Characterization of solubilized proteins from tissue culture-and host-derived nuclear polyhedra of Lymantria dispar and Autographa californica.
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R A DiCapua
Publications and source records attributed to R A DiCapua.
Immunochemical characterization of Lymantri dispar NPV hemagglutinin: protein-carbohydrate interaction.
The agglutination of chicken erythrocytes by Lymantria dispar nuclear polyhedrosis virus polyhedrin has been shown to provide specific virus identification. Selected mono- and oligosaccharides, present in blood group substances, were assayed by the Land-steiner hapten inhibition technique for specific inhibition of polyhedrin hemagglutination. N-acetylgalactosamine and N-acetylglucosamine inhibit to the greatest extent; galactosamine, glucosamine and fucose to a lesser extent. The hapten inhibition data suggest that a monosaccharide possessing an equatorial 2-acetamido group interacts most avidly with the polyhedrin-combining site. Bergold demonstrated that the polyhedrin dissociates into six subunits at a pH greater than 10.0. Diafiltration equilibrium and Scatchard analysis indicate that N-acetylgalactosamine binds most avidly to the polyhedrin (Kd = 1.7 X 10(-6)) which contains six available sites, suggesting that one hemagglutination site resides on each subunit. Since virions derived in vivo and polyhedrin are serologically cross-reactive, this protein-carbohydrate interaction may play a role in host infectivity by providing a receptor site for virus attachment to target cells.
Acetylgalactosamine↗
Morphogenesis of marek's disease virus in feather follicle epithelium.
Three evaluative systems, immunodiffusion, fluorescent antibody (FA), and electron microscopy (EM), were used to follow the morphogenesis of Marek's disease virus in inoculated chickens. Of the three, EM and FA were the most sensitive in detecting early stages of infection. Virus particles were found in skin biopsy specimens as early as 12 days post inoculation. Immature naked particles appeared first in the nucleus; later particles were enveloped in the cytoplasm and enclosed in cytoplasmic inclusion bodies. No evidence for continued virus replication was seen in feather follicles after an initial burst of heavy virus production, which lasted several weeks. Residual virus, however, was found occasionally in cytoplasmic inclusion bodies within keratinized material near the feathers. This was believed to contribute to the long-term shedding of infectious virus into the environment.
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