Glycosylation of purified enveloped nucleocapsids of the granulosis virus infecting Plodia interpunctella as determined by lectin binding.

Using various iodinated plant lectins and a sensitive in vitro lectin binding procedure in which the radiolabeled lectins are applied directly to viral proteins on nitrocellulose sheets transferred from sodium dodecyl sulfate-polyacrylamide gels (Bartles and Hubbard, 1984; Glass et al., 1981), the proteins of the granulosis virus infecting Plodia interpunctella were probed for carbohydrate moieties. Six proteins (Mr 39 700, 31 000, 29 900, 26 300, 17 800 and 12 600) could be detected using a probe for alpha-D-N-acetylgalactosamine. Three proteins were also detectable with the probe specific for alpha-L-fucose (Mr 44 900, 31 000 and 17 800). One protein (Mr 17 800) was detected with the probe for sialic acid.