The DC then transport the virus to the target T cells, maintaining the viral infectivity for up to four days. The virus finally infects the T cells, signaling the beginning of viral replication, without infecting the original dendritic cell. The authors suggest that DC-SIGN might induce a conformational change in the complex before the binding on the envelope glycoprotein, thus providing a more stable formation and increase in infectivity. Examination of the same effect on the envelope glycoprotein is also necessary, using various antibodies to the particular envelope as a comparison for viral infectivity. This internalization would protect the virus during migration to the lymphoid tissue.
Further research is necessary to determine which model, if either, is correct.
The antibodies could be added directly to the cells, only allowing for binding to externally located gp120 proteins. Then in another group of similar cells streptolysin-O can be used to open the plasma membrane and allow the antibodies to reach any internalized proteins. The amount of fluorescence in each condition can be compared. The necessity of DC-SIGN to act in a trans conformation versus a cis conformation must also be explicitly explored. Further research is necessary to study the effects of DC-SIGN in vivo.