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Stiles B, Wood HA. A study of the glycoproteins of Autographa californica nuclear polyhedrosis virus (AcNPV). Virology. 1983;131(1):230-41doi: 10.1016/0042-6822(83)90548-2.
Stiles, B., & Wood, H. A. (1983). A study of the glycoproteins of Autographa californica nuclear polyhedrosis virus (AcNPV). Virology, 131(1), 230-41. https://doi.org/10.1016/0042-6822(83)90548-2
Stiles, B, and Wood, H A. "A study of the glycoproteins of Autographa californica nuclear polyhedrosis virus (AcNPV)." Virology vol. 131,1 (1983): 230-41. doi: https://doi.org/10.1016/0042-6822(83)90548-2
Stiles B, Wood HA. A study of the glycoproteins of Autographa californica nuclear polyhedrosis virus (AcNPV). Virology. 1983 Nov;131(1):230-41. doi: 10.1016/0042-6822(83)90548-2. PMID: 18639173; PMCID: PMC7131021.
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Virology. 1983 Nov;131(1):230-41. doi: 10.1016/0042-6822(83)90548-2.

A study of the glycoproteins of Autographa californica nuclear polyhedrosis virus (AcNPV).

Virology

B Stiles, H A Wood

Affiliations

  1. Boyce Thompson Institute at Cornell University, Tower Road, Ithaca, New York 14853, USA.

PMID: 18639173 PMCID: PMC7131021 DOI: 10.1016/0042-6822(83)90548-2

Abstract

Pulse labeling with tritiated mannose was used to follow the time course of Autographa californica nuclear polyhedrosis virus (AcNPV) glycoprotein synthesis in Spodoptera frugiperda IPLB-21 cells. Nine viral-induced intracellular glycoproteins were first detected from as early as 2 hr postinoculation (67K, early phase) to as late as 14 hr (36K and 19K glycoproteins, intermediate phase). Glycosylation of these proteins was observed to continue to the end of the experiment (28 hr postinoculation). Seven of these intracellular glycoproteins could also be detected in infected Trichoplusia ni TN-368 cells 24 hr postinoculation. When the glycosylation inhibitor tunicamycin was present (from 0 hr postinoculation) there was no detectable glycosylation of any of these viral-induced glycoproteins. Metabolic labeling of the nonoccluded virus budded from IPLB-21 and TN-368 with tritiated mannose or N-acetylglucosamine identified 11 structural glycoproteins, 8 of which were identical in both virus preparations. All of these structural glycoproteins were sensitive to the inhibitory action of tunicamycin. A single 42K structural glycoprotein was detected (with acetylglucosamine only) in the occluded form of AcNPV. Glycosylation of this structural protein appeared to be insensitive to tunicamycin. Lactoperoxidase-catalyzed radioiodination was used to determine which of the virus structural glycoproteins are exposed on the virion surface.

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