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Isolation of Viral Replication Compartment-enriched Sub-nuclear Fractions from Adenovirus-infected Normal Human Cells
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Early events of polyoma infection: adsorption, penetration and nuclear transport

R A Consigli1, J I Haynes, D Chang

  • 1Division of Biology, Kansas State University, Manhattan 66506, USA.

Transactions of the Kansas Academy of Science. Kansas Academy of Science
|April 1, 1992
PubMed

Insights

Polyoma virions use specific attachment proteins for cell binding and infection. Different forms of the major capsid protein (VP1) are crucial for attachment and hemagglutination, with specific VP1 species mediating cell receptor interactions.

Area of Science:

  • Virology
  • Cell Biology
  • Protein Chemistry

Background:

  • Polyoma virions utilize distinct attachment proteins for hemagglutination and binding to cultured mouse kidney cells (MKC).
  • MKC exhibit both specific (productive infection) and nonspecific (nonproductive) receptors for virion binding.
  • Empty capsids exhibit hemagglutination and bind to nonspecific receptors but do not mediate productive infection.

Purpose of the Study:

  • To investigate the role of polyoma virion attachment proteins in cell binding and infection.
  • To characterize the specific VP1 protein species involved in virion attachment and hemagglutination.
  • To identify and characterize the MKC cell receptor(s) for polyoma virions.

Main Methods:

  • Isoelectric focusing of the major capsid protein (VP1) to separate modified species.
  • Precipitation assays with specific antisera to determine VP1 species function.
  • Crosslinking studies to covalently link virion attachment proteins to cell receptors, followed by SDS-PAGE analysis.
  • Use of anti-idiotype antibodies to identify receptor proteins in MKC extracts and membrane preparations.

Main Results:

  • VP1 separated into six species (A-F) differing in post-translational modifications.
  • VP1 species E is implicated in specific adsorption, while species D and F are involved in hemagglutination.
  • The virion attachment domain is localized to an 18 kDa C-terminal fragment of VP1.
  • A 120 kDa band was identified after crosslinking MKC receptors to VP1.
  • A putative 50 kDa receptor protein was identified using an anti-idiotype antibody.

Conclusions:

  • Specific modifications of VP1 are critical for distinct functions like cell attachment and hemagglutination.
  • The C-terminal region of VP1 contains the primary attachment domain.
  • A 50 kDa protein on MKC is identified as a potential receptor for polyoma virions.
Keywords:
NASA Discipline Cell BiologyNASA Discipline Developmental BiologyNASA Discipline Number 93-10NASA Program NSCORTNon-NASA Center

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