Kansau I, Labigne A
Unité de Pathogénie Bactérienne des Muqueuses, INSERM U389, Institut Pasteur, Paris, France.
Aliment Pharmacol Ther. 1996 Apr;10 Suppl 1:51-6. doi: 10.1046/j.1365-2036.1996.22164005.x.
As in any other bacterium, Helicobacter pylori synthesizes two heat shock proteins, the HspA (GroES or Hsp 10 homologue) and the HspB (GroEL or Hsp60 homologue). This article summarizes the present knowledge of genetics, function and the antigenic, immunogenic and protective properties of these two abundant proteins. H. pylori HspA and HspB antigens have vital functions for the bacterium; they share most of the bacterial chaperonin characteristics. However, the unique structure of HspA and its unique capacity to specifically bind nickel ions, strongly suggest an essential role of HspA with regard to the urease metallo-enzyme. The putative role of the H. pylori Hsp antigens in autoimmunity is also addressed.
与其他任何细菌一样，幽门螺杆菌合成两种热休克蛋白，即HspA（GroES或Hsp 10同源物）和HspB（GroEL或Hsp60同源物）。本文总结了目前关于这两种丰富蛋白质的遗传学、功能以及抗原性、免疫原性和保护性的知识。幽门螺杆菌HspA和HspB抗原对该细菌具有重要功能；它们具有大多数细菌伴侣蛋白的特征。然而，HspA的独特结构及其特异性结合镍离子的独特能力，强烈表明HspA在脲酶金属酶方面具有重要作用。本文还探讨了幽门螺杆菌Hsp抗原在自身免疫中的假定作用。
