addition, similar levels of\n                    <jats:styled-content style=\"fixed-case\">RABV<\/jats:styled-content>\n                    \u2010G were obtained when \u03b1\u2010factor mating factor from\n                    <jats:italic>Saccharomyces cerevisiae<\/jats:italic>\n                    or the acid phosphatase\n                    <jats:styled-content style=\"fixed-case\">PHO<\/jats:styled-content>\n                    1 was used as a secretion signal. Therefore, sequence optimization and secretion signal were not the major bottlenecks for high\u2010level expression of\n                    <jats:styled-content style=\"fixed-case\">RABV<\/jats:styled-content>\n                    \u2010G in\n                    <jats:italic>P.\u00a0pastoris<\/jats:italic>\n                    . Unfolded protein response (\n                    <jats:styled-content style=\"fixed-case\">UPR<\/jats:styled-content>\n                    ) was induced in clones containing high copy number of\n                    <jats:styled-content style=\"fixed-case\">RABV<\/jats:styled-content>\n                    \u2010G expression cassette indicating that folding was the limiting step for\n                    <jats:styled-content style=\"fixed-case\">RABV<\/jats:styled-content>\n                    \u2010G secretion. To circumvent this limitation, co\u2010overexpression of five factors involved in oxidative protein folding was investigated. Among these factors only\n                    <jats:italic>\n                      <jats:styled-content style=\"fixed-case\">PDI<\/jats:styled-content>\n                      1\n                    <\/jats:italic>\n                    ,\n                    <jats:italic>\n                      <jats:styled-content style=\"fixed-case\">ERO<\/jats:styled-content>\n                      1\n                    <\/jats:italic>\n                    and\n                    <jats:italic>\n                      <jats:styled-content style=\"fixed-case\">GPX<\/jats:styled-content>\n                      1\n                    <\/jats:italic>\n                    proved their benefit to enhance the expression. The highest expression level of\n                    <jats:styled-content style=\"fixed-case\">RABV<\/jats:styled-content>\n                    \u2010G reached 1230\u00a0ng\u00a0ml\n                    <jats:sup>\u22121<\/jats:sup>\n                    . Competitive neutralizing assay confirmed that the recombinant protein was produced in the correct conformational form in this host.\n                  <\/jats:p>","DOI":"10.1111\/1751-7915.12350","type":"journal-article","created":{"date-parts":[[2016,2,16]],"date-time":"2016-02-16T04:23:56Z","timestamp":1455596636000},"page":"355-368","source":"Crossref","is-referenced-by-count":39,"title":["Molecular optimization of rabies virus glycoprotein expression in\n                    <i>Pichia pastoris<\/i>"],"prefix":"10.1111","volume":"9","author":[{"given":"Safa","family":"Ben Azoun","sequence":"first","affiliation":[{"name":"Laboratory of Molecular Microbiology, Vaccinology and Biotechnology Development Biofermentation Unit Institut Pasteur de Tunis 13, place Pasteur. 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