We observed neither in Raji/DC-SIGN cells nor in MDDC antiviral Cinoxacin activity of AH against DENV. This indicates that AH interacts rather specifically with high-mannose N-glycans on HIV-1 glycoprotein gp120, but not with DENV glycoprotein E. The mAb 2G12 specifically recognizes a cluster of highmannose-type oligosaccharides on HIV-1 gp120. mAb 2G12 could inhibit HIV binding to Raji/DC-SIGN + cells and could also bind to yeast glycoproteins. We therefore assumed that mAb 2G12 could potentially recognize the E-protein of DENV, however no inhibitory effect on DENV was observed. We can thus conclude that not all CBAs interact with all types of glycosylated enveloped viruses. The lectins HHA, GNA and UDA have a broad spectrum antiviral activity against HIV, SIV, HCV, HCMV and DENV but not against parainfluenza-3, vesicular stomatitis virus, respiratory syncytial virus or herpes simplex virus. This may be because of differences in carbohydrate structures on the glycoproteins of the viral envelope of different viruses grown in different host cells. The glycosylation pattern in DENV differs from HIV because they replicate in mosquito cells and human cells, respectively. In vertebrate and invertebrate hosts the glycosylation process is fundamentally different. N-glycosylation in mammalian cells is often of the complex-type because a lot of different processing enzymes could add a diversity of monosaccharides. Glycans produced in insect cells are far less complex, because of less diversity in processing enzymes and usually contain more high-mannose and pauci-mannose-type glycans. When DENV is captured by DC, a maturation and activation process occurs. DC require downregulation of C-type lectin receptors, upregulation of costimulatory molecules, chemokine receptors and enhancement of their APC function 
to migrate to the nodal T-cell areas and activate the immune system. Cytokines implicated in Chloroquine Phosphate vascular leakage are produced, the complement system becomes activated and virus-induced antibodies can cause DHF via binding to Fc-receptors. Several research groups demonstrated maturation of DC induced by DENV infection. Some groups made segregation in the DC population after DENV infection, the infected DC and the uninfected bystander cells. They found that bystander cells, in contrast to infected DC, upregulate the cell surface expression of costimulatory molecules, HLA and maturation molecules. This activation is induced by TNF-a and IFN-a secreted by DENVinfected DC. We observed an upregulation of the costimulatory molecules CD80 and CD86 and a downregulation of DC-SIGN and MR on the total DC population following DENV infection. This could indicate that the DC are activated and can interact with naive T-cells and subsequently activate the immune system resulting in increased vascular permeability and fever. When we examined the effect of the CBAs on the expression level of the cell surface markers of the total DC population, we are able to inhibit the activation of all DC caused by DENV and keeping the DC in an immature state. Furthermore, DC do not express costimulatory molecules and can not interact nor activate T-cells. An approach to inhibit DENVinduced activation of DC may prevent the immunopathological component of DENV disease. Immunoglobulin G was previously shown to inhibit the differentiation and maturation of DC in vitro indicating that the DC activation process is an important target for controlling immune responses in several diseases. In conclusion, we observed broad spectrum antiviral activity of HHA, GNA and UDA against all four serotypes of DENV.