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The human cell-surface attachment factors and receptors for the dengue virus (DENV) envelope (E) protein are a heterogeneous group of host molecules essential for viral entry and infection (Cruz-Oliveira et al., 2015, PMID: 26380894). The DENV E protein mediates initial attachment to the cell surface via glycosaminoglycans, primarily heparan sulfate, which serves to concentrate the virus (Chen et al., 1997, PMID: 9371593). High-affinity interactions then occur with various receptors depending on the cell type, including C-type lectins such as DC-SIGN (CD209) on dendritic cells and L-SIGN (CD209L) in the liver (Tassaneetrithep et al., 2003, PMID: 12634810). Furthermore, DENV utilizes apoptotic mimicry to enter cells by binding to phosphatidylserine receptors like AXL and Tyro3 (Meertens et al., 2012, PMID: 22509223). Other identified factors include the mannose receptor (CD206), GRP78 (HSPA5), and CD14, which facilitate endocytosis and subsequent membrane fusion (Jindadamrongwech et al., 2004, PMID: 15140498). Because these factors are critical for the initiation of the viral life cycle, they represent significant targets for the development of antiviral entry inhibitors and therapeutic antibodies.
Inhibition of viral attachment to host cell-surface factors and blocking of receptor-mediated endocytosis.
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