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J Gen Virol 73 (1992), 627-632; DOI 10.1099/0022-1317-73-3-627
© 1992 Society for General Microbiology
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Shedding of a rhinovirus minor group binding protein: evidence for a Ca2+-dependent process

Franz Hofer1, Berthold Berger1, Martin Gruenberger1, Herwig Machat1, Rudolf Dernick2, Uwe Tessmer2, Ernst Kuechler1 and Dieter Blaas1

1 Institute of Biochemistry, University of Vienna, Waehringerstrasse 17, A-1090 Vienna, Austria
and2 Heinrich Pette Institute of Experimental Virology and Immunology at the University of Hamburg, Martinistrasse 52, D-2000 Hamburg 20, Germany

Soluble rhinovirus minor group binding activity was found to be shed into the medium upon incubation of HeLa cells at 37°C. Although substantial amounts of this protein were released, no decrease of virus binding to the cell surface was seen. When the membrane-associated receptor was stripped from the cells with trypsin, virus binding was rapidly restored from an intracellular pool even in the absence of de novo protein synthesis. The release of this 85K virus-binding activity was inhibited by metal chelators such as EDTA, EGTA or 1,10-phenanthroline. The potential involvement of a Ca2+-dependent protease and/or a phospholipase in this process is discussed.

Received 9 September 1991; accepted 14 November 1991.


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