A peptide-model for the heparin-binding property of pseudorabies virus glycoprotein III
β Scribed by Dirk Sawitzky; Andrea Voigt; Karl-Otto Habermehl
- Publisher
- Springer-Verlag
- Year
- 1993
- Tongue
- English
- Weight
- 505 KB
- Volume
- 182
- Category
- Article
- ISSN
- 0300-8584
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β¦ Synopsis
The pseudorabies virus glycoprotein III (PrV-glII) has been identified previously as the major viral component binding to a heparin-like receptor on the surface of target cells. The amino acid sequence of glII contains three regions corresponding to consensus sequences for heparin binding. A synthetic peptide corresponding to amino acids 134 to 141 of PrV-glII bound heparin in a dot blot assay. In contrast, a synthetic peptide derived from amino acids 290-299 of PrV-gIII did not bind heparin. We therefore conclude that the region containing amino acid 134-141 is involved in binding to the heparin-like cellular receptor.
π SIMILAR VOLUMES
The binding properties of trivalent metal ions to polyelectrolytes were investigated through the use of terbium [Tb(lII)] in fluorescence studies. Tbe fluorescence intensity and lifetimes of the Ianthanide ions are directly dependent upon the number of water molecules bound to their inner coordinati