Noncovalent SUMO-interaction motifs in HIV integrase play important roles in SUMOylation， cofactor binding， and virus replication.

HIV integrase (IN) and its cellular cofactors， including lens-epithelium-derived growth factor (LEDGF/p75)， Ku70， p300， and Rad52， are subject to small ubiquitin-like modifier (SUMO) modification. In addition to covalent SUMOylation， SUMO paralogs can also noncovalently bind proteins through SUMO-interacting motifs (SIMs). However， little is known about whether HIV IN contains SIMs and the roles of these motifs.

HIV replication，Human immunodeficiency virus (HIV)，Integrase (IN)，LEDGF/p75，Nuclear localization，Protein-protein interaction，SUMO-interacting motifs (SIMs)，SUMOyla