The vaccinia virus K2L gene encodes a serine protease inhibitor which inhibits cell-cell fusion

Zhou, J., Sun, X. Y., Fernando, G. J. P. and Frazer, I. H. (1992) The vaccinia virus K2L gene encodes a serine protease inhibitor which inhibits cell-cell fusion. Virology, 189 2: 678-686. doi:10.1016/0042-6822(92)90591-C


Author Zhou, J.
Sun, X. Y.
Fernando, G. J. P.
Frazer, I. H.
Title The vaccinia virus K2L gene encodes a serine protease inhibitor which inhibits cell-cell fusion
Journal name Virology   Check publisher's open access policy
ISSN 0042-6822
1096-0341
Publication date 1992-08-01
Sub-type Article (original research)
DOI 10.1016/0042-6822(92)90591-C
Volume 189
Issue 2
Start page 678
End page 686
Total pages 9
Place of publication Maryland Heights, MO United States
Publisher Academic Press
Language eng
Formatted abstract
In certain circumstances, cells infected with vaccinia virus (VV) undergo fusion, but this does not occur in tissue cultures infected with wild-type VV. The VV genome includes three genes (B24R, B13R, and K2L) encoding polypeptides that are structurally related to members of the plasma serine protease inhibitor (SPI) superfamily. In this study, we demonstrate by deleting these genes singly or in combination that the K2L gene encoding SPI- 3, but not the B24R or B13R genes encoding SPI-1 and SPI-2, inhibits cell- cell fusion in VV-infected cells. A VV-encoded hemagglutinin (HA) has previously been demonstrated to inhibit cell-cell fusion, but fusion- promoting VVs with K2L gene deletions had normal expression and cellular location of the VV HA. As both HA and SPI-3 independently inhibit cell-cell fusion in VV-infected cells, there must be at least two fusion-promoting mechanisms encoded by VV. These may play different roles in virus-cell fusion and in cell-cell fusion after VV infection.
Keyword Envelope Protein
Gel electrophoresis
Expression Vectors
Membrane Fusion
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Medicine Publications
 
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