Taylor Philip R, Zamze Susanne, Stillion Richard J, Wong Simon Y C, Gordon Siamon, Martinez-Pomares Luisa
Sir William Dunn School of Pathology, Oxford University, South Parks Road, Oxford OX1 3RE, United Kingdom.
Proc Natl Acad Sci U S A. 2004 Feb 17;101(7):1963-8. doi: 10.1073/pnas.0308490100. Epub 2004 Feb 5.
The cysteine-rich domain (CR) of the mannose receptor binds sulfated glycoprotein CR ligand (CRL) expressed by subpopulations of myeloid cells in secondary lymphoid organs (CRL(+) cells). In naïve mice, these CRL(+) cells, metallophilic macrophages (M) in spleen and subcapsular sinus M in lymph nodes, are located strategically for antigen capture and are adjacent to B cell follicles, but their role in the immune response is unknown. We have exploited the lectin activity of CR to develop a highly specific system for targeting protein to CRL(+) M. We demonstrate that the sulfated carbohydrates recognized by CR are exposed to the extracellular milieu and mediate highly specific targeting of CR-containing proteins. This model will allow the dissection of the role of metallophilic M in an immune response in vivo.
甘露糖受体的富含半胱氨酸结构域（CR）与次级淋巴器官中髓样细胞亚群表达的硫酸化糖蛋白CR配体（CRL）（CRL(+)细胞）结合。在未接触过抗原的小鼠中，这些CRL(+)细胞，即脾脏中的亲金属巨噬细胞（M）和淋巴结中的被膜下窦巨噬细胞，在战略上定位用于捕获抗原，且与B细胞滤泡相邻，但其在免疫反应中的作用尚不清楚。我们利用CR的凝集素活性开发了一种将蛋白质靶向CRL(+) M的高度特异性系统。我们证明，CR识别的硫酸化碳水化合物暴露于细胞外环境，并介导含CR的蛋白质的高度特异性靶向。该模型将有助于剖析亲金属M在体内免疫反应中的作用。
