Recombinant antigen from Helicobacter pylori urease as vaccine against H. pylori-associated disease

Ryoji Fujii1, Fumiko Morihara, Keigo Fukushima

  • 1Fukuyama Medical Laboratory Co., Fukuyama-city, Hiroshima 720-8510, Japan.

Insights

Researchers developed seventeen monoclonal antibodies targeting Helicobacter pylori urease (UreB). Several antibodies inhibited urease activity and showed specific binding to the stomach pathogen, offering potential diagnostic and therapeutic applications.

Area of Science:

  • Biochemistry
  • Immunology
  • Microbiology

Background:

  • The beta-subunit (UreB) of Helicobacter pylori urease contains the enzyme's active site.
  • Understanding UreB is crucial for developing targeted interventions against H. pylori.

Purpose of the Study:

  • To generate and characterize monoclonal antibodies against the UreB subunit of H. pylori urease.
  • To assess the specificity, cross-reactivity, and functional impact of these antibodies on urease activity.

Main Methods:

  • Determined a key 135-amino acid sequence of UreB.
  • Expressed UreB as a recombinant glutathione-S-transferase (GST) fusion protein in E. coli.
  • Produced 17 monoclonal antibodies (UA-1-17) using UreB-GST as the immunogen.

Main Results:

  • Monoclonal antibodies demonstrated high specificity to UreB, with some cross-reacting with Jack bean urease.
  • Approximately 70% of antibodies inhibited urease enzymatic activity, with UA-15 MAb reducing activity by 53%.
  • Antibodies and rabbit antiserum specifically bound to H. pylori in human stomach mucosa and suppressed urease activity.

Conclusions:

  • Generated specific monoclonal antibodies against H. pylori urease beta-subunit (UreB).
  • Demonstrated the potential of these antibodies for diagnostic detection and therapeutic inhibition of H. pylori urease.
  • Highlighted the immunogenic properties of recombinant UreB-GST in inducing specific antibodies and antisera.

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