title: Adenoviral E2 IVa2 protein interacts with L4 33K protein and E2 DNA-binding protein.
abstract: Adenovirus (AdV) is thought to follow a sequential assembly pathway similar to that observed in dsDNA bacteriophages and herpesviruses. First, empty capsids are assembled, and then the genome is packaged through a ring-like structure, referred to as a portal, located at a unique vertex. In human AdV serotype 5 (HAdV5), the IVa2 protein initiates specific recognition of viral genome by associating with the viral packaging domain located between nucleotides 220 and 400 of the genome. IVa2 is located at a unique vertex on mature capsids and plays an essential role during genome packaging, most likely by acting as a DNA packaging ATPase. In this study, we demonstrated interactions among IVa2, 33K and DNA-binding protein (DBP) in virus-infected cells by in vivo cross-linking of HAdV5-infected cells followed by Western blot, and co-immunoprecipitation of IVa2, 33K and DBP from nuclear extracts of HAdV5-infected cells. Confocal microscopy demonstrated co-localization of IVa2, 33K and DBP in virus-infected cells and also in cells transfected with IVa2, 33K and DBP genes. Immunogold electron microscopy of purified HAdV5 showed the presence of IVa2, 33K or DBP at a single site on the virus particles. Our results provide indirect evidence that IVa2, 33K and DBP may form a complex at a unique vertex on viral capsids and cooperate in genome packaging.
authors: Department of Comparative Pathobiology, Purdue University Center for Cancer Research, and Bindley Bioscience Center, Purdue University, West Lafayette, IN, USA.
authors: Yadvinder S
authors: YS
authors: Ahi
authors: Department of Comparative Pathobiology, Purdue University Center for Cancer Research, and Bindley Bioscience Center, Purdue University, West Lafayette, IN, USA.
authors: Sai V
authors: SV
authors: Vemula
authors: Department of Comparative Pathobiology, Purdue University Center for Cancer Research, and Bindley Bioscience Center, Purdue University, West Lafayette, IN, USA.
authors: Suresh K
authors: SK
authors: Mittal
mesh_terms: D017502:Adenovirus E2 Proteins / Q000235:genetics / Q000378:metabolism*; D000258:Adenovirus Infections, Human / Q000821:virology*; D000260:Adenoviruses, Human / Q000235:genetics / Q000378:metabolism*; D002460:Cell Line; D006801:Humans; D011485:Protein Binding; D017361:Viral Nonstructural Proteins / Q000235:genetics / Q000378:metabolism*; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism*
chemical_list: D017502:Adenovirus E2 Proteins; C582538:L4-33K protein, adenovirus type 5; D017361:Viral Nonstructural Proteins; D014764:Viral Proteins; C056232:iva2 protein, adenovirus