Virology, Nebraska Center for
Date of this Version
2017
Citation
Vaccine 35 (2017) 3067–3075. doi:10.1016/j.vaccine.2017.04.054
Abstract
The outer-domain core of gp120 may serve as a better HIV vaccine immunogen than the full-length gp120 because of its greater stability and immunogenicity. In our previous report, we introduced two disulfide bonds to the outer-domain core of gp120 to fix its conformation into a CD4-bound state, which resulted in a significant increase in its immunogenicity when compared to the wild-type outer-domain core. In this report, to further improve the immunogenicity of the outer-domain core based immunogen, we have introduced a Tryptophan residue at gp120 amino acid sequence position 375 (375S/W). Our data from immunized guinea pigs indeed shows a striking increase in the immune response due to this stabilized core outer-domain. Therefore, we conclude that the addition of 375W to the outer-domain core of gp120 further stabilizes the structure of immunogen and increases the immunogenicity
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Comments
Copyright (c) 2017 The Author(s). Published by Elsevier Ltd. This is an open access article under the CC BY-NC-ND license