Flinn H M, Rangarajan D, Smith D F
Department of Biochemistry, Imperial College of Science, Technology and Medicine, London, UK.
Mol Biochem Parasitol. 1994 Jun;65(2):259-70. doi: 10.1016/0166-6851(94)90077-9.
A family of differentially expressed genes from Leishmania major contains one sequence (Gene B) that encodes a novel, hydrophilic protein found on the surface of infective parasite stages. The 177-residue, acidic Gene B protein is characterised by an amino acid repetitive element, comprising 45% of the total molecule, that is related to the cell-wall binding domain of protein A from Staphylococcus aureus. No identifiable signal peptide, membrane-spanning domain or consensus for glycosylphosphatidylinositol anchor attachment to the cell surface is found elsewhere in the deduced protein sequence. In vitro, the Gene B protein fractionates with the parasite cell surface glycoconjugates, lipophosphoglycan and the glycoinositolphospholipids. This protein is the first characterised surface peptide marker for infective stages of the Leishmania life cycle.
来自硕大利什曼原虫的一个差异表达基因家族包含一个序列（基因B），该序列编码一种在感染性寄生虫阶段表面发现的新型亲水性蛋白质。这种由177个氨基酸残基组成的酸性基因B蛋白的特征是具有一个氨基酸重复元件，该元件占整个分子的45%，与金黄色葡萄球菌蛋白A的细胞壁结合结构域相关。在推导的蛋白质序列中其他位置未发现可识别的信号肽、跨膜结构域或糖基磷脂酰肌醇锚定连接到细胞表面的共有序列。在体外，基因B蛋白与寄生虫细胞表面糖缀合物、脂磷壁酸和糖基肌醇磷脂一起分级分离。这种蛋白质是利什曼原虫生命周期感染阶段首个被鉴定的表面肽标记物。
