Helicobacter pylori strain ATCC700392 encodes a methyl-accepting chemotaxis receptor protein (MCP) for arginine and sodium bicarbonate

FEMS Microbiol Lett. 2003 Jul 29;224(2):175-81. doi: 10.1016/S0378-1097(03)00423-3.

Abstract

Helicobacter pylori ATCC43504 responds chemotactically to aspartic acid and serine, but not to arginine, nor to sodium bicarbonate. In contrast, H. pylori ATCC700392 (strain 26695) shows chemotaxis to all four attractants. Open reading frame HP0099 from H. pylori 26695 is predicted to encode one of three methyl-accepting chemotaxis receptor proteins (MCPs). When Escherichia coli is transformed with a plasmid carrying HP0099 from strain 26695, the recombinants acquire chemotaxis to arginine, bicarbonate, and urea. In H. pylori 43504, the HP0099 gene is interrupted with a mini-IS605 insertion, which accounts for its inability to recognize arginine and bicarbonate as attractants. Together, these results argue that the H. pylori HP0099 gene encodes an MCP for arginine and bicarbonate.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arginine / pharmacology*
  • Bacterial Proteins*
  • Base Sequence
  • Chemotaxis / drug effects*
  • Chemotaxis / genetics
  • DNA Transposable Elements
  • Helicobacter pylori / genetics*
  • Helicobacter pylori / metabolism
  • Membrane Proteins / genetics*
  • Membrane Proteins / metabolism
  • Methyl-Accepting Chemotaxis Proteins
  • Molecular Sequence Data
  • Signal Transduction
  • Sodium Bicarbonate / pharmacology*
  • Substrate Specificity
  • Urea / pharmacology

Substances

  • Bacterial Proteins
  • DNA Transposable Elements
  • Membrane Proteins
  • Methyl-Accepting Chemotaxis Proteins
  • Sodium Bicarbonate
  • Urea
  • Arginine