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

Marzi, Andrea; Gramberg, Thomas; Simmons, Graham; Möller, Peggy; Rennekamp, Andrew J.; Krumbiegel, Mandy; Geier, Martina; Eisemann, Jutta; Turza, Nadine; Saunier, Bertrand; Steinkasserer, Alexander; Becker, Stephan; Bates, Paul; Hofmann, Heike; Pöhlmann, Stefan

doi:10.1128/jvi.78.21.12090-12095.2004

Cited by 369 publications

(398 citation statements)

References 62 publications

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“…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.…”

Section: Discussionmentioning

confidence: 99%

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

Lin

Xiang

Wang

et al. 2009

The Journal of Immunology

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Dendritic cell-specific ICAM-3-grabbing nonintegrin (DC-SIGN/CD209) has become hot topic in recent studies because of its important roles in immune responses and immune escape. CD209 has been well characterized in humans and several other mammals, but little documentation exists about it in lower vertebrates. This is the first report on the identification and functional characterization of a fish DC-SIGN/CD209 molecule. The zebrafish DC-SIGN/CD209 cDNA translates into 343 aa organized into three domains structurally conserved among vertebrates. An EPN motif essential for interacting with Ca2+ and for recognizing mannose-containing motifs has been identified. Several conserved motifs crucial for internalization and signal transduction are also present within the cytoplasmic tail. Phylogenetic analysis supports the hypothesis that CD209 family members diverged from a common ancestor. The expression of DC-SIGN/CD209 in immune-related tissues can be significantly up-regulated by exogenous Ags and IL-4. This molecule associates with various APCs, including macrophages, B lymphocytes, and a possible dendritic cell-like (CD83+/CD80+CD209+) population. Functionally, T cell activation, Ab (IgM) production, and bacterial vaccination-elicited immunoprotection can be dramatically inhibited by a CD209 blockade after stimulation with keyhole limpet hemocyanin (KLH) in vivo or challenged with Aeromonas hydrophila, suggesting that DC-SIGN/CD209 in zebrafish is crucial for the initiation and development of adaptive immunity. Phagocytosis analysis showed that DC-SIGN/CD209 does not participate in the uptake of KLH Ag, suggesting that other mechanisms might exist that underlie DC-SIGN/CD209 involvement. We hope that the present study will contribute to a better cross-species understanding of the evolutionary history of the DC-SIGN/CD209 family.

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Section: Discussionmentioning

confidence: 99%

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

Lin

Xiang

Wang

et al. 2009

The Journal of Immunology

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“…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).…”

mentioning

confidence: 99%

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

Kuhn

Radoshitzky

Guth

et al. 2006

Journal of Biological Chemistry

120

136

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The GP 1,2 envelope glycoproteins (GP) of filoviruses (marburg-and ebolaviruses) mediate cell-surface attachment, membrane fusion, and entry into permissive cells. Here we show that a 151-amino acid fragment of the Lake Victoria marburgvirus GP 1 subunit bound filoviruspermissive cell lines more efficiently than full-length GP 1 . An homologous 148-amino acid fragment of the Zaire ebolavirus GP 1 subunit similarly bound the same cell lines more efficiently than a series of longer GP 1 truncation variants. Neither the marburgvirus GP 1 fragment nor that of ebolavirus bound a nonpermissive lymphocyte cell line. Both fragments specifically inhibited replication of infectious Zaire ebolavirus, as well as entry of retroviruses pseudotyped with either Lake Victoria marburgvirus or Zaire ebolavirus GP 1,2 . These studies identify the receptor-binding domains of both viruses, indicate that these viruses utilize a common receptor, and suggest that a single small molecule or vaccine can be developed to inhibit infection of all filoviruses.

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“…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).…”

mentioning

confidence: 99%

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

Davis

Nguyen

Hanna

et al. 2006

J Virol

301

307

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The C-type lectins DC-SIGN and DC-SIGNR bind mannose-rich glycans with high affinity. In vitro, cells expressing these attachment factors efficiently capture, and are infected by, a diverse array of appropriately glycosylated pathogens, including dengue virus. In this study, we investigated whether these lectins could enhance cellular infection by West Nile virus (WNV), a mosquito-borne flavivirus related to dengue virus. We discovered that DC-SIGNR promoted WNV infection much more efficiently than did DC-SIGN, particularly when the virus was grown in human cell types. The presence of a single N-linked glycosylation site on either the prM or E glycoprotein of WNV was sufficient to allow DC-SIGNR-mediated infection, demonstrating that uncleaved prM protein present on a flavivirus virion can influence viral tropism under certain circumstances. Preferential utilization of DC-SIGNR was a specific property conferred by the WNV envelope glycoproteins. Chimeras between DC-SIGN and DC-SIGNR demonstrated that the ability of DC-SIGNR to promote WNV infection maps to its carbohydrate recognition domain. WNV virions and subviral particles bound to DC-SIGNR with much greater affinity than DC-SIGN. We believe this is the first report of a pathogen interacting more efficiently with DC-SIGNR than with DC-SIGN. Our results should lead to the discovery of new mechanisms by which these well-studied lectins discriminate among ligands.The first step in viral entry is the stable attachment of the virion to the surface of a new target cell, a process that can be inefficient for many viruses (16,34,62,73). Cellular proteins that facilitate productive infection by increasing the efficiency of virus binding, but whose presence is not absolutely required for viral entry, are often referred to as attachment factors (4). Two of the most extensively studied attachment factors are the lectins DC-SIGN (CD209) (18, 29) and DC-SIGNR (L-SIGN) (CD209L) (7,67,78). Both are tetrameric type II transmembrane proteins containing calcium-dependent (C-type) carbohydrate recognition domains (CRDs) (55). DC-SIGN is highly expressed in monocyte-derived dendritic cells (MDDCs) in vitro (29) and at lower levels (86) in vivo in subsets of macrophages (45,53,79) and dendritic cells (23,29,40,80,86). 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). In addition to recognizing viral...

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

Cited by 369 publications

References 62 publications

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

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

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

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

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