title: Distinct functional domains within the acidic cluster of tegument protein pp28 required for trafficking and cytoplasmic envelopment of human cytomegalovirus.
abstract: Human cytomegalovirus UL99-encoded tegument protein pp28 contains a 16 aa acidic cluster that is required for pp28 trafficking to the assembly compartment (AC) and the virus assembly. However, functional signals within the acidic cluster of pp28 remain undefined. Here, we demonstrated that an acidic cluster rather than specific sorting signals was required for trafficking to the AC. Recombinant viruses with chimeric pp28 proteins expressing non-native acidic clusters exhibited delayed viral growth kinetics and decreased production of infectious virus, indicating that the native acidic cluster of pp28 was essential for wild-type virus assembly. These results suggested that the acidic cluster of pp28 has distinct functional domains required for trafficking and for efficient virus assembly. The first half (aa 44-50) of the acidic cluster was sufficient for pp28 trafficking, whereas the native acidic cluster consisting of aa 51-59 was required for the assembly of wild-type levels of infectious virus.
authors.affiliation: Severance Biomedical Science Institute, Brain Korea 21 PLUS Project for Medical Science, Yonsei University College of Medicine, Seoul, Republic of Korea.
authors.forename: Jun-Young
authors.initials: JY
authors.lastname: Seo
authors.affiliation: Severance Biomedical Science Institute, Brain Korea 21 PLUS Project for Medical Science, Yonsei University College of Medicine, Seoul, Republic of Korea.
authors.forename: Hyejin
authors.initials: H
authors.lastname: Jeon
authors.affiliation: Severance Biomedical Science Institute, Brain Korea 21 PLUS Project for Medical Science, Yonsei University College of Medicine, Seoul, Republic of Korea.
authors.forename: Sookyung
authors.initials: S
authors.lastname: Hong
authors.affiliation: Departments of Pediatrics and Microbiology, School of Medicine, University of Alabama at Birmingham, Birmingham, AL, USA.
authors.forename: William J
authors.initials: WJ
authors.lastname: Britt
mesh_terms: D020816:Amino Acid Motifs; D003587:Cytomegalovirus / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D003586:Cytomegalovirus Infections / Q000821:virology*; D003593:Cytoplasm / Q000821:virology*; D006801:Humans; D010750:Phosphoproteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D021381:Protein Transport; D014764:Viral Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
chemical_list: D010750:Phosphoproteins; D014764:Viral Proteins; C070746:human cytomegalovirus protein pp28