PMID: 9557661Apr 29, 1998Paper

Effect of cleavage mutants on syncytium formation directed by the wild-type fusion protein of Newcastle disease virus

Journal of Virology
Z LiT G Morrison

Abstract

The effects of Newcastle disease virus (NDV) fusion (F) glycoprotein cleavage mutants on the cleavage and syncytium-forming activity of the wild-type F protein were examined. F protein cleavage mutants were made by altering amino acids in the furin recognition region (amino acids 112 to 116) in the F protein of a virulent strain of NDV. Four mutants were made: Q114P replaced the glutamine residue with proline; K115G replaced lysine with glycine; double mutant K115G, R113G replaced both a lysine and an arginine with glycine residues; and a triple mutant, R112G, K115G, F117L, replaced three amino acids to mimic the sequence found in avirulent strains of NDV. All mutants except Q114P were cleavage negative and fusion negative. However, addition of exogenous trypsin cleaved all mutant F proteins and activated fusion. As expected for an oligomeric protein, the fusion-negative mutants had a dominant negative phenotype: cotransfection of wild-type and mutant F protein cDNAs resulted in an inhibition of syncytium formation. The presence of the mutant F protein did not inhibit cleavage of the wild-type protein. Furthermore, evidence is presented that suggests that the mutant protein and the wild-type protein formed heterooligomers. By m...Continue Reading

References

Nov 6, 1992·Science·J M White
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Citations

Sep 15, 2006·Journal of Virology·Homer D PantuaTrudy G Morrison
Mar 8, 2012·Future Microbiology·Dmitriy Zamarin, Peter Palese
Nov 20, 2002·Journal of Virology·Lori W McGinnesTrudy G Morrison
Sep 29, 2005·Journal of Virology·Kelly Ann MeulendykeRebecca Ellis Dutch
Feb 26, 2010·Journal of Virology·Lori W McGinnesTrudy G Morrison
Jan 21, 2003·The Journal of General Virology·Sigrid ElshuberChristian W Mandl
Jul 23, 2003·Biochimica Et Biophysica Acta·Trudy G Morrison

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