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J Virol, July 1998, p. 5552-5558, Vol. 72, No. 7
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Epstein-Barr Virus Uses Different Complexes of
Glycoproteins gH and gL To Infect B Lymphocytes and Epithelial
Cells
Xi
Wang,1
William
J.
Kenyon,1
Qingxue
Li,1,
Jürgen
Müllberg,2,
and
Lindsey M.
Hutt-Fletcher1,*
School of Biological Sciences, University of
Missouri
Kansas City, Kansas City,
Missouri,1 and
Department of Molecular
Biology, Immunex Research and Development Corporation, Seattle,
Washington2
Received 30 January 1998/Accepted 9 April 1998
The Epstein-Barr virus (EBV) gH-gL complex includes a third
glycoprotein, gp42. gp42 binds to HLA class II on the surfaces of B
lymphocytes, and this interaction is essential for infection of the B
cell. We report here that, in contrast, gp42 is dispensable for
infection of epithelial cell line SVKCR2. A soluble form of gp42,
gp42.Fc, can, however, inhibit infection of both cell types. Soluble
gp42 can interact with EBV gH and gL and can rescue the ability of
virus lacking gp42 to transform B cells, suggesting that a
gH-gL-gp42.Fc complex can be formed by extrinsic addition of the
soluble protein. Truncated forms of gp42.Fc that retain the ability to
bind HLA class II but that cannot interact with gH and gL still inhibit
B-cell infection by wild-type virus but cannot inhibit infection of
SVKCR2 cells or rescue the ability of recombinant gp42-negative virus
to transform B cells. An analysis of wild-type virions indicates the
presence of more gH and gL than gp42. To explain these results, we
describe a model in which wild-type EBV virions are proposed to contain
two types of gH-gL complexes, one that includes gp42 and one that does
not. We further propose that these two forms of the complex have
mutually exclusive abilities to mediate the infection of B cells and
epithelial cells. Conversion of one to the other concurrently alters
the ability of virus to infect each cell type. The model also suggests
that epithelial cells may express a molecule that serves the same
cofactor function for this cell type as HLA class II does for B cells
and that the gH-gL complex interacts directly with this putative
epithelial cofactor.
*
Corresponding author. Mailing address: School of
Biological Sciences, University of Missouri
Kansas City, 5007 Rockhill
Rd., Kansas City, MO 64110. Phone: (816) 235-2575. Fax: (816) 235-5595. E-mail: huttfletcher{at}cctr.umkc.edu.

Present address: Department of Microbiology and Immunology,
University of Michigan Medical School, Ann Arbor, MI 48109.

Present address: Department of Medicine, Section of Pathobiology,
Obere Zahlbacker, 55101 Mainz, Germany.
J Virol, July 1998, p. 5552-5558, Vol. 72, No. 7
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
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