Albert M. Wu , Tanuja Singh , Yung Liang Chen , Kimberly M. Anderson , Su Chen Li , Yu Teh Li
{"title":"肺炎链球菌SP2159基因编码的岩藻胶蛋白相关蛋白(FRP)的聚糖结合谱","authors":"Albert M. Wu , Tanuja Singh , Yung Liang Chen , Kimberly M. Anderson , Su Chen Li , Yu Teh Li","doi":"10.1016/j.biopen.2017.12.002","DOIUrl":null,"url":null,"abstract":"<div><p>The recombinant fucolectin-related protein (FRP) of unknown function, encoded by the SP2159 gene of <em>Streptococcus pneumoniae,</em> was expressed in <em>E. coli</em>. In this study, its glycan-recognition epitopes and their binding potencies were examined by enzyme-linked lectinosorbent and inhibition assays. The results indicate that FRP reacted strongly with human blood group <strong>ABH</strong> and <span>l</span>-Fucα1→2-active glycotopes and in their polyvalent (super) forms. When expressed by mass relative potency, the binding affinities of FRP to poly-<span>l</span>-Fucα1→glycotopes were about 5.0 × 10<sup>5</sup> folds higher than that of the mono-<span>l</span>-Fucα1→glycotope form. This unique binding property of FRP can be used as a special tool to differentiate complex forms of <span>l</span>-Fucα1→2 and other forms of glycotopes.</p></div>","PeriodicalId":92004,"journal":{"name":"Biochimie open","volume":"6 ","pages":"Pages 17-23"},"PeriodicalIF":0.0000,"publicationDate":"2018-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.biopen.2017.12.002","citationCount":"2","resultStr":"{\"title\":\"Glycan binding profile of a fucolectin-related protein (FRP) encoded by the SP2159 gene of Streptococcus pneumoniae\",\"authors\":\"Albert M. Wu , Tanuja Singh , Yung Liang Chen , Kimberly M. Anderson , Su Chen Li , Yu Teh Li\",\"doi\":\"10.1016/j.biopen.2017.12.002\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>The recombinant fucolectin-related protein (FRP) of unknown function, encoded by the SP2159 gene of <em>Streptococcus pneumoniae,</em> was expressed in <em>E. coli</em>. In this study, its glycan-recognition epitopes and their binding potencies were examined by enzyme-linked lectinosorbent and inhibition assays. The results indicate that FRP reacted strongly with human blood group <strong>ABH</strong> and <span>l</span>-Fucα1→2-active glycotopes and in their polyvalent (super) forms. When expressed by mass relative potency, the binding affinities of FRP to poly-<span>l</span>-Fucα1→glycotopes were about 5.0 × 10<sup>5</sup> folds higher than that of the mono-<span>l</span>-Fucα1→glycotope form. This unique binding property of FRP can be used as a special tool to differentiate complex forms of <span>l</span>-Fucα1→2 and other forms of glycotopes.</p></div>\",\"PeriodicalId\":92004,\"journal\":{\"name\":\"Biochimie open\",\"volume\":\"6 \",\"pages\":\"Pages 17-23\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2018-06-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/j.biopen.2017.12.002\",\"citationCount\":\"2\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimie open\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S2214008517300184\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimie open","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S2214008517300184","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Glycan binding profile of a fucolectin-related protein (FRP) encoded by the SP2159 gene of Streptococcus pneumoniae
The recombinant fucolectin-related protein (FRP) of unknown function, encoded by the SP2159 gene of Streptococcus pneumoniae, was expressed in E. coli. In this study, its glycan-recognition epitopes and their binding potencies were examined by enzyme-linked lectinosorbent and inhibition assays. The results indicate that FRP reacted strongly with human blood group ABH and l-Fucα1→2-active glycotopes and in their polyvalent (super) forms. When expressed by mass relative potency, the binding affinities of FRP to poly-l-Fucα1→glycotopes were about 5.0 × 105 folds higher than that of the mono-l-Fucα1→glycotope form. This unique binding property of FRP can be used as a special tool to differentiate complex forms of l-Fucα1→2 and other forms of glycotopes.