In situ localization of the 60 k protein of Helicobacter pylori, which belongs to the family of heat shock proteins, by immuno-electron microscopy

Zentralbl Bakteriol. 1993 Sep;280(1-2):73-85. doi: 10.1016/s0934-8840(11)80942-4.

Abstract

The groEl homologue of Helicobacter pylori was isolated and characterized by means of immunoelectron microscopy, after cryosectioning. The 60 k protein was isolated from Helicobacter pylori by treatment of the cells with 2-butanol and purified by anion exchange chromatography. The native molecular weight of the 60 k protein was estimated to be 420 k by size exclusion chromatography. The purified 60 k protein showed the typical rotational symmetry of chaperonins when analyzed by electron microscopy. Ultrathin sections of Helicobacter pylori were immunostained by a polyclonal antibody directed against the hsp-65 of Mycobacterium tuberculosis. The label revealed a clustered localization of the 60 k protein on the cell surface as well as in the periplasmic space.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Antibodies, Bacterial / immunology
  • Bacterial Proteins / analysis*
  • Bacterial Proteins / ultrastructure
  • Chaperonin 60
  • Chaperonins*
  • Cross Reactions
  • Electrophoresis, Polyacrylamide Gel
  • Heat-Shock Proteins / analysis*
  • Heat-Shock Proteins / immunology
  • Heat-Shock Proteins / ultrastructure
  • Helicobacter pylori / chemistry*
  • Helicobacter pylori / ultrastructure
  • Immunoblotting
  • In Situ Hybridization
  • Microscopy, Immunoelectron
  • Molecular Sequence Data
  • Mycobacterium tuberculosis / immunology
  • Sequence Homology, Amino Acid

Substances

  • 60K protein, Helicobacter pylori
  • Antibodies, Bacterial
  • Bacterial Proteins
  • Chaperonin 60
  • Heat-Shock Proteins
  • heat-shock protein 65, Mycobacterium
  • Chaperonins