Pritzer E, Kuroda K, Garten W, Nagai Y, Klenk H D
Institut für Virologie, Philipps-Universität, Marburg, F.R.G.
Virus Res. 1990 Mar;15(3):237-42. doi: 10.1016/0168-1702(90)90031-6.
The primary structure of the F protein of a host range mutant of the Ulster strain of Newcastle Disease virus (NDV) has been determined by nucleotide sequence analysis and compared to that of the wild type and other NDV strains. The cleavage site of the mutant had the sequence Gly-Lys-Gln-Arg-Arg as compared to two isolated basic amino acids [Gly-Lys(Arg)-Gln-Gly-Arg] with the apathogenic strains and two pairs of basic amino acids [Arg-Arg-Gln-Lys(Arg)-Arg] with the pathogenic strains. The data indicate that the cleavability of the F protein of NDV increases with the number of arginine and lysine residues at the cleavage site and that the susceptibility of the pathogenic strains to ubiquitous host proteases depends on both pairs of basic amino acids.
通过核苷酸序列分析确定了新城疫病毒（NDV）阿尔斯特株宿主范围突变体F蛋白的一级结构，并与野生型及其他NDV毒株进行了比较。该突变体的裂解位点序列为甘氨酸-赖氨酸-谷氨酰胺-精氨酸-精氨酸，而无致病性毒株的裂解位点为两个孤立的碱性氨基酸[甘氨酸-赖氨酸（精氨酸）-谷氨酰胺-甘氨酸-精氨酸]，致病性毒株的裂解位点为两对碱性氨基酸[精氨酸-精氨酸-谷氨酰胺-赖氨酸（精氨酸）-精氨酸]。数据表明，NDV F蛋白的可裂解性随裂解位点精氨酸和赖氨酸残基数量的增加而增加，致病性毒株对普遍存在的宿主蛋白酶的敏感性取决于两对碱性氨基酸。
