聚糖
表位
糖肽
糖基化
抗体
背景(考古学)
生物
艾滋病疫苗
人类免疫缺陷病毒(HIV)
糖蛋白
抗原
计算生物学
病毒学
生物化学
免疫学
疫苗试验
古生物学
抗生素
作者
Md. Ruhul Amin,Jason S. McLellan,Wei Huang,Jared Orwenyo,Dennis R. Burton,Wayne C. Koff,Peter D. Kwong,Lai-Xi Wang
标识
DOI:10.1038/nchembio.1288
摘要
A new class of glycan-reactive HIV-neutralizing antibodies, including PG9 and PG16, has been recently discovered that seem to recognize previously uncharacterized glycopeptide epitopes on HIV-1 gp120. However, further characterization and reconstitution of the precise neutralizing epitopes are complicated by the heterogeneity of glycosylation. We report here the design, synthesis and antigenic evaluation of new cyclic V1V2 glycopeptides carrying defined N-linked glycans at the conserved glycosylation sites (Asn160 and Asn156 or Asn173) derived from gp120 of two HIV-1 isolates. Antibody binding studies confirmed the necessity of a Man₅GlcNAc₂ glycan at Asn160 for recognition by PG9 and PG16 and further revealed a critical role of a sialylated N-glycan at the secondary site (Asn156 or Asn173) in the context of glycopeptides for antibody binding. In addition to defining the glycan specificities of PG9 and PG16, the identified synthetic glycopeptides provide a valuable template for HIV-1 vaccine design.
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