The surface of enveloped viruses can be extensively glycosylated. Unlike the glycans coating pathogens such as bacteria and fungi, glycans on viruses are added and processed by the host-cell during biosynthesis. Glycoproteins are typically subjected to α-mannosidase processing and Golgi-mediated glycosyltransferase extension to form complex-type glycans. In envelope viruses, exceptions to this default pathway are common and lead to the presence of oligomannose-type glycan structures on the virion surface. In one extreme example, HIV-1 utilises a high density of glycans to limit host antibody recognition of protein. However, the high density limits glycan processing and the resulting oligomannose structures can be recognised by broadly neutralising antibodies isolated from HIV-1 infected patients. Here we discuss how divergence from host-cell glycosylation can be targeted for vaccine design.

包膜病毒的表面可以被广泛糖基化。与包被病原体（如细菌和真菌）的聚糖不同，病毒上的聚糖是在生物合成过程中由宿主细胞添加和加工的。糖蛋白通常经过 α-甘露糖苷酶加工和高尔基体介导的糖基转移酶延伸以形成复合型聚糖。在包膜病毒中，这种默认途径的例外情况很常见，并导致病毒粒子表面存在寡甘露糖型聚糖结构。在一个极端的例子中，HIV-1 利用高密度的聚糖来限制宿主抗体对蛋白质的识别。然而，高密度限制了聚糖加工，由此产生的寡甘露糖结构可以通过从 HIV-1 感染患者中分离的广泛中和抗体来识别。