The Use of Liposomes to Shape Epitope Structure and Modulate Immunogenic Responses of Peptide Vaccines Against HIV MPER

Publication date: Available online 18 April 2015 Source:Advances in Protein Chemistry and Structural Biology Author(s): Beatriz Apellániz , José L. Nieva Peptide vaccines have been shown effective in preventing animal infection in some instances, and various formulations are under evaluation for their potential clinical use in humans. In the case of the Human Immunodeficiency Virus type-1 (HIV-1) infection, viral escape from immune surveillance restricts relevant neutralizing humoral responses to a handful of sites of vulnerability on the envelope glycoprotein. The membrane-proximal external region (MPER) on the gp41 transmembrane subunit has been identified as the only linear B-epitope that embodies an HIV vulnerability site. Thus, focusing humoral responses to MPER by peptide-based immunogens is a pursued goal in HIV vaccine development. The location of this sequence in the vicinity of the membrane interface, its composition (rich in aromatic residues), and the requirement of long-hydrophobic heavy-chain third complementarity-determining region loops for antibody-mediated neutralization suggests that in addition to the specific amino acid composition, antigenicity and immunogenicity of MPER can be modulated by membrane lipids. In this chapter, we give an overview of applications of lipid vesicles (liposomes) to the development of MPER-targeting vaccines, both as type-B adjuvants and epitope structure-shaping devices.
Source: Advances in Protein Chemistry and Structural Biology - Category: Biochemistry Source Type: research