Autographa californica Nuclear Polyhedrosis Virus Structural Proteins Compared from in vivo and in vitro Sources

Abstract

Polyhedrin obtained from A. californica nuclear polyhedrosis virus was apparently not modified in terms of primary structure after passage through alternate host systems, in vivo and in vitro, as investigated by 2-dimensional, high-voltage electrophoresis of tryptic digests of this protein and amino acid analysis. N-terminal analyses were conducted using an improved technique which showed proline to be the N-terminal amino acid. Passage of enveloped nucleocapsids through alternate hosts as studied by SDS-PAGE [sodium dodecyl sulfate-polyacrylamide gel electrophoresis] showed the polypeptide compositions to be very similar. [Larvae of A. californica and Trichoplusia ni and cell lines from T. ni (TN-368-10) and Spodoptera frugiperda (IPLB-22) were used.].