Phosphoglycosylation of a secreted acid phosphatase from Leishmania donovani
Phosphoglycosylation of a secreted acid phosphatase from Leishmania donovani
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DOI：
10.1093/glycob/9.6.627
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发表时间：
1999-06-01
期刊：
影响因子：
4.3
通讯作者：
Olafson, RW
中科院分区：
文献类型：
--
作者：
Lippert, DN;Dwyer, DW;Olafson, RW
L.donovani 的分泌酸性磷酸酶 (SAcP) 是一种异质糖蛋白，显示出广泛的 N- 和 O- 连接糖基化。 O- 连接糖因其与主要脂磷酸聚糖表面抗原和释放的磷酸聚糖的磷酸聚糖结构相似而受到特别关注（Turco 等人，1987 年；Greis 等人，1992 年），本研究描述了使用质谱、氨基酸测序和酶促碳水化合物测序进行 SAcP O 连接糖基化。对聚糖链长度和肽糖基化位点分布进行分析，发现平均 O 连接结构的长度与 32 个重复单元相似。糖基化肽的氨基酸序列分析表明，磷酸糖基化不是随机发生的，而是定位于位于 C 末端的一系列简并富含丝氨酸/苏氨酸的重复序列中的特定丝氨酸残基。没有获得苏氨酸残基修饰的证据。观察到的模式表明可能存在用于磷酸聚糖结构定位的共有序列。
The secreted acid phosphatase (SAcP) of L.donovani is a heterogeneous glycoprotein that displays a wide array of N- and O-linked glycosylations, The O-linked sugars are of particular interest due to their similarity to the phosphoglycan structures of the major lipophosphoglycan surface antigen and released phosphoglycan (Turco et at, 1987; Greis et al,, 1992), This study describes a structural analysis of the SAcP O-linked glycosylations using mass spectroscopy, amino acid sequencing, and enzymatic carbohydrate sequencing. Analysis of glycan chain lengths and peptide glycosylation site distribution was performed, revealing that the average O-linked structure was similar to 32 repeat units in length. Amino acid sequence analysis of glycosylated peptides showed that phosphoglycosylations did not occur randomly but were localized to specific serine residues within an array of degenerate serine/threonine-rich repeat sequences localized in the C-terminus. No evidence was obtained for modification of threonine residues. The observed pattern suggested that a consensus sequence may exist for localization of phosphoglycan structures.