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Endocytosis of an anti-nucleic acid antibody is mediated by cell-surface heparan sulfate proteoglycans and chondroitin sulfate proteoglycans

Authors
Kim, Minjae; Kim, Hye-Jin; Pham, Chuong D.; Seo, Youngsil; Park, Hyunjoon; Lee, Yeonjin; Lee, Joungmin; Kwon, Myung-Hee
Department
Department of Microbiology
Abstract
A subset of anti-DNA or nucleic acid antibodies can internalize in a variety of living cells. Although their endocytosis pathways and cellular localizations have been studied in several types of cells, little is known about the cell surface endocytic receptors for anti-DNA Abs. Here we investigated the receptor for internalization of 3D8 scFv antibody. Cell surface binding and internalization of 3D8 scFv was dramatically inhibited in the presence of soluble HS and CS, by enzymatic cleavage of HS and CS, and in HS/CS-deficient cells. It was also revealed that sulfation groups on HS and CS chain is important for binding and internalization of 3D8 scFv. Intracellular co-localization between three molecules of 3D8 scFv-HSPG-caveolin 1 (a caveosome marker) as well as 3D8 scFv-CSPG-caveolin 1 was observed in HeLa cells, demonstrating that 3D8 scFv enters cells though the interaction with HSPGs via caveosome-mediated endocytosis pathway. Moreover, 3D8 scFv was intracellularly colocalized with syndecan-2 (a transmembrane HSPG) and glypican-3 (a GPI-anchored HSPG). Our results show that cell surface HSPGs and CSPGs are true internalizing receptors for 3D8 scFv antibody, which have important implications for the understanding of potential cell membrane targets for macromolecular delivery.
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