Physicochemical properties and location of capsule components, in particular the synergistic factor, in the occlusion body of a granulosis virus of the armyworm, Pseudaletia unipuncta.
A synergistic strain of granulosis virus (GVH) enhances the infection of larvae of the armyworm, Pseudaletia unipuncta, with a nuclear polyhedrosis virus (NPV). The matrix of the capsule (occlusion body) of GVH contains two major components, the structural protein and the synergistic factor. The structure of the capsule matrix of GVH was analyzed with a primary amine-coupling reagent, 2,4,6,-trinitrobenzene 1-sulfonic acid (TNBS). When undissolved capsules are incubated with TNBS, only the structural protein is labeled by TNBS. This indicates that the synergistic factor is not accessible to TNBS. Tests with the isolated capsule components show that the synergistic factor is more soluble than the structural protein at neutral pH. The synergistic factor has a strong affinity for viral envelopes. The attachment of about eight molecules of the synergistic factor to each enveloped NPV greatly enhances the infectivity of the virus.
Yamamoto
T
T
Department of Entomological Sciences, University of California, Berkeley, California 94720, USA.
Tanada
Y
Y