Schäffer C, Graninger M, Messner P
Zentrum für Ultrastrukturforschung, Ludwig Boltzmann-Institut für Molekulare Nanotechnologie, Universität für Bodenkultur Wien, Vienna, Austria.
Proteomics. 2001 Feb;1(2):248-61. doi: 10.1002/1615-9861(200102)1:2<248::AID-PROT248>3.0.CO;2-K.
With the advances of molecular biology and with improved analytical techniques a significant change of perception has taken place regarding prokaryotic glycoproteins. Glycosylation of proteins from prokaryotes is no longer considered a specific feature of certain organisms but has been demonstrated for many archaea and bacteria. Besides the occurrence of glycosylated enzymes, antigens and other cell envelope components, surface layer (S-layer) glycoproteins represent the best-studied examples of glycosylated prokaryotic proteins. They are widely distributed among archaeal wild-type strains, but among bacteria they have been mainly observed with Gram-positive organisms. There is, in general, an enormous increase of reports on the presence of glycosylated proteins among prokaryotes. For their isolation and characterization a great number of methods are available, aiming at the identification of the covalent linkage between the carbohydrate and the polypeptide portion. So far, several differences in structure and biosynthesis have been observed in comparison to eukaryotic glycoproteins. In this review we introduce a protocol which has been successfully applied to the investigation of the complex structures, linkage units, and polypeptide consensus sequences of glycosylated bacterial S-layer proteins.
随着分子生物学的进展以及分析技术的改进，人们对原核生物糖蛋白的认识发生了重大变化。原核生物蛋白质的糖基化不再被认为是某些生物体的特定特征，而是在许多古菌和细菌中都有发现。除了糖基化酶、抗原和其他细胞包膜成分的存在外，表层（S 层）糖蛋白是研究得最好的糖基化原核生物蛋白质实例。它们广泛分布于古菌野生型菌株中，但在细菌中，主要在革兰氏阳性菌中观察到。总体而言，关于原核生物中糖基化蛋白质存在的报道大量增加。对于它们的分离和表征，有大量方法可用，目的是鉴定碳水化合物与多肽部分之间的共价连接。到目前为止，与真核生物糖蛋白相比，在结构和生物合成方面已经观察到一些差异。在这篇综述中，我们介绍了一种已成功应用于研究糖基化细菌 S 层蛋白的复杂结构、连接单元和多肽共有序列的方案。
