Human SP110 plays an important role in resisting intracellular pathogens, and hence has become an important drug target for preventing intracellular pathogen diseases, such as tuberculosis, hepatic veno-occlusive disease, and intracellular cancers. Unfortunately, so far little is known about the interactions of SP110 with the other proteins in a cell, which is considered to be the key for revealing its action mechanism and mediated pathway. Using both the genetic and structural analyses as well as the segment-docking approach, we have identified two proteins: the human remodeling and spacing factor 1 (RSF1) and the activating transcription factor 7 interacting protein (ATF7IP). They are very likely interacting with human SP110 during the process of viral infections. Owing to the close relationship of RSF1 with the chromatin remodeling and ATF7IP with the chromatin formation, it is logical to infer that human SP110 may be involved in the chromatin remodeling and formation as well. These findings may provide useful insights into the development of new drugs for treating and preventing intracellular pathogen diseases.
Keywords: Intracellular pathogen, mycobacterium tuberculosis, hepatic veno-occlusive disease, intracellular cancer, segment docking, genetic/structural analysis, SP110, interactions, proteins, ATF7IP, viral infections, chromatin remodeling