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首页> 外文期刊>Plant and Soil >Lipopolysaccharide core components of Rhizobium etli reacting with a panel of monoclonal antibodies.
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Lipopolysaccharide core components of Rhizobium etli reacting with a panel of monoclonal antibodies.

机译：根瘤菌的脂多糖核心成分与一组单克隆抗体反应。

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Monoclonal antibodies that react with Rhizobium leguminosarum lipopolysaccharide core antigens (LPS-2) were used to investigate LPS-2 structure in Rhizobium etli. The panel of antibodies (JIM 32-JIM 35, JIM 37, JIM 38) specific for LPS-2 of R. leguminosarum strain 3841 and its core components displayed similar reactivities towards isolated LPS-2 from R. etli CE109 (a mutant of wild-type strain R. etli CE3 that displays LPS-2 as its main LPS form on the cell surface). This result suggests that the antibodies bind to similar epitopes on both strains and, hence, R. leguminosarum and R. etli have very similar LPS core and lipid A antigen structures. More detailed analysis of the antibody binding sites with isolated LPS-2 and lipid A from R. etli suggests that some of the antibodies (JIM 32, 33, 34, and MASM-I) bind some part of the core oligosaccharides, while others (JIM 35 and JIM 38) involve lipid A. These antibodies have already proven useful in the biochemical analysis of the LPS antigen forms.For example, the loss of reactivity of certain LPS forms with antibody JIM 37 has led to the discovery of a hitherto unnoticed form of the LPS antigen in a precipitate formed during the phenol/water extraction procedure. This new form reacts with the JIM37 antibody. Furthermore, the positive reaction of some of the antibodies with only sonicated wild-type R. etli cells suggests that either an effective way of masking the display of core antigens on whole bacterial cells is occurring or that core formsof the LPSs are never displayed on the surface of the bacterial cells. Either possibility, once confirmed, could be important for designating the Rhizobium cell surface and could also have some bearing on symbiotic nodule infection and development.
机译：与豆科根瘤菌脂多糖核心抗原（LPS-2）反应的单克隆抗体用于研究根瘤菌中的LPS-2结构。特异于豆科念珠菌菌株3841的LPS-2的抗体组（JIM 32-JIM 35，JIM 37，JIM 38）及其核心成分对从埃特里氏菌CE109（野生突变体）分离的LPS-2表现出相似的反应性型菌株R. etli CE3，在细胞表面显示LPS-2作为其主要LPS形式。该结果表明抗体在两个菌株上均结合相似的表位，因此，豆科农杆菌和etli具有非常相似的LPS核心和脂质A抗原结构。对来自分离的R.etli的LPS-2和脂质A的抗体结合位点的更详细分析表明，某些抗体（JIM 32、33、34和MASM-1）结合了核心寡糖的某些部分，而其他（ JIM 35和JIM 38）涉及脂质A.这些抗体已被证明可用于LPS抗原形式的生化分析，例如某些LPS形式与抗体JIM 37的反应性丧失导致迄今未发现的发现。酚/水提取过程中形成的沉淀物中形成LPS抗原的形式。这种新形式与JIM37抗体反应。此外，某些抗体仅与经超声处理的野生型R. etli细胞发生阳性反应，这表明存在一种有效的掩盖核心抗原在整个细菌细胞上展示的有效方法，或者LPS的核心形式从未展示过。细菌细胞的表面。一旦被证实，这两种可能性对于指定根瘤菌细胞表面都很重要，并且也可能与共生结节的感染和发育有关。

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