Specific Residues of a Conserved Domain in the N Terminus of the Human Cytomegalovirus pUL50 Protein Determine Its Intranuclear Interaction with pUL53

• DOI: 10.1074/jbc.m111.331207
• Publication Date: 2012-05-16T00:18:19Z
• Authors: Jens Milbradt; Sabrina Auerochs; Madhumati Sevvana; Yves A. Muller; Heinrich Sticht; Manfred Marschall
• Keywords: Conserved sequence

Herpesviral capsids are assembled in the host cell nucleus and subsequently translocated to cytoplasm. During this process it has been demonstrated that human cytomegalovirus proteins pUL50 pUL53 interact form, together with other viral cellular proteins, nuclear egress complex at envelope. In study we provide evidence specific residues of a conserved N-terminal region determine its intranuclear interaction pUL53. silico evaluation biophysical analyses suggested forms regular secondary structure adopting globular fold. Importantly, site-directed replacement individual amino acids by alanine indicated strong functional influence inside domain. particular, mutation widely Glu-56 or Tyr-57 led loss Consistent binding properties, mutants E56A Y57A showed defective function recruitment envelope expression plasmid-transfected cytomegalovirus-infected cells. addition, analysis 3-20 form an amphipathic α-helix appears be among Herpesviridae. Point revealed structural role for stability rather than direct contrast, central part domain including is directly responsible thus determines formation basic complex.