Key result
Metal chelators inhibit 85K rhinovirus binding protein release from HeLa cells, suggesting a Ca2+-dependent process.
Why the study?
The mechanisms underlying the shedding of rhinovirus minor group binding proteins and the role of Ca2+-dependent processes were unclear.
The shedding of the rhinovirus minor group binding protein from HeLa cells appears to be a Ca2+-dependent process, potentially involving a Ca2+-dependent protease or phospholipase.
Answers are grounded in this paper and cite their sources.
Hypothesis-generating in cell culture; leaves open relevance to human rhinovirus infection or therapy.
Soluble rhinovirus minor group binding activity was found to be shed into the medium upon incubation of HeLa cells at 37 degrees 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 Ca(2+)-dependent protease and/or a phospholipase in this process is discussed.
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Hofer et al. (1992) studied Rhinovirus infection. Metal chelators (EDTA, EGTA, 1,10-phenanthroline) was evaluated on Release of 85K virus-binding activity. The release of an 85K rhinovirus minor group binding protein from HeLa cells was inhibited by metal chelators, suggesting a Ca2+-dependent process.
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