Characterization of the structural proteins of hemorrhagic enteritis virus.

The structural proteins of hemorrhagic enteritis (HEV), a turkey adenovirus, were analyzed by polyacrylamide gel electrophoresis (PAGE) and Western blotting using polyspecific, monospecific and monoclonal antibodies for detection. In purified HEV preparations, eleven polypeptides with apparent molecular weights ranging from 96,000 to 9,500 (96k to 9.5k), were specifically recognized by convalescent turkey serum. Six of these polypeptides were further characterized by PAGE, Western blotting, ELISA, sucrose gradient centrifugation and electron microscopy. The 96k polypeptide was identified as the hexon polypeptide which is a monomer of the major outer capsid or hexon protein. The 51/52k and 29k polypeptides, identified as the penton base and fiber polypeptides respectively, were the components of the vertex or penton protein. The 57k polypeptide was identified as a homologue of the human adenovirus type 2 (Ad 2) IIIa protein with which it shares a common epitope. Two core proteins with molecular weights of 12.5 and 9.5k were present in purified HEV nucleoprotein cores. The proteins of two HEV isolates, one apathogenic (HEV-A) and one virulent (HEV-V), resembled each other in most respects. However, differences between HEV-A and HEV-V were found in electrophoretic migration of the penton base protein both under native and denatured conditions, and in the electrophoretic migration of the 43/44k polypeptide. Moreover, homologous antiserum against the fiber protein reacted stronger than heterologous antiserum in an ELISA. Single fibers were detected by electron microscopy attached to the penton base proteins of HEV virions and in isolated pentons. The feature of having single fibers is shared with the mammalian adenoviruses and the avian egg drop syndrome 1976 virus (EDS 76 V), but not with the fowl adenoviruses which have double fibers attached to their penton base proteins.