LIPOOLIGOSACCHARIDES (LOS) OF NEISSERIA-GONORRHOEAE AND NEISSERIA-MENINGITIDIS HAVE COMPONENTS THAT ARE IMMUNOCHEMICALLY SIMILAR TO PRECURSORS OF HUMAN-BLOOD GROUP ANTIGENS - CARBOHYDRATE SEQUENCE SPECIFICITY OF THE MOUSE MONOCLONAL-ANTIBODIES THAT RECOGNIZE CROSSREACTING ANTIGENS ON LOS AND HUMAN-ERYTHROCYTES
LIPOOLIGOSACCHARIDES (LOS) OF NEISSERIA-GONORRHOEAE AND NEISSERIA-MENINGITIDIS HAVE COMPONENTS THAT ARE IMMUNOCHEMICALLY SIMILAR TO PRECURSORS OF HUMAN-BLOOD GROUP ANTIGENS - CARBOHYDRATE SEQUENCE SPECIFICITY OF THE MOUSE MONOCLONAL-ANTIBODIES THAT RECOGNIZE CROSSREACTING ANTIGENS ON LOS AND HUMAN-ERYTHROCYTES
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DOI：
10.1084/jem.168.1.107
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发表时间：
1988-07-01
影响因子：
15.3
通讯作者：
MACHER, BA
中科院分区：
文献类型：
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作者：
MANDRELL, RE;GRIFFISS, JM;MACHER, BA
我们已经使用针对淋球菌脂低聚糖(LOS)高度保守表位的鼠单抗3F11和06B4来鉴定人红细胞上免疫化学上相似的结构。单抗3F11能凝集所有随机选择的成人红细胞，而单抗06B4只凝集相同标本的80%。这些抗体与红细胞的凝集活性类似于人的冷凝集素，其凝集反应发生在4度。C，并随孵化温度的升高而降低。人类婴儿红细胞的凝集性较差，但婴儿或成人细胞的酶处理导致3F11和06B4定义的表位表达增加。这两种抗体都与来自人红细胞和中性粒细胞的一系列中性鞘糖脂结合，这些中性粒细胞具有2型(Gal.beta1.fwdarw.4GlcNAc)或N-乙酰乳糖胺结构。这两种抗体都没有与来自人胎粪的糖鞘糖脂结合，人胎粪中的糖鞘糖脂具有1型(Gal.beta1.fwdarw.3GlcNAc)结构。抗体不能与N-乙酰乳糖胺糖脂结合，不能与非还原末端唾液酸或Gal.alpha.fwdarw结合。3半乳糖二糖。抗体结合也被与N-乙酰乳糖胺氨基鞘糖脂的倒数第二个氨基葡萄糖残基相连的岩藻糖所阻断。虽然这两种抗体都与线状和支链N-乙酰乳糖胺糖脂结合，但3F11对分支结构的亲和力比06B4更高。3F11与N-乙酰乳糖胺处理和未处理的成人和婴儿红细胞以及与LOS处理的红细胞的活性在特异性上与1b2非常相似，如果不相同的话。1b2是一种从小鼠身上接种线性N-乙酰乳糖胺糖脂制备的单抗。
We have used mouse mAbs, 3F11 and 06B4, that are specific for highly conserved epitopes of Neisseria gonorrhoeae lipooligosaccharides (LOS) to identify immunochemically similar structures on human erythrocytes. mAb 3F11 agglutinated erythrocytes from all randomly selected adult humans, while mAb 06B4 agglutinated only 80% of the same specimens. The antibodies had an activity with erythrocytes similar to human cold agglutinins in that the agglutination occurred at 4.degree. C and decreased with increasing incubation temperature. Human infant erythrocytes were agglutinated less well, but enzymatic treatment of either infant or adult cells resulted in an increase in expression of the 3F11- and 06B4-defined epitopes. Both antibodies bound to a series of neutral glycosphingolipids from human erythrocytes and neutrophils that have a type 2 (Gal.beta.1 .fwdarw. 4GlcNAc) or N-acetyllactosamine strucutre. Neither antibody bound to glycosphingolipids from human meconium, which have a type 1 (Gal.beta.1 .fwdarw. 3GlcNAc) structure. The antibodies were unable to bind to N-acetyl-lactosamine glycosphingolipids with a nonreducing terminal sialic acid or a Gal.alpha.1 .fwdarw. 3Gal disaccharide. Antibody binding also was blocked by the presence of fucose linked to the penultimate glucosamine residue of N-acetyllactosamine glycosphingolipids. Although both antibodies bound to linear and branched-chain N-acetyllactosamine glycosphingolipids, 3F11 had a higher affinity for branched structures than did 06B4. The activity of 3F11 with human adult and infant treated and untreated erythrocytes with N-acetyllactosamine glycosphingolipids, and with LOS was very similar, if not identical, in specificity to 1B2, an mAb prepared from mice inoculated with a linear N-acetyllactosamine glycosphingolipid.