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Structural and Intracellular Proteins of the Nonoccluded Baculovirus HZ-1

J P Burand1, B Stiles, H A Wood

  • 1Boyce Thompson Institute for Plant Research, Ithaca, New York 14853.

Journal of Virology
|April 1, 1983
PubMed

Insights

This study details the replication kinetics of the HZ-1 baculovirus in TN-368 cells, identifying 28 structural proteins, including 14 glycoproteins. It also maps the appearance of 37 viral polypeptides and detects post-transcriptional modifications.

Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • The HZ-1 baculovirus is a persistent, nonoccluded virus.
  • Understanding viral replication kinetics is crucial for controlling viral infections and developing antiviral strategies.

Purpose of the Study:

  • To investigate the replication kinetics of the HZ-1 baculovirus in TN-368 cells.
  • To identify and characterize viral structural proteins and their modifications.

Main Methods:

  • Plaque purification of HZ-1 baculovirus.
  • Replication kinetics study in TN-368 cells.
  • Pulse-labeling with [(35)S]methionine to identify viral polypeptides.
  • Use of radiolabeled sugars (N-[(3)H]acetylglucosamine, [(3)H]mannose) and tunicamycin to detect glycosylated proteins.

Main Results:

  • Identified 28 HZ-1 baculovirus structural proteins with molecular weights ranging from 153,000 to 14,000.
  • Determined that 14 of the identified structural proteins are glycosylated.
  • Mapped the sequence of appearance of 37 virus-induced intracellular polypeptides.
  • Detected post-transcriptional modification of two virus-induced proteins.

Conclusions:

  • The study provides a comprehensive analysis of HZ-1 baculovirus replication and protein synthesis.
  • Characterization of viral glycoproteins and post-transcriptional modifications offers insights into viral assembly and pathogenesis.
  • Findings contribute to the understanding of persistent baculovirus infections.

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