Human cytomegalovirus nuclear egress complex (NEC)

The **Human cytomegalovirus nuclear egress complex** is a heterodimeric viral protein assembly, primarily comprising the membrane-anchored **pUL50** and nucleoplasmic **pUL53** proteins, that forms at the inner nuclear membrane of infected host cells[1][2][3]. This complex acts as a scaffold, recruiting additional viral and cellular factors (such as kinases pUL97, PKC, CDK1) to orchestrate dramatic reorganization of the nuclear lamina, permit the docking and budding of viral capsids through the nuclear envelope, and facilitate the critical nuclear-to-cytoplasmic transit of newly formed viral particles[1][4][7]. The NEC is structurally and functionally conserved among herpesviruses and is considered essential for efficient viral replication and pathogenesis[1][4][7]. The pUL50–pUL53 interaction is highly specific, with pUL53’s N-terminal α-helical extension "hooking" into pUL50, and this interface is a potential target for antiviral drug development[2][3][9]. Current research identifies the NEC as a unique therapeutic target for novel anti-cytomegalovirus drugs, although NEC-specific inhibitors have yet to be clinically implemented[4][7][9].

Other names

HCMV nuclear egress complexHuman cytomegalovirus NECpUL50-pUL53 complex

Inhibition of associated viral kinase UL97 disrupts NEC function and nuclear egress[6] Direct binding to NEC subunits (hypothetical, as rational drugs are still in development)[7][9]