CONSERVATION OF THE D-MANNOSE-ADHESION PROTEIN AMONG TYPE-1 FIMBRIATED MEMBERS OF THE FAMILY ENTEROBACTERIACEAE
CONSERVATION OF THE D-MANNOSE-ADHESION PROTEIN AMONG TYPE-1 FIMBRIATED MEMBERS OF THE FAMILY ENTEROBACTERIACEAE
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DOI：
10.1038/336682a0
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发表时间：
1988-12-15
期刊：
影响因子：
64.8
通讯作者：
BEACHEY, EH
中科院分区：
文献类型：
--
作者：
ABRAHAM, SN;SUN, DX;BEACHEY, EH
肠杆菌科的多种属和种具有使它们能够结合真核细胞上的D-甘露糖残基的表面菌毛1 -3。直到最近，人们认为D-甘露糖结合位点位于大肠杆菌中这些细胞器的相对分子质量（Mr）为17，000（17 K）的主要结构亚基（FimA）中4，5。新的证据表明，该结合位点存在于位于菌毛顶端和沿菌毛长度沿着长间隔的次要蛋白Mr 28 -31 K（FimH）中6 -12，并使人联想到肾盂肾炎相关皮利（Pap）和S菌毛的次要顶端粘附蛋白13，14。与主要FimA亚基的抗原异质性不同，FimH的抗原结构在不同的E.大肠杆菌10，11.在这里，我们报告了一个更广泛的保护，这种次要的粘附蛋白延伸到其他属和种的1型菌毛肠杆菌。我们的研究结果可能对开发针对动物（甚至人类）革兰氏阴性杆菌感染的广泛保护性疫苗具有影响。
A variety of genera and species of the family Enterobacteriaceae bear surface fimbriae that enable them to bind to D-mannose residues on eukaryotic cells1–3. Until recently, it was thought that the D-mannose binding site was located in the major structural subunit (FimA), of relative molecular mass (Mr) 17,000 (17 K), of these organelles inEscherichia coli4,5. New evidence indicates that this binding site resides instead in a minor protein Mr28–31 K (FimH) located at the tips and at long intervals along the length of the fimbriae6–12, and is reminiscent of the minor tip adhesion proteins of pyelonephritis-associated pili (Pap) and S fimbriae13,14. In contrast to the antigenic heterogeneity of the major FimA subunit, the antigenic structure of FimH is conserved among different strains ofE. coli10,11. Here, we report an even broader conservation of this minor adhesion protein extending to other genera and species of type 1 fimbriated Enterobacteriaceae. Our results may have implications for the development of broadly protective vaccines against Gram-negative bacillary infections in animals and perhaps in man.