Specific glycan-modified HIV envelope proteins as vaccine immunogens against
Introduction A major obstacle in current AIDS/HIV vaccine development is the failure to induce broadly neutralizing antibodies against primary isolates of human immunodeficiency virus. Standard vaccination approaches prime the adaptive immune system to recognize viral envelope proteins. However, these methods have failed in the case of HIV-1, as the epitopes of the viral envelope are too variable and the functionally important epitopes of the gp120 envelope protein are masked by glycosylation. Although HIV type 1 (HIV-1) envelope proteins have been targeted for vaccine development for over two decades, immunity induced by early vaccines has been effective only against laboratory-adapted isolates or chimeric viruses (SHIV) bearing the homologous env genes. Despite considerable evidence indicating the role of glycosylation in modulating envelope antigenicity, relatively few have addressed its potential role in influencing the immunogenicity of HIV-1 envelope proteins. Technology description UW researchers have engineered an HIV gp120 molecule that displays interesting new biochemical and biological properties. The elimination of a single N-linked glycan site increased sensitivity to broadly neutralizing monoclonal antibodies; transformed the ability to mediate CD4-independent viral infection; and upon immunization in experimental animals, elicited sera possessing higher and broader neutralizing activities than that of the non-mutated HIV-1 gp120. These findings demonstrate the potential utility of specific glycan-modified HIV envelope proteins as a component of safe and broadly efficacious vaccines against HIV/AIDS. Business Opportunity While an effective HIV vaccine does not yet exist, the market for HIV/AIDS treatment is expected to grow to $10.6 billion by the year 2015. Intellectual Property Position A United States patent and a Canadian patent are pending on this technology. Related Publication Li, Y. et al (2008). “Removal of a single N-linked glycan in human immunodeficiency virus type 1 gp120 results in an enhanced ability to induce neutralizing antibody responses.” Journal of Virology 82(2): 638Type of Offer: Licensing
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