Molecular optimization of rabies virus glycoprotein expression in Pichia pastoris.
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Nevertheless, data showed that the secretion of the optimized RABV-G gene was not tremendously increased as compared with the non-optimized one.Among these factors only PDI1, ERO1 and GPX1 proved their benefit to enhance the expression.Competitive neutralizing assay confirmed that the recombinant protein was produced in the correct conformational form in this host.
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Affiliation: Laboratory of Molecular Microbiology, Vaccinology and Biotechnology Development, Biofermentation Unit, Institut Pasteur de Tunis, 13, place Pasteur. BP. 74, Tunis, 1002, Tunisia.
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mbt212350-fig-0004: Competition of the neutralizing activity of the rabiesâimmune serum by recombinant RABVâG. The neutralizing titres (IU mlâ1) were determined in the presence of varying amounts of RABVâG expressed by αâ7/P6 recombinant clone, NC (negative control): culture supernatant of KM71H strain transformed with empty pPICZαA vector. Mentions: To prove that the RABVâG expressed by clone αâ7/P6 was secreted in its native form and can compete with rabies virus to react with antiârabies neutralizing serum and to block cell infection, the RFFIT test was used with the modifications introduced by Li et al. (2010). The neutralizing activity of rabiesâimmune serum was evaluated in the presence of different levels of recombinant RABVâG varying from 0.8 to 49 Όg mlâ1. As shown in Fig. 4, the neutralizing titre of the rabiesâimmune serum was significantly reduced in the presence of RABVâG compared with that seen in the absence of recombinant RABVâG. These results suggest that the RABVâG produced by P. pastoris was recognized by rabies virus neutralizing antibodies. |
View Article: PubMed Central - PubMed
Affiliation: Laboratory of Molecular Microbiology, Vaccinology and Biotechnology Development, Biofermentation Unit, Institut Pasteur de Tunis, 13, place Pasteur. BP. 74, Tunis, 1002, Tunisia.