Occluding the mannose moieties on human immunodeficiency virus type 1 gp120 with griffithsin improves the antibody responses to both proteins in mice Academic Article uri icon

Overview

MeSH Major

  • AIDS Vaccines
  • Algal Proteins
  • Antibody Formation
  • HIV Antibodies
  • HIV Envelope Protein gp120
  • HIV-1
  • Lectins
  • Mannose-Binding Lectin

abstract

  • To assess the influence of mannosylated glycans on the immunogenicity of human immunodeficiency virus type 1 (HIV-1) Env proteins, we immunized mice with monomeric gp120 in the presence and absence of the mannose-binding protein, griffithsin (GRFT). For comparison, other groups of mice received the nonglycosylated HIV-1 Gag protein, with and without GRFT. Coimmunization with GRFT increased the anti-gp120 IgG reactivity significantly, but had no effect on the anti-Gag response. We also investigated the IgG response to GRFT and found that gp120, but not Gag, enhanced its immunogenicity. For both proteins, IgG1 antibodies dominated the IgG response, with IgG2b as the next most prevalent subclass. We conclude that gp120-GRFT complexes are more immunogenic than the free proteins, for both components, and that occluding the mannose moieties on monomeric gp120 can improve the humoral immune response to this protein.

publication date

  • February 2012

Research

keywords

  • Academic Article

Identity

Language

  • eng

PubMed Central ID

  • PMC3275927

Digital Object Identifier (DOI)

  • 10.1089/aid.2011.0101

PubMed ID

  • 21793733

Additional Document Info

start page

  • 206

end page

  • 14

volume

  • 28

number

  • 2