Modares Journal of Biotechnology

Abstract Background:
HIV has at least six regulatory genes among which the Vif protein can control HIV replication. This study, as the first report, investigated the important mutations in VIF protein in sequences from Iranian patients and using immunoinformatics, conserved regions of this protein and B-Cell, T-Cell and CTL epitopes to stimulate the immune system, were determined.
Methods:
VIF sequences were obtained from NCBI GenBank, and tertiary structures, B-Cell, T-Cell and CTL epitopes were predicted by bioinformatics tools; besides, their antigenic and allergenic properties were studied.
Results:
The most prevalent mutations in Vif protein were related to S 49 P (90%), S 140 N and N 186 S (80%). Two substitutions at positions 41 and 42 were introduced which have effect on Vif binding to host factor. In addition, three regions were identified as the best epitope sequences with high potential to induce immune system and the lowest allergic properties, among which 5-32 region was suggested as the best vaccine candidate regions.
Conclusion:
This study as the first study from Iran using immunoinformatics tools to introduced a region with the high potential to induce humoral and cellular immune systems and lowest allergenic properties which can be used for further studies on HIV vaccines.

Abstract Foot and Mouth Disease (FMD) is a highly contagious and devastating disease that spreads rapidly and causes many economic damages. One of the important methods for detection of FMD and particularly differentiation of vaccinated from infected animals, is the use of non-structural proteins as antigens in ELISA kits. The purpose of this study was cloning of the gene sequence and expression of the antigenic regions of 3D nonstructural protein as one of the diagnostic options. For amplification of the antigenic regions of FMD virus 3D protein, specific primers containing NdeI and EcoRI restriction sites were designed and the polymerase chain reaction was performed. The sequences cut by these two enzymes, were inserted into PET21a+ vectors. The recombinant plasmids were then transformed into E. coli (DH5α). Colony-PCR tests and enzymatic digestions were performed on the resulting colonies and the presence of the target gene was confirmed. The gene sequence was further confirmed after sequencing. For production of recombinant antigens, the recombinant vector was transferred to the expression host of E. coli-BL21. The bacteria containing the recombinant gene were induced with IPTG and the expression of the recombinant protein was confirmed using the SDS-PAGE method. The molecular weight of the recombinant protein was about 24 kDa, and it can be used in the design of ELISA diagnostic kit.