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J Gen Virol 68 (1987), 2093-2104; DOI 10.1099/0022-1317-68-8-2093
© 1987 Society for General Microbiology

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Generation and Properties of the Glycoprotein E-related 32K/34K/35K and 55K/57K Polypeptides Encoded by Herpes Simplex Virus Type 1

A. M. Cross, R. G. Hope and H. S. Marsden

Medical Research Council, Institute of Virology, Church Street, Glasgow G11 5JR, U.K.

A hybridoma line was isolated which produced antibody reacting with polypeptides of apparent molecular weights 32000, 34000 and 35000 (32K/34K/35K) and 55000 and 57000 (55K/57K). These were sulphated glycoproteins that have previously been found in the medium of herpes simplex virus type 1 (HSV-1)-infected cells. By tryptic peptide mapping and serological cross-reactions the polypeptides were shown to be related to HSV-1 glycoprotein E (gE-1) but they lacked the Fc binding function. The 32K/34K/35K and 55K/57K polypeptides were not found in the medium of HSV-1-infected cells incubated in serum-free medium. They could be generated in vitro from purified gE-1 in the presence of serum. It is likely that 32K/34K/35K and 55K/57K are derived from gE-1 by the action of serum proteases.

Keywords: HSV-1, glycoprotein E, Fc binding

Received 20 January 1987; accepted 27 April 1987.


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K. Polcicova, K. Goldsmith, B. L. Rainish, T. W. Wisner, and D. C. Johnson
The Extracellular Domain of Herpes Simplex Virus gE Is Indispensable for Efficient Cell-to-Cell Spread: Evidence for gE/gI Receptors
J. Virol., September 15, 2005; 79(18): 11990 - 12001.
[Abstract] [Full Text] [PDF]




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