| Cellular Uptake of Gold Nanoparticles Bearing HIV gp120 Oligomannosides. | |
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MedLine Citation:
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PMID: 22433013 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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ABSTRACT: Dendritic cells are the most potent of the professional antigen presenting cells which display a pivotal role in the generation and regulation of adaptive immune responses against HIV-1. The migratory nature of dendritic cells is subverted by HIV-1 to gain access to lymph nodes where viral replication occurs. Dendritic cells express several calcium-dependent C-type lectin receptors including dendritic cell-specific ICAM-3 grabbing non-integrin (DC-SIGN), which constitute a mayor receptor for HIV-1. DC-SIGN recognizes N-linked high-mannose glycan clusters on HIV gp120 through multivalent and Ca2+ dependent protein-carbohydrate interactions. Therefore mimicking the cluster presentation of oligomannosides from the virus surface is a strategic approach for carbohydrate-based microbicides. We have shown that gold nanoparticles (mannoGNPs) displaying multiple copies of structural motifs (di-, tri-, tetra-, penta- or heptaoligomanosides) of the N-linked high-mannose glycan of viral gp120 are efficient inhibitors of DC-SIGN mediated trans-infection of human T cells. We have now prepared the corresponding fluorescent-labeled glyconanoparticles (FITC-mannoGNPs) and studied their uptake by DC-SIGN expressing Burkitt lymphoma cells (Raji DC-SIGN cell line) and monocyte-derived immature dendritic cells (iDCs) by flow cytometry and confocal laser scanning microscopy. We demonstrate that the 1.8 nm oligomannoside coated nanoparticles are endocytosed following both DC-SIGN-dependent and -independent pathways and part of them colocalize with DC-SIGN in early endosomes. The blocking and sequestration of DC-SIGN receptors by mannoGNPs could explain their ability to inhibit HIV-1 trans-infection of human T cells in vitro. |
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Authors:
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Soledad Penadés; Blanca Arnaiz; Olga Martínez-Ávila; Juan Manuel Falcon-Perez |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2012-3-21 |
Journal Detail:
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Title: Bioconjugate chemistry Volume: - ISSN: 1520-4812 ISO Abbreviation: - Publication Date: 2012 Mar |
Date Detail:
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Created Date: 2012-3-21 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9010319 Medline TA: Bioconjug Chem Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
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