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J Gen Virol 72 (1991), 3085-3089; DOI 10.1099/0022-1317-72-12-3085
© 1991 Society for General Microbiology

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A Transformation-specific Polypeptide Distinct from Heat Shock Proteins is Induced by Herpes Simplex Virus Type 2 Infection

R. E. P. Hewitt, M. Grassie, D. McNab, A. Orr, J.-F. Lucasson and J. C. M. Macnab

MRC Virology Unit, Institute of Virology, Church Street, Glasgow G11 5JR, U.K.

A tumour-specific polypeptide designated U90 is one of a set of polypeptides which are encoded by the host cell and are specific for the transformed cell state, being immunoprecipitated by the sera of tumour-bearing animals. The interest in these tumour-specific polypeptides centres on the finding that they are also recognized by antisera raised against herpes simplex virus type 2 (HSV-2)-infected cells, implying some role for HSV-2 in tumorigenesis. The peptide map of HSV-2-induced U90 is indistinguishable from that of U90 present in uninfected tumour cells, including mouse cells transformed by human papillomavirus type 16. In tumour cells, U90 is located principally in the plasma membrane fraction and cannot be induced by heat shock, glucose starvation, or treatment with tunicamycin or calcium ionophore. U90 is not related to either the heat shock protein of Mr 90000 (HSP90) or the glucose-related polypeptide of Mr 94000 (GRP94) as determined by peptide mapping and the use of monospecific, monoclonal and antipeptide antibodies. This suggests that U90 is a novel transformation-specific protein which can be induced by infection with HSV-2.

Received 11 March 1991; accepted 19 August 1991.


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M Grassie, D McNab, and J. Macnab
The characteristic which makes the cell-coded HSV-inducible U90 distinctive in transformed cells is its greatly increased half-life
J. Cell Sci., January 4, 1993; 104(4): 1083 - 1090.
[Abstract] [PDF]




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Copyright © 1991 by the Society for General Microbiology.