Virus-like particles as universal influenza vaccines

• Type of Material: Article
• Authors: Sang-Moo Kang, Georgia State University; Min-Chul Kim, Emory University; Richard W Compans, Emory University
• Language: English
• Date: 2012-08-01
• Publisher: Taylor & Francis: STM, Behavioural Science and Public Health Titles - No Open Select
• Publication Version: Author Accepted Manuscript (After Peer Review)
• Copyright Statement: © 2012 Expert Reviews Ltd.
• Final Published Version (URL): http://dx.doi.org/10.1586/ERV.12.70
• Title of Journal or Parent Work: Expert Review of Vaccines
• ISSN: 1476-0584
• Volume: 11
• Issue: 8
• Start Page: 995
• End Page: 1007
• Grant/Funding Information: This work was supported in part by NIH/NIAID grant AI0680003 (RW Compans), and NIH/NIAID grants AI081385 (SM Kang) and AI093772 (SM Kang).
• Keywords: adjuvant; INTRAVIRIONIC ANTIGENIC-COMPETITION; PROTECTIVE IMMUNE-RESPONSES; A-VIRUS; HEMAGGLUTININ MEMBRANE GLYCOPROTEIN; EXPRESSING H5 HEMAGGLUTININ; Life Sciences & Biomedicine; NA; M2 PROTON CHANNEL; Immunology; VLPs; universal vaccine; AVIAN INFLUENZA; influenza; M2; T-CELL RESPONSES; Science & Technology; DENDRITIC CELLS; HA stalk domain; LETHAL INFLUENZA
• Research Categories: Biology, General; Health Sciences, Immunology

Abstract

Current influenza vaccines are primarily targeted to induce immunity to the influenza virus strain-specific hemagglutinin antigen and are not effective in controlling outbreaks of new pandemic viruses. An approach for developing universal vaccines is to present highly conserved antigenic epitopes in an immunogenic conformation such as virus-like particles (VLPs) together with an adjuvant to enhance the vaccine immunogenicity. In this review, the authors focus on conserved antigenic targets and molecular adjuvants that were presented in VLPs. Conserved antigenic targets that include the hemagglutinin stalk domain, the external domain of influenza M2 and neuraminidase are discussed in addition to molecular adjuvants that are engineered to be incorporated into VLPs in a membrane-anchored form. © 2012 2012 Expert Reviews Ltd.