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Journal of Virology, October 1999, p. 8750-8761, Vol. 73, No. 10
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Vaccinia Virus Envelope D8L Protein Binds to Cell
Surface Chondroitin Sulfate and Mediates the Adsorption of
Intracellular Mature Virions to Cells
Jye-Chian
Hsiao,
Che-Sheng
Chung, and
Wen
Chang*
Institute of Molecular Biology, Academia
Sinica, Nankang, Taipei, Taiwan, Republic of China
Received 27 May 1999/Accepted 12 July 1999
We previously showed that an envelope A27L protein of intracellular
mature virions (IMV) of vaccinia virus binds to cell surface heparan
sulfate during virus infection. In the present study we identified
another viral envelope protein, D8L, that binds to chondroitin sulfate
on cells. Soluble D8L protein interferes with the adsorption of
wild-type vaccinia virions to cells, indicating a role in virus entry.
To explore the interaction of cell surface glycosaminoglycans and
vaccinia virus, we generated mutant viruses from a control virus,
WR32-7/Ind14K (A27L+ D8L+) to be defective
in expression of either the A27L or the D8L gene (A27L+
D8L
or A27L
D8L+) or both
(A27L
D8L
). The A27L+
D8L+ and A27L
D8L+ mutants grew
well in BSC40 cells, consistent with previous observations. However,
the IMV titers of A27L+ D8L
and
A27L
D8L
viruses in BSC40 cells were
reduced, reaching only 10% of the level for the control virus. The
data suggested an important role for D8L protein in WR32-7/Ind14K virus
growth in cell cultures. A27L protein, on the other hand, could not
complement the functions of D8L protein. The low titers of the
A27L+ D8L
and A27L
D8L
mutant viruses were not due to defects in the
morphogenesis of IMV, and the mutant virions demonstrated a brick shape
similar to that of the control virions. Furthermore, the infectivities of the A27L+ D8L
and A27L
D8L
mutant virions were 6 to 10% of that of the
A27L+ D8L+ control virus. Virion binding assays
revealed that A27L+ D8L
and
A27L
D8L
mutant virions bound less well to
BSC40 cells, indicating that binding of viral D8L protein to cell
surface chondroitin sulfate could be important for vaccinia virus entry.
*
Corresponding author. Mailing address: Institute of
Molecular Biology, Academia Sinica, #128 Sec. 2, Yen Chiu Yuan Rd.,
Nankang, Taipei 11529, Taiwan, Republic of China. Phone:
886-2-2789-9230. Fax: 886-2-2782-6085. E-mail:
mbwen{at}ccvax.sinica.edu.tw.
Journal of Virology, October 1999, p. 8750-8761, Vol. 73, No. 10
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
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