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Sequence of the mouse adenovirus serotype-1 DNA encoding the precursor to capsid protein VI

B Song1, K R Spindler, C S Young

  • 1Department of Microbiology, Columbia University, New York, NY 10032.

Gene
|January 23, 1995
PubMed

Insights

Researchers determined the mouse adenovirus (MAV-1) protein VI precursor (preVI) sequence, finding significant similarity to human adenovirus preVI. This conservation suggests a shared functional role in viral replication and endoproteinase activation.

Area of Science:

  • Virology
  • Molecular Biology
  • Structural Biology

Background:

  • Adenoviruses are non-enveloped viruses with icosahedral capsids, responsible for various infections in mammals.
  • Structural protein VI (pVI) plays a crucial role in the viral life cycle, including cell entry and DNA release.
  • Mouse adenovirus (MAV-1) is a significant pathogen in laboratory mice, necessitating research into its molecular mechanisms.

Purpose of the Study:

  • To determine the nucleotide sequence encoding the precursor to virion structural protein VI (preVI) of mouse adenovirus (Ad) serotype-1 (MAV-1).
  • To compare the MAV-1 preVI sequence with homologous sequences from other adenoviruses, particularly human Ad serotype-2.
  • To identify conserved regions and potential functional domains within the MAV-1 preVI sequence.

Main Methods:

  • Bioinformatic analysis of the MAV-1 genome to identify the gene encoding preVI.
  • Amino acid sequence prediction based on the determined nucleotide sequence.
  • Sequence alignment and comparison with the human Ad serotype-2 preVI sequence using established algorithms.

Main Results:

  • The nucleotide sequence encoding MAV-1 preVI was determined, predicting a 237-amino-acid precursor protein.
  • The MAV-1 preVI sequence exhibits 45% identity and 66% similarity to the human Ad serotype-2 preVI sequence.
  • Significant sequence conservation was observed at both the N terminus (including the endoproteinase cleavage site) and the C terminus (potentially involved in endoproteinase activation).

Conclusions:

  • The MAV-1 preVI sequence shares significant homology with human adenovirus preVI, indicating conserved structural and functional properties.
  • The conserved C-terminal residues may be critical for activating the adenovirus endoproteinase, a key enzyme in viral replication.
  • The conserved N-terminal region, including the cleavage site, suggests a conserved mechanism for processing and activating protein VI during viral assembly or infection.

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