HIV camouflage Spike hiper Glycosilation

HIV-1 envelope glycoprotein (Env), the fusion machine on the surface of HIV-1, is metastable and one of the most highly glycosylated protein complexes known. Figure shows Env trimer HIV protein, its fusion and anchoring domain is shown in yellow, receptor recognition and binding domain is shown in red. Sugars of glycosilated sites of the trimeric HIV spike are shown in blue.
En la figura se muestra la proteína de envuelta, reconocimiento y fusión del HIV o VIH). El dominio de fusión que se une a la membrana se muestra en amarillo, el dominio de reconocimiento se muestra en rojo. La proteína Env del HIV es una de las más glicosiladas y está por tanto recubierto de azúcares (azul) que le sirven como camuflaje para evadir al sistema inmune.

Interactive giroscopic image

The envelope glycoprotein (Env) spike, a heterodimeric trimer consisting of three gp120 exterior subunits and three gp41 transmembrane subunits, is the only HIV-1-specific target for neutralizing antibodies (NAbs). The appropriate presentation of Env to the immune system may be an essential part of a successful vaccine strategy. Unfortunately, the Env trimer has evolved features to minimize the elicitation and impact of neutralizing antibodies, including a heavy coat of carbohydrate. Approximately 50% of the mass of gp120 consists of carbohydrate, with most of the more than 24 potential N-linked glycosylation sites (PNGSs) utilized in most HIV-1 variants

Env is highly glycosylated, and yet vaccine developers have lacked guidance on how to assess whether their immunogens have optimal glycosylation. 

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