title: Amino acid exchanges in the putative nuclear export signal of adenovirus type 5 L4-100K severely reduce viral progeny due to effects on hexon biogenesis.
abstract: The adenovirus type 5 nonstructural L4-100K protein is indispensable for efficient lytic infection. During the late phase, L4-100K promotes selective translation of viral late transcripts and mediates the trimerization of the major capsid protein hexon. In the present study, the role of a potential nuclear export signal in L4-100K was investigated. Intriguingly, amino acid substitutions in this sequence resulted in severely diminished progeny virus production, seemingly by precluding proper hexon biogenesis.
authors.affiliation: Heinrich Pette Institute for Experimental Virology, Hamburg, Germany.
authors.forename: Orkide O
authors.initials: OO
authors.lastname: Koyuncu
authors.forename: Thomas
authors.initials: T
authors.lastname: Speiseder
authors.forename: Thomas
authors.initials: T
authors.lastname: Dobner
authors.forename: Melanie
authors.initials: M
authors.lastname: Schmid
mesh_terms: D000260:Adenoviruses, Human / Q000235:genetics / Q000502:physiology*; D019943:Amino Acid Substitution; D036022:Capsid Proteins / Q000378:metabolism*; D050505:Mutant Proteins / Q000235:genetics / Q000378:metabolism; D049790:Nuclear Export Signals; D055503:Protein Multimerization; D017361:Viral Nonstructural Proteins / Q000235:genetics / Q000378:metabolism*
chemical_list: D036022:Capsid Proteins; C477284:L4-100K protein, adenovirus type 5; D050505:Mutant Proteins; D049790:Nuclear Export Signals; D017361:Viral Nonstructural Proteins; C018315:hexon capsid protein, Adenovirus