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Novel Member of the CD209 (DC-SIGN) Gene Family in Primates

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TLDR
The data suggest that the CD209 gene family has undergone recent evolutionary processes involving duplications and deletions, the latter of which may be tolerated because of potentially redundant functional activities of the molecules encoded by these genes.
Abstract
Two CD209 family genes identified in humans, CD209 (DC-SIGN) and CD209L (DC-SIGNR/L-SIGN), encode C-type lectins that serve as adhesion receptors for ICAM-2 and ICAM-3 and participate in the transmission of human and simian immunodeficiency viruses (HIV and SIV, respectively) to target cells in vitro. Here we characterize the CD209 gene family in nonhuman primates and show that recent evolutionary alterations have occurred in this family across primate species. All of the primate species tested, specifically, Old World monkeys (OWM) and apes, have orthologues of human CD209. In contrast, CD209L is missing in OWM but present in apes. A third family member, that we have named CD209L2, was cloned from rhesus monkey cDNA and subsequently identified in OWM and apes but not in humans. Rhesus CD209L2 mRNA was prominently expressed in the liver and axillary lymph nodes, although preliminary data suggest that levels of expression may vary among individuals. Despite a high level of sequence similarity to both human and rhesus CD209, rhesus CD209L2 was substantially less effective at binding ICAM-3 and poorly transmitted HIV type 1 and SIV to target cells relative to CD209. Our data suggest that the CD209 gene family has undergone recent evolutionary processes involving duplications and deletions, the latter of which may be tolerated because of potentially redundant functional activities of the molecules encoded by these genes.

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Journal ArticleDOI

The C-type lectin-like domain superfamily

TL;DR: The superfamily of proteins containing C‐type lectin‐like domains (CTLDs) is a large group of extracellular Metazoan proteins with diverse functions that have evolved to specifically recognize protein, lipid and inorganic ligands, including the vertebrate clade‐specific snake venoms, and fish antifreeze and bird egg‐shell proteins.
Journal ArticleDOI

Raji B cells, misidentified as THP-1 cells, stimulate DC-SIGN-mediated HIV transmission.

TL;DR: It is demonstrated that true THP-1 cells do not support DC-SIGN-mediated HIV-1 transmission, whereas human B cell lines efficiently enhance this process, indicating that there are features common to B cells and DCs that facilitate transmission of HIV- 1.
Journal Article

DC-SIGN and immunoregulation.

TL;DR: In this article, the C-type lectin superfamily of Dendritic cells (DCs) has been shown to play an important role in mediating DC adhesion, migration, inflammation, activating primary T cell, triggering immune response and participating in immune escape of pathogens and tumors.
Journal ArticleDOI

DC-SIGN and L-SIGN: the SIGNs for infection

TL;DR: Findings support the tandem-neck-repeat region of L-SIGN as an excellent candidate acting as a functional target for selective pressures exerted by pathogens.
References
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Journal ArticleDOI

The neighbor-joining method: a new method for reconstructing phylogenetic trees.

TL;DR: The neighbor-joining method and Sattath and Tversky's method are shown to be generally better than the other methods for reconstructing phylogenetic trees from evolutionary distance data.
Journal ArticleDOI

DC-SIGN, a dendritic cell-specific HIV-1-binding protein that enhances trans-infection of T cells

TL;DR: It is proposed that DC-SIGN efficiently captures HIV-1 in the periphery and facilitates its transport to secondary lymphoid organs rich in T cells, to enhance infection in trans of these target cells.
Journal ArticleDOI

Identification of DC-SIGN, a Novel Dendritic Cell–Specific ICAM-3 Receptor that Supports Primary Immune Responses

TL;DR: It is demonstrated that ICAM-3 expressed by resting T cells is important in this first contact with dendritic cells, and it is predicted that DC-SIGN enables T cell receptor engagement by stabilization of the DC-T cell contact zone.
Journal ArticleDOI

Vpr is required for efficient replication of human immunodeficiency virus type-1 in mononuclear phagocytes.

TL;DR: It is shown that vpr is important for efficient viral replication in primary monocyte/macrophages, but appears to play no role in activated or resting T cell infection, and a role for vpr molecules produced in newly infected cells is suggested, in addition to its presumed function in the virion.
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