In contrast, binding of DC-SIGNR gave considerably larger Dhs at 20 mins (e.g., >200 and > 400 nm for G13-/G27-DiMan, respectively), which also showed significant increases with time (e.g., >600 and 900 nm for G13-/G27-DiMan at 160 min) and finally stayed at ∼700 nm at 320 min. Such Dh values were far too large to be individual Gx-DiMan coated with a monolayer of proteins, a strong indication of DC-SIGNR and G13/G27-DiMan crosslinking to form large GNP-lectin assemblies. Such crosslinking reactions happened over a relatively long period, leading to gradually increased assemblies over time and eventually precipitated out of the solution after 5 h (Fig. ). In contrast, DC-SIGN-Gx-DiMan assemblies were highly stable and showed no signs of precipitation after 5 h (Fig. ). Overall, these results indicated that the mode of G13/27-DiMan binding with DC-SIGN and DC-SIGNR were clearly different: DC-SIGN binds simultaneously with all four CRDs to a single Gx-DiMan and forms small, isolated single particles, whereas DC-SIGNR and Gx-DiMan crosslink each other to form large scale assemblies.