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The extensive diversity of the HIV-1 Envelope glycoprotein (Env) has hindered vaccine design, exemplified by the scarcity of broad and potent neutralising antibodies in infected patients. The extensive N-linked glycosylation that covers the antigenic protein surface has emerged as a promising target for vaccination as an increasing number of broadly neutralising antibodies have been isolated from a subset of infected patients. Immunogens that recreate the glycosylation of viral Env are being developed to elicit these protective antibodies prior to infection. An important part of this design process is to characterise the glycosylation of these candidate immunogens to ensure the epitopes for these bnAbs are present. The Crispin laboratory have developed a methodology to define the glycosylation of candidate immunogens on both a global and site-specific level and applied this to a leading soluble trimeric vaccine candidate. Joel has utilised this method to elucidate the changes in glycosylation resulting from a diverse range of immunogen design platforms and to compare the glycosylation of soluble immunogens with viral derived Env.
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