Kobayashi H, Komido M, Watanabe M, Matsuda K, Suzuki M, Ikeda T, Oyamada H, Shibata N, Suzuki S
Second Department of Hygienic Chemistry, Tohoku College of Pharmacy, Miyagi, Japan.
Infect Immun. 1994 Oct;62(10):4425-31. doi: 10.1128/iai.62.10.4425-4431.1994.
We conducted a structural analysis of the antigenic cell wall mannoprotein (mannan) isolated from Candida kefyr (formerly Candida pseudotropicalis) IFO 0586. The result of two-dimensional homonuclear Hartmann-Hahn analysis of this mannan indicates that the molecule is constructed from alpha-1,2- and alpha-1,6-linked mannopyranose residues. Upon alkali treatment (beta-elimination reaction), this mannan released two alpha-1,2-linked mannooligosaccharides, biose and triose. The structure of the alkali-stable mannan (outer chain) moiety was investigated by acetolysis. The structures of the resultant oligosaccharides, biose and triose, from the outer chain moiety were found to be the same as those of the alkali-released ones. Further, the treatment of the parent mannan with an Arthrobacter GJM-1 exo-alpha-mannosidase gave a linear mannan consisting solely of alpha-1,6-linked mannopyranose residues. These results indicate that the mannan forms the long backbone of the alpha-1,6 linkage, with a large number of short alpha-1,2-linked oligomannosyl side chains forming a comblike structure. Moreover, we investigated the serological properties of this mannan by performing an inhibition assay of a slide agglutination reaction with mannooligosaccharides and polyclonal factor sera (Candida Check; Iatron). The result indicates that the factor 1 serum preferentially recognizes the alpha-1,2-linked oligomannosyl side chains in this mannan. On the other hand, the fact that the mannan does not contain an antigenic determinant(s) corresponding to factor 8 suggests that the epitope(s) of this factor resides in other molecules on the cell surface of this strain.
我们对从高加索假丝酵母(原热带假丝酵母)IFO 0586中分离出的抗原性细胞壁甘露糖蛋白(甘露聚糖)进行了结构分析。对该甘露聚糖进行二维同核Hartmann-Hahn分析的结果表明,该分子由α-1,2-和α-1,6-连接的甘露吡喃糖残基构成。经碱处理(β-消除反应)后,该甘露聚糖释放出两种α-1,2-连接的甘露寡糖,即二糖和三糖。通过乙酰解研究了碱稳定的甘露聚糖(外链)部分的结构。发现从外链部分得到的寡糖二糖和三糖的结构与碱释放的那些相同。此外,用节杆菌GJM-1外切α-甘露糖苷酶处理亲本甘露聚糖,得到了仅由α-1,6-连接的甘露吡喃糖残基组成的线性甘露聚糖。这些结果表明,甘露聚糖形成了α-1,6连接的长主链,有大量短的α-1,2-连接的寡甘露糖基侧链形成梳状结构。此外,我们通过用甘露寡糖和多克隆因子血清(念珠菌检测;医创)进行玻片凝集反应抑制试验,研究了该甘露聚糖的血清学特性。结果表明,因子1血清优先识别该甘露聚糖中的α-1,2-连接的寡甘露糖基侧链。另一方面,该甘露聚糖不含有与因子8相对应的抗原决定簇这一事实表明,该因子的表位存在于该菌株细胞表面的其他分子中。