J Bacteriol Virol.  2008 Jun;38(2):53-60. 10.4167/jbv.2008.38.2.53.

Proteomic analysis of Helicobacter pylori J99 Outer Membrane Protein by Tandem Mass Spectrometry

Affiliations
  • 1Department of Microbiology,Gyeongsang National University College of Medicine, Jinju, Korea. scbaik@gaechuk.gsnu.ac.kr
  • 2Department of Pediatrics, Gyeongsang National University College of Medicine, Jinju, Korea.
  • 3Central Instrument Facility, Gyeongsang National University, Jinju, Korea.
  • 4Research Institute of Life Science, Gyeongsang National University, Jinju, Korea.

Abstract

The protein identity of sarcosine-insoluble outer membrane proteins (OMPs) of Helicobacter pylori J99 was determined with the basic study of understanding the function of proteins. A sarcosine-insoluble OMPs was resolved by two-dimensional electrophoresis with immobilized pH gradient strips. The most abundant proteins were shown in the alkaline pI regions (6.0~11.0) with molecular masses of 10 to 100 kDa. We have performed an extensive proteome analysis by quadrupole time of flight (Q-TOF) mass spectrometry (MS). Here, of 50 spots processed, 42 spots were identified, which represented 16 genes and we newly detected 8 kinds of proteins (JHP0119, JHP0388, JHP1046, JHP1405, JHP0073, JHP0551, JHP1382, JHP0552) from the sarcosin-insoluble fraction of H. pylori J99. Those may be used to elucidate the characterization of the OMPs of H. pylori J99, which will help identify new potential target proteins for vaccine development and drug therapy.

Keyword

Helicobacter pylori; Outer membrane protein; Q-TOF MS

MeSH Terms

Electrophoresis
Helicobacter
Helicobacter pylori
Mass Spectrometry
Membrane Proteins
Membranes
Proteins
Proteome
Proton-Motive Force
Tandem Mass Spectrometry
Membrane Proteins
Proteins
Proteome
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