{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,12]],"date-time":"2026-03-12T01:22:11Z","timestamp":1773278531390,"version":"3.50.1"},"reference-count":42,"publisher":"Microbiology Society","issue":"6","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2013,6,1]]},"abstract":"<jats:p>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 <jats:italic>in vivo<\/jats:italic> 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.<\/jats:p>","DOI":"10.1099\/vir.0.049346-0","type":"journal-article","created":{"date-parts":[[2013,2,7]],"date-time":"2013-02-07T07:14:12Z","timestamp":1360221252000},"page":"1325-1334","source":"Crossref","is-referenced-by-count":21,"title":["Adenoviral E2 IVa2 protein interacts with L4 33K protein and E2 DNA-binding protein"],"prefix":"10.1099","volume":"94","author":[{"given":"Yadvinder S.","family":"Ahi","sequence":"first","affiliation":[{"name":"Department of Comparative Pathobiology, Purdue University Center for Cancer Research, and Bindley Bioscience Center, Purdue University, West Lafayette, IN, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sai V.","family":"Vemula","sequence":"additional","affiliation":[{"name":"Department of Comparative Pathobiology, Purdue University Center for Cancer Research, and 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