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Expression of the SU glycoprotein of maedi visna virus in baculovirus

P Carter1, R G Dalziel

  • 1Department of Veterinary Pathology, University of Edinburgh, U.K.

Archives of Virology
|January 1, 1997
PubMed

Insights

Researchers developed a new way to study ovine lentivirus envelope glycoprotein (gp 135). This recombinant protein is glycosylated and recognized by sheep antibodies, aiding structure-function studies.

Area of Science:

  • Virology
  • Immunology
  • Molecular Biology

Background:

  • The ovine lentivirus maedi visna virus envelope glycoprotein (gp 135) is a key target for antibody responses.
  • Understanding the specific regions of gp 135 that trigger these responses is crucial but limited.
  • Existing research is hampered by a lack of suitable reagents for structure-function analysis.

Purpose of the Study:

  • To develop a recombinant form of the ovine lentivirus gp 135.
  • To create a tool for studying the structure and function of gp 135.
  • To facilitate the investigation of antibody responses against maedi visna virus.

Main Methods:

  • Utilized a baculovirus expression system for protein production.
  • Engineered gp 135 to lack the viral signal sequence.
  • Characterized the recombinant protein for glycosylation and antibody recognition.

Main Results:

  • Successfully produced a recombinant gp 135 protein lacking the viral signal sequence.
  • The recombinant gp 135 was found to be glycosylated.
  • Immune sera from clinically affected animals recognized the recombinant gp 135.

Conclusions:

  • The recombinant gp 135 is a valuable tool for studying ovine lentivirus.
  • This reagent will aid in understanding the structure-function relationships of gp 135.
  • Further research can now investigate specific antigenic regions of gp 135.

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