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Short Communication |
1 Albert Einstein College of Medicine, Microbiology and Immunology Department, 1300 Morris Park Avenue, Bronx, NY 10461, USA
2 Progenics Pharmaceuticals Inc., 777 Old Saw Mill River Road, Tarrytown, NY 10591, USA
Correspondence
Tatjana Dragic
tdragic{at}aecom.yu.edu
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Present address: GlaxoSmithKline R&D, B38 2 58, Greenford Road, London UB6 0HE, UK. 
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; Lechner et al., 2000). These individuals may remain asymptomatic or they may develop chronic hepatitis or cirrhosis, the latter often leading to hepatocellular carcinoma (Fry & Flint, 1997). Hepatocytes are the major target cells of HCV (Boisvert et al., 2001; Fournier et al., 1998; Ikeda et al., 1998) and the tissue tropism of the virus is restricted by the envelope glycoproteins E1 and E2 (E1E2) (Lavillette et al., 2005; McKeating et al., 2004). E1 has homologies to the class II fusion proteins of other flaviviruses and alphaviruses (Garry & Dash, 2003). E2 is a receptor-binding subunit with affinity for CD81 (Pileri et al., 1998), which serves as an entry co-receptor for HCV (Cormier et al., 2004b; McKeating et al., 2004) and additional molecules implicated in HCV entry (Bartosch et al., 2003; Lavillette et al., 2005; Scarselli et al., 2002). We and others have demonstrated that L-SIGN (liver/lymph node-specific, intercellular adhesion molecule-3-grabbing non-integrin, CD209L or DC-SIGNR) also binds soluble HCV E2 (sE2) and mediates trans-infection of liver cells by HCV pseudoparticles (HCVpp) (Cormier et al., 2004a; Gardner et al., 2003; Lozach et al., 2003, 2004; Pohlmann et al., 2003). L-SIGN may concentrate HCV in the liver and enable captured virus to cross the endothelial barrier, thereby facilitating infection of adjacent hepatocytes.
L-SIGN and DC-SIGN (dendritic cell-specific, CD209) are homologous type II membrane proteins characterized by a carboxyl-terminal carbohydrate-recognition domain (CRD), a juxtamembrane oligomerization or ‘neck’ domain, a single transmembrane-spanning domain and a short cytoplasmic tail. L-SIGN is expressed on liver sinusoidal endothelial cells (Bashirova et al., 2001; Pohlmann et al., 2001b; Soilleux et al., 2000), which are specialized non-myeloid antigen-presenting cells involved in immune surveillance (Knolle & Gerken, 2000). DC-SIGN is important for activation of resting T cells (Geijtenbeek et al., 2000a). In addition, the SIGN molecules act as receptors for certain viral and non-viral pathogens by binding high-mannose and related surface glycans. For Human immunodeficiency virus 1 (HIV-1), the SIGN molecules do not act as conventional entry receptors. Instead, SIGN-expressing cells capture virus and facilitate its delivery to, and trans-infection of, susceptible target cells (Geijtenbeek et al., 2000b; Pohlmann et al., 2001a, b).
L-SIGN gene polymorphisms have been identified that differ in the number of repeats of a 69 bp sequence in the neck region (Bashirova et al., 2001; Feinberg et al., 2005; Liu & Zhu, 2005). Each repeat encodes a hydrophobic heptad motif characteristic of 
-helical coiled coils (Feinberg et al., 2005; Mitchell et al., 2001). In Caucasians, the most common L-SIGN allele encodes seven repeat segments (L-SIGN-7) and comprises just over 50 % of all alleles. Other alleles encode from three to nine tandem repeats (L-SIGN-3 to L-SIGN-9) and vary in frequency from 0.3 (L-SIGN-3) to 29 % (L-SIGN-5) (Bashirova et al., 2001). Little is known about the expression and function of these L-SIGN isoforms at the cell surface. Fig. 1 depicts the domain structures of the proteins encoded by the L-SIGN isoforms examined in this study. The 23 aa repeat segments are numbered relative to those encoded by L-SIGN-7, with the first repeat beginning at Ile-89 (Mummidi et al., 2001).
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; Gardner et al., 2003). DNAs encoding the 3-, 4-, 5- and 9-repeat forms of L-SIGN were synthesized chemically (DNA 2.0) and subcloned into the pcDNA3.1 expression vector (Invitrogen). HeLa cells were modified to express L-SIGN isoforms stably and analysed by flow cytometry following staining with monoclonal antibodies (mAbs). Using mAb 120604 to the CRD (R&D Systems), each of the isoforms was detected at high levels, demonstrating that the proteins were expressed efficiently and transported to the cell surface (Fig. 2a). Similar results were obtained using another CRD-specific mAb (120612; R&D Systems), as well as mAb DC28 (R&D Systems) to the repeat region (data not shown). Expression of all alleles was calculated relative to L-SIGN-7 (Fig. 2b) and these expression ratios were used to normalize sE2 binding and trans-infection with HCVpp. Moreover, non-quantitative Western blots were performed with mAb DC28 to confirm that L-SIGN isoforms expressed in HeLa cells differed in size, as expected (Fig. 2c). When deglycosylated, each L-SIGN isoform migrated as one major band consistent with its expected molecular mass. Multiple major bands were observed in the absence of N-glycosidase F (PNGase F) treatment for most isoforms and suggest glycosylation variants. The molecular mass observed for untreated L-SIGN-7 was consistent with prior reports (Pohlmann et al., 2001b).
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; Gardner et al., 2003). Here, we used a flow-cytometry method to examine binding of sE2 to L-SIGN isoforms, according to a protocol previously described by us (Gardner et al., 2003). Detection of sE2 capture by L-SIGN relied on anti-E2 mAb 091a-5 (Austral) coupled to FluoSpheres (Molecular Probes). This mAb does not detect sE2 bound to CD81; hence the low expression level of this viral receptor on HeLa cells did not interfere with our assay. The mean MFI observed for parental HeLa cells was 5±3, whereas levels of specific binding to L-SIGN transfectants were 9- to 25-fold above background binding. Moreover, binding of sE2 was normalized for L-SIGN isoform-expression ratios that were measured in parallel within each experiment. Soluble E2 glycoprotein bound all isoforms but with different efficiencies (Fig. 3a). The strongest binding was to L-SIGN-7, whereas the weakest binding was exhibited by isoform 3 and this difference was statistically significant (P=0.04). The differences observed between L-SIGN-7 and the other three isoforms followed a trend towards significance (0.1<P<0.2). All statistical analyses were performed using an unpaired t-test to calculate two-tailed P values.
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; Gardner et al., 2003). Briefly, cells were incubated with purified and concentrated HCVpp in a binding buffer and then washed extensively to remove unbound virus. Cell lysates were analysed for HIV-1 p24 content using the Coulter HIV-1 p24 antigen assay (Beckman Coulter). Background binding to parental HeLa cells was 546±98 ng ml–1. In contrast, binding to L-SIGN-positive cells was significantly higher and also different between the two alleles. Mean p24 values from three independent experiments were 960±126 ng ml–1 for HeLa–L-SIGN-3 cells and 2006±159 ng ml–1 for HeLa–L-SIGN-7 cells (P=0.01). These differences remained significant even when normalized for expression levels of the two alleles (1247 versus 2006 ng ml–1) (Fig. 3a
, below x axis). Note that the input amount of HCVpp-associated p24 was 10 µg ml–1, resulting in approximately 10 and 20 % capture efficiencies of pseudoparticles by HeLa–L-SIGN-3 and -7 cells, respectively.
Parental HeLa cells and HeLa-SIGN transfectants then were analysed for their abilities to mediate trans-infection of Huh-7 hepatoma cells by HCVpp bearing the envelope glycoproteins of the H77 1a isolate, as described previously (Cormier et al., 2004a). Trans-infection levels were normalized for L-SIGN allele-expression levels and a pattern similar to the one observed for sE2 and HCVpp binding emerged (Fig. 3b). The highest levels of trans-infection were mediated by L-SIGN-7-expressing HeLa cells, followed by L-SIGN-9, -5, -4 and -3. The difference between the trans-infection efficiencies of L-SIGN-7 and L-SIGN-9 was not statistically significant (P=0.577). However, differences between L-SIGN-7 and the other isoforms were statistically significant: L-SIGN-3 (P=0.0001), L-SIGN-4 (P=0.002) and L-SIGN-5 (P=0.003).
In order to ascertain that trans-infection was mediated specifically by L-SIGN isoforms, it was also examined in the presence of >IC90 concentrations of agents that bind the CRD (Cormier et al., 2004a). Mannan (Sigma), as well as mAbs 120604 and 120612, efficiently blocked trans-infection mediated by each of the L-SIGN isoforms (Fig. 3b). The level of trans-infection was inhibited by 58–100 % for mAb 120604, 68–100 % for mAb 120602 and 48–82 % for mannan. In contrast, isotype-control mouse IgG had no effect on trans-infection and was used as the positive control in Fig. 3(b). There was no obvious variation between the different isoforms in the potency of the inhibitors at the concentrations used. The data indicated that L-SIGN-3, -4, -5 and -9 mediated trans-infection via interactions between their CRD and HCVpp, as observed previously for L-SIGN-7 (Cormier et al., 2004a; Lozach et al., 2004).
This report evaluated the expression and function in mammalian cells of L-SIGN variants that comprised three, four, five, seven or nine oligomerization domain repeats. We demonstrated that alleles encoding the five isoforms were translated efficiently and correctly, were exported to the surface of HeLa cells and were reactive with mAbs to the CRD and repeat region. Each of these isoforms bound different levels of HCV sE2. The statistically significant difference observed between isoforms 3 and 7 was confirmed by their different efficiencies at capturing HCVpp. Capture differences translated into different trans-infection efficiencies of liver cells by HCVpp. Soluble E2 binding, HCVpp capture and trans-infection were highest for L-SIGN-7, decreased with progressive deletions of tandem repeats and were lowest for L-SIGN-3.
Variations in HCVpp capture and trans-infection could reflect differences in the oligomeric states of the L-SIGN isoforms and support for this notion is provided by recent studies. Cell-surface L-SIGN-7 and DC-SIGN exist as tetramers (Bernhard et al., 2004; Feinberg et al., 2005; Mitchell et al., 2001), as do recombinant, soluble forms of these proteins (Feinberg et al., 2005; Mitchell et al., 2001; Snyder et al., 2005). A recent study showed a gradual increase in the ability of L-SIGN isoforms with four, five, six or seven repeats to form stable tetramers (Guo et al., 2006). Moreover, soluble SIGN molecules containing one to two tandem repeats form monomers and dimers, whereas a five-repeat version of soluble DC-SIGN forms a mixture of dimers and tetramers (Feinberg et al., 2005; Snyder et al., 2005). It appears, therefore, that increasing the number of repeats increases the oligomerization state of SIGN receptors, which may affect their avidity for glycan ligands. In the context of soluble L-SIGN proteins, the number of tandem repeats has been reported to influence binding affinity for HIV-1 gp120 (Snyder et al., 2005).
Our findings may have implications for the transmission and pathogenesis of HCV. As proposed previously, L-SIGN may capture HCV in the liver and deliver virus to susceptible hepatocytes (Gardner et al., 2003; Lozach et al., 2003, 2004; Pohlmann et al., 2003). L-SIGN isoforms could influence the in vivo process by mediating trans-infection with varying efficiencies. Polymorphisms in L-SIGN and DC-SIGN could thereby afford protection against HCV infection and disease progression, and future studies will examine whether L-SIGN repeat-region gene polymorphisms are more prevalent in high-risk individuals who remain uninfected or in individuals who resolve disease. In addition, polymorphisms in L-SIGN and DC-SIGN could affect HCV disease by modulating host immune responses to the virus.
Similarly, direct infection and trans-infection by other pathogens may be affected by L-SIGN polymorphisms. L-SIGN and DC-SIGN bind to or facilitate infection by a diverse array of viral and non-viral pathogens, including HIV-1 and other primate lentiviruses (Baribaud et al., 2001; Geijtenbeek et al., 2000b; Lee et al., 2001), Ebola virus (Alvarez et al., 2002), Marburg virus (Marzi et al., 2004), Dengue virus (Tassaneetrithep et al., 2003), severe acute respiratory syndrome coronavirus (SARS-CoV) (Marzi et al., 2004; Yang et al., 2004), cytomegalovirus (Halary et al., 2002), Sindbis virus (Klimstra et al., 2003), Leishmania amastigotes (Colmenares et al., 2002), Mycobacterium tuberculosis (Geijtenbeek et al., 2003), Candida albicans (Cambi et al., 2003), Helicobacter pylori (Bergman et al., 2004) and Aspergillus fumigatus (Serrano-Gomez et al., 2004). We note, however, that a recent in vitro study by Gramberg et al. (2006) did not find a significant difference in cis-infection by SARS-CoV and Ebola or trans-infection of HIV-1 mediated by L-SIGN isoforms 5, 6 and 7. Moreover this group did not find major differences in the oligomerization states of the different isoforms. Other recent studies, however, have demonstrated that gene polymorphisms in DC-SIGNR and DC-SIGN affect viral transmission and load in vivo (Liu et al., 2004, 2006; Martin et al., 2004). Homozygosity for L-SIGN-7 was associated with increased risk of HIV-1 infection, while heterozygosity for L-SIGN-7 and -5 conferred protection against infection (Liu et al., 2006). A rare six-repeat form of DC-SIGN (DC-SIGN-6) was shown to confer protection against mucosal infection by HIV-1 (Liu et al., 2004). In another study, a promoter-region polymorphism (–336C) in DC-SIGN was associated with an increased risk of parenteral but not mucosal infection by HIV-1 (Martin et al., 2004). The DC-SIGN –336G allele was recently shown to modulate the severity of disease mediated by dengue virus infection (Sakuntabhai et al., 2005). Finally, Nattermann et al. (2006) recently reported that HCV-infected patients carrying L-SIGN alleles 5, 6 and 7 had higher viral loads compared with carriers of alleles 4 and 9. This finding is generally consistent with the pattern of trans-infection that we observed, but for allele 9, which behaves similarly to allele 7. The reasons for this discrepancy could be molecular or immunological and remain to be determined. Overall, the cited reports are consistent with the model whereby capture of pathogens by C-type lectins can assist their dissemination to and infection of target cells (Geijtenbeek et al., 2000b). Our findings support a molecular mechanism whereby genetic polymorphisms could impact diseases caused by HCV and other pathogens recognized by L-SIGN and DC-SIGN.
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ACKNOWLEDGEMENTS |
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Received 15 March 2006;
accepted 5 May 2006.
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