Isolation and Identification of a Protein Interacting With P37 Protein of Mycoplasma hyorhinis
DOI:
Author:
Affiliation:

Clc Number:

Fund Project:

This work was supported by grants from The National Natural Sciences Foundation of China (30130190), Natural Science Foundation of Beijing(7012007) and Oncology Key Program of Peking University.

  • Article
  • |
  • Figures
  • |
  • Metrics
  • |
  • Reference
  • |
  • Related
  • |
  • Cited by
  • |
  • Materials
  • |
  • Comments
    Abstract:

    High ratio infection of Mycoplasma hyorhinis in gastric tumor tissues suggests a possible association between mycoplasma infection and cancer. P37, an outer-membrane bacterial protein from Mycoplasma hyorhinis, increases neoplastic invasivity and metastasis and induces TNF-α secretion from human peripheral blood mononuclear cells (PBMC). To investigate the functional mechanism of P37, yeast two-hybrid system was used to isolate proteins interacted with P37 from a human placenta cDNA library. Among the 2.6×106 transformant clones, one positive clone was obtained. Sequence analysis revealed that the clone is a cDNA fragment from Norpeg and encode a carboxy terminal protein. The interaction between P37 and Norpeg was further confirmed by ELISA and GST-Pull down assay. This result would be useful to study the function of P37 further.

    Reference
    Related
    Cited by
Get Citation

SUN Yu-Ning, JIN Geng-Lin, ZHANG Jian-Zhi, WU Jian, SHOU Cheng-Chao. Isolation and Identification of a Protein Interacting With P37 Protein of Mycoplasma hyorhinis[J]. Progress in Biochemistry and Biophysics,2004,31(10):902-906

Copy
Share
Article Metrics
  • Abstract:
  • PDF:
  • HTML:
  • Cited by:
History
  • Received:April 26,2004
  • Revised:May 30,2004
  • Accepted:
  • Online:
  • Published: