The macrophage galactose-type lectin (MGL) recognizes glycan moieties exposed by pathogens and malignant cells. Particularly, mucin-1 (MUC1) glycoprotein presents an altered glycosylation in several cancers. To estimate the ability of distinct MGL orthologs to recognize aberrant glycan cores in mucins, we applied evanescent-field detection to a versatile MUC1-like glycopeptide microarray platform. Here, as binding was sequence-dependent, we demonstrated that not only sugars but also peptide region impact the recognition of murine MGL1 (mMGL1). In addition, we observed for all three MGL orthologs that divalent glycan presentation increased the binding. To assess the utility of the glycopeptide binders of the MGL orthologs for MGL targeting, we performed uptake assays with fluorescein-MUC1 using murine dendritic cells. A diglycosylated MUC1 peptide was preferentially internalized in an MGL-dependent fashion, thus showing the utility for divalent MGL targeting. These findings may be relevant to a rational design of antitumor vaccines targeting dendritic cells via MGL.

中文翻译：

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糖肽作为树突状细胞的目标：探索对巨噬细胞半乳糖型凝集素（MGL）直系同源物的MUC1糖肽结合概况。

巨噬细胞半乳糖型凝集素（MGL）识别病原体和恶性细胞暴露的聚糖部分。特别是，黏蛋白1（MUC1）糖蛋白在几种癌症中呈现出糖基化改变。为了评估不同的MGL直系同源物识别粘蛋白中异常聚糖核心的能力，我们将消逝场检测应用于多功能MUC1样糖肽微阵列平台。在这里，由于结合是序列依赖性的，我们证明不仅糖而且肽区也会影响鼠MGL1（mMGL1）的识别。另外，我们观察到对于所有三个MGL直向同源物，二价聚糖呈递增加了结合。为了评估MGL直系同源物的糖肽结合剂对MGL靶向的效用，我们使用了鼠类树突状细胞对荧光素-MUC1进行了吸​​收分析。二糖基化的MUC1肽优先以MGL依赖性的方式内在化，因此显示了对二价MGL靶向的实用性。这些发现可能与通过MGL靶向树突状细胞的抗肿瘤疫苗的合理设计有关。