Tryptophan 375 stabilizes the outer-domain core of gp120 for HIV vaccine immunogen design

Duoyi Hu, Dane Bowder, Wenzhong Wei, Jesse Thompson, Mark A. Wilson, Shi Hua Xiang

Research output: Contribution to journalArticlepeer-review

2 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)3067-3075
Number of pages9
Issue number23
StatePublished - May 25 2017


  • 375W
  • Gp120
  • HIV-1 subtype C
  • Immunogenicity
  • Outer domain (OD)
  • Structure-based design
  • Vaccine

ASJC Scopus subject areas

  • Molecular Medicine
  • General Immunology and Microbiology
  • General Veterinary
  • Public Health, Environmental and Occupational Health
  • Infectious Diseases


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