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ID 21539
本文ファイル
著者
Sato, Yuichiro
Okuyama, Satomi
NDC
植物学
抄録(英)
The primary structure of a lectin,designated OAA, isolated from thefreshwater cyanobacterium, Oscillatoriaagardhii NIES-204, was determined by thecombination of Edman degradation andESI-mass spectrometry. OAA is apolypeptide (MW 13,925) consisting of twotandem repeats. Interestingly, each repeatsequence of OAA showed a high degree ofsimilarity to those of a myxobacterium,Myxococcus xanthus hemagglutinin(MBHA), and a marine red alga Eucheumaserra lectin (ESA-2). A systematic bindingassay with pyridylaminated oligosaccharidesrevealed that OAA exclusively binds to highmannose (HM) type N-glycans, but not toother N-glycans, including complex types,hybrid types and the pentasaccharide core,or oligosaccharides from glycolipids. OAAdid not interact with any of free mono-andoligomannoses that are constituents of thebranched oligomannosides. These resultssuggest that the core disaccharide, GlcNAc-GlcNAc, is also essential for binding to OAA.The binding activity of OAA to HMtype N-glycanswas dramatically decreased whenα1-2 Man was attached to α1-3 Manbranched from the α1-6 Man of thepentasaccharide core. This specificity ofOAA for HM type oligosaccharides isdistinct from other HM-binding lectins.Kinetic analysis with an HMheptasaccharide revealed that OAApossesses two carbohydrate-binding sitesper molecule, with an association constant of2.41×10^8M^-1. Furthermore, OAA potentlyinhibits HIV replication in MT-4 cells(EC50=44.5 nM). Thus, we have found anovel lectin family sharing similar structureand carbohydrate binding specificity amongbacteria, cyanobacteria, and marine algae.
掲載誌名
Journal of Biological Chemistry
282巻
15号
開始ページ
11021
終了ページ
11029
出版年月日
2007-04-13
出版者
The American Society for Biochemistry and Molecular Biology
ISSN
0021-9258
NCID
出版者DOI
言語
英語
NII資源タイプ
学術雑誌論文
広大資料タイプ
学術雑誌論文
DCMIタイプ
text
フォーマット
application/pdf
著者版フラグ
author
権利情報
Copyright (c) 2007 by the American Society for Biochemistry and Molecular Biology.
関連情報URL
部局名
生物圏科学研究科