DC-SIGN and DC-SIGNR Interact with the Glycoprotein of Marburg Virus and the S Protein of Severe Acute Respiratory Syndrome Coronavirus

Abstract

The lectins DC-SIGN and DC-SIGNR can augment viral infection; however, the range of pathogens interacting with these attachment factors is incompletely defined. Here we show that DC-SIGN and DC-SIGNR enhance infection mediated by the glycoprotein (GP) of Marburg virus (MARV) and the S protein of severe acute respiratory syndrome coronavirus and might promote viral dissemination. SIGNR1, a murine DC-SIGN homologue, also enhanced infection driven by MARV and Ebola virus GP and could be targeted to assess the role of attachment factors in filovirus infection in vivo.

The DC-SIGN of Zebrafish: Insights into the Existence of a CD209 Homologue in a Lower Vertebrate and Its Involvement in Adaptive Immunity

“…The primitive CD209 might originate from teleosts during early vertebrate evolution, because we have failed in an attempt to search for homologous sequences in the lower species such as lancelet (Branchiostoma floridae), whose genome sequence has been recently identified (43). Although genetic mechanisms such as deletion and mutation have led to the differentiation of CD209 homologues among different species to some extent, there is no remarkable divergence with regard to the basic structure and variety observed among fish, amphibians, avian specfies, and the mouse until the divergence of CD209, CD209L, and CD209L2 from one another in primates (44). The multigenic nature of the CD209 family in primates, but not in early vertebrates, raises the possibility that the CD209 family was genetically conserved during the long history of vertebrate evolution until recent evolutionary alterations occurred across primate species.…”

Conserved Receptor-binding Domains of Lake Victoria Marburgvirus and Zaire Ebolavirus Bind a Common Receptor

“…However, the C-type lectin asialoglycoprotein receptor (27,28), DC-SIGN (29,30), hMGL (31), L-SIGN (29,30), and LSECtin (32), as well as other molecules, including folate receptor-␣ (33) and ␤1 integrins (15), have been shown or suggested to enhance filovirus cell entry. Subtle differences between marburgvirus and ebolavirus infection efficiencies in different cell lines or following glycosidase or protease treatment have led to the suggestion that these viruses utilize distinct receptors or entry mechanisms (5).…”

West Nile Virus Discriminates between DC-SIGN and DC-SIGNR for Cellular Attachment and Infection

“…DC-SIGNR is expressed on microvascular endothelial cells, especially in the liver sinusoids and lymph nodes (7,67,81). By facilitating virion attachment, DC-SIGN and DC-SIGNR [henceforth referred to collectively as DC-SIGN(R)] can greatly increase the susceptibility of permissive cells to infection by a wide array of enveloped viruses or allow nonpermissive cells to capture and transmit these viruses to target cells in trans (3,17,35,47,52,60,76,84).Viruses that bind to DC-SIGN(R) appear to do so via highmannose, N-linked glycans on their glycoproteins (44,48,51). This fact is readily explained by crystallographic studies demonstrating that mannose-rich oligosaccharides fit into elongated binding sites in the CRDs of DC-SIGN(R) (24).…”