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Expression and Analysis of EBV gp350 in the Yeast SaccharomycesCerevisiae

  • L. D. Schultz
  • J. Tanner
  • K. Hofmann
  • E. Emini
  • E. Kieff
  • R. W. Ellis
Part of the Experimental Biology and Medicine book series (EBAM, volume 15)

Abstract

Epstein-Barr Virus (EBV) causes infectious mononucleosis and has been implicated strongly, along with essential cofactors, as a causative agent for the development of nasopharyngeal carcinoma, Burkitt’s lymphoma, and B-cell malignancies in immune-deficient patients. The two major glycoprotein components of the virion are gp350 and gp220, which are encoded by the same gene (1). They are both capable of eliciting neutralizing antibodies in vitro (2). In addition, recent data suggest that viral gp350 can be protective in a primate model (cottontop marmoset) of EBV infection (3). Thus, gp350 may be a useful immunogen for eliciting protective immunity against EBV infections. In this report, we describe the expression in yeast (Saccharomyces cerevisiae) of the secretable form of gp350, minus the membrane anchor sequence. The yeast-derived gp375 shows structural and immunological similarities to the viral gp350.

Keywords

Infectious Mononucleosis Viral Gp350 Gp350 Antibody Elicit Neutralize Antibody Immunological Similarity 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

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    C. Beisel, J. Tanner, T. Matsuo, D.A. Thorley-Lawson, F. Kezdy, E. Kieff, J. Virol. 54, 665 (1985).PubMedGoogle Scholar
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    D.A. Thorley-Lawson, K. Geilinger, Proc. Natl. Acad. Sci., U.S.A. 77, 5307 (1980).PubMedCrossRefGoogle Scholar
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    M.A. Epstein, A.J. Morgan, S. Finerty, B.G. Randle, J.K. Kirkwood, Nature 318, 287 (1985).PubMedCrossRefGoogle Scholar

Copyright information

© The Humana Press Inc. 1987

Authors and Affiliations

  • L. D. Schultz
    • 1
  • J. Tanner
    • 2
  • K. Hofmann
    • 1
  • E. Emini
    • 1
  • E. Kieff
    • 2
  • R. W. Ellis
    • 1
  1. 1.Merck Sharp & Dohme Res. Labs.West PointUSA
  2. 2.University of ChicagoChicagoUSA

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