N-glycans harboring the Lewis a epitope are expressed at the surface of plant cells

被引:161
作者
Fitchette-Lainé, AC
Gomord, V
Cabanes, M
Michalski, JC
Saint Macary, M
Foucher, B
Cavelier, B
Hawes, C
Lerouge, P
Faye, L
机构
[1] Univ Rouen, Fac Sci, IFRMP 23, ESA CNRS 6037, F-76821 Mt St Aignan, France
[2] Univ Sci & Tech Lille Flandres Artois, UMR CNRS 111, Lab Chim Biol C9, F-59655 Villeneuve Dascq, France
[3] Etab Transfus Sanguine & Genet Humaine Haute Norm, F-76232 Bois Guillaume, France
[4] Oxford Brookes Univ, Res Sch Biol & Mol Sci, Oxford OX3 0BP, England
关键词
D O I
10.1046/j.1365-313x.1997.12061411.x
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
In plants, N-linked glycans are processed in the Golgi apparatus to complex-type N-glycans of limited size containing a beta(1,2)-xylose and/or an alpha(1,3)-fucose residue. Larger mono-and bi-antennary N-linked complex glycans have not often been described. This study has re-examined the structure of such plant N-linked glycans, and, through both immunological and structural data, it is shown that the antennae are composed of Lewis a (Le(a)) antigens, comprising the carbohydrate sequence Gal beta 1-3[Fuc alpha 1-4]GlcNAc. Furthermore, a fucosyltransferase activity involved in the biosynthesis of this antigen was detected in sycamore cells. This is the first characterization in plants of a Lewis antigen that is usually found on cell-surface glycoconjugates in mammals and involved in recognition and adhesion processes. Le(a)-containing N-linked glycans are widely distributed in plants and highly expressed at the cell surface, which may suggest a putative function in cell/cell communication.
引用
收藏
页码:1411 / 1417
页数:7
相关论文
共 17 条
  • [1] [Anonymous], 1988, Antibodies: A Laboratory Manual
  • [2] BROCKAUSEN I, 1997, GLYCOSCIENCES STATUS
  • [3] A SIMPLE AND RAPID METHOD FOR THE PERMETHYLATION OF CARBOHYDRATES
    CIUCANU, I
    KEREK, F
    [J]. CARBOHYDRATE RESEARCH, 1984, 131 (02) : 209 - 217
  • [4] A PLANT FUCOSYL-TRANSFERASE WITH HUMAN LEWIS BLOOD-GROUP SPECIFICITY
    CRAWLEY, SC
    HINDSGAUL, O
    RATCLIFFE, RM
    LAMONTAGNE, LR
    PALCIC, MM
    [J]. CARBOHYDRATE RESEARCH, 1989, 193 : 249 - 256
  • [5] EMERY N, 1995, GLYCOBIOLOGY, V5, P563
  • [6] AFFINITY PURIFICATION OF ANTIBODIES SPECIFIC FOR ASN-LINKED GLYCANS CONTAINING ALPHA-1-]3 FUCOSE OR BETA-1-]2 XYLOSE
    FAYE, L
    GOMORD, V
    FITCHETTELAINE, AC
    CHRISPEELS, MJ
    [J]. ANALYTICAL BIOCHEMISTRY, 1993, 209 (01) : 104 - 108
  • [7] UREASE IN JACK-BEAN (CANAVALIA-ENSIFORMIS (L) DC) SEEDS IS A CYTOSOLIC PROTEIN
    FAYE, L
    GREENWOOD, JS
    CHRISPEELS, MJ
    [J]. PLANTA, 1986, 168 (04) : 579 - 585
  • [8] Feizi Ten, 1993, Current Opinion in Structural Biology, V3, P701, DOI 10.1016/0959-440X(93)90053-N
  • [9] GAS-LIQUID-CHROMATOGRAPHY AND MASS-SPECTROMETRY OF METHYLATED AND ACETYLATED METHYL GLYCOSIDES - APPLICATION TO THE STRUCTURAL-ANALYSIS OF GLYCOPROTEIN GLYCANS
    FOURNET, B
    STRECKER, G
    LEROY, Y
    MONTREUIL, J
    [J]. ANALYTICAL BIOCHEMISTRY, 1981, 116 (02) : 489 - 502
  • [10] REEXAMINATION OF THE PYRIDYLAMINATION USED FOR FLUORESCENCE LABELING OF OLIGOSACCHARIDES AND ITS APPLICATION TO GLYCOPROTEINS
    HASE, S
    IBUKI, T
    IKENAKA, T
    [J]. JOURNAL OF BIOCHEMISTRY, 1984, 95 (01) : 197 - 203