Proteomic analysis of Helicobacter pylori J99 outer membrane protein by tandem mass spectrometryopen access
- Authors
- Kim, K.-M.; Lee, S.-G.; Joo, J.-S.; Kwon, Y.-C.; Bea, D.-W.; Song, J.-Y.; Kang, H.-L.; Lee, W.-K.; Cho, M.-J.; Rhee, K.-H.; Youn, H.-S.; Baik, S.-C.
- Issue Date
- 2008
- Publisher
- The Korean Society for Mocrobiology / The Korean Society of Virology
- Keywords
- Helicobacter pylori; Outer membrane protein; Q-TOF MS
- Citation
- Journal of Bacteriology and Virology, v.38, no.2, pp 53 - 60
- Pages
- 8
- Indexed
- SCOPUS
KCI
- Journal Title
- Journal of Bacteriology and Virology
- Volume
- 38
- Number
- 2
- Start Page
- 53
- End Page
- 60
- URI
- https://scholarworks.gnu.ac.kr/handle/sw.gnu/28134
- DOI
- 10.4167/jbv.2008.38.2.53
- ISSN
- 1598-2467
2093-0429
- 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.
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