RT Journal Article SR Electronic(1) A1 Ahi, Yadvinder S. A1 Vemula, Sai V. A1 Mittal, Suresh K.YR 2013 T1 Adenoviral E2 IVa2 protein interacts with L4 33K protein and E2 DNA-binding protein JF Journal of General Virology, VO 94 IS 6 SP 1325 OP 1334 DO https://doi.org/10.1099/vir.0.049346-0 PB Microbiology Society, SN 1465-2099, AB 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., UL https://www.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.049346-0