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

Autor: Banerjee K; Department of Microbiology and Immunology, Weill Cornell Medical College, New York, New York 10021, USA., Michael E, Eggink D, van Montfort T, Lasnik AB, Palmer KE, Sanders RW, Moore JP, Klasse PJ
Jazyk: angličtina
Zdroj: AIDS research and human retroviruses [AIDS Res Hum Retroviruses] 2012 Feb; Vol. 28 (2), pp. 206-14. Date of Electronic Publication: 2011 Jul 27.
DOI: 10.1089/aid.2011.0101
Abstrakt: 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.
Databáze: MEDLINE