Cytomegaloviral proteins that associate with the nuclear lamina: components of a postulated nuclear egress complex

• DOI: 10.1099/vir.0.005231-0
• Publication Date: 2009-02-13T02:10:33Z
• Authors: Jens Milbradt; Sabrina Auerochs; Heinrich Sticht; Manfred Marschall
• Keywords: Nuclear lamina; Nuclear pore; Colocalization; Immunoprecipitation; Inner membrane

The nuclear egress of cytomegaloviral capsids traversing the envelope is dependent on a locally restricted destabilization rigid lamina. It has been suggested that multi-component complex (NEC) formed comprised both viral and cellular proteins which act to recruit lamin-phosphorylating protein kinases. Recently, we reported lamina-associated human cytomegalovirus-encoded pUL50 pUL53, conserved among herpesviruses, interact with each other kinase C (PKC) in transfected cells. multiple interactions transmembrane PKC PKC-binding p32, appear crucial formation NEC. In this study, mapped individual interaction sequence elements by coimmunoprecipitation analysis deletion mutants yeast two-hybrid studies. Amino acids 1-250 were shown be responsible for 100-280 100-358 p32. Interestingly, p32 specifically interacted NEC components, including kinases pUL97, thus possibly acting as an adaptor recruitment lamin B receptor. Notably, was only Immunofluorescence studies visualized colocalization components at rim coexpression data imply tight between least six leads postulated multi-protein required egress.