Cell surface Lactobacillus plantarum LA 318 glyceraldehyde-3-phosphate dehydrogenase (GAPDH) adheres to human colonic mucin

H. Kinoshita, H. Uchida, Y. Kawai, T. Kawasaki, N. Wakahara, H. Matsuo, M. Watanabe, H. Kitazawa, S. Ohnuma, K. Miura, A. Horii, T. Saito

Research output: Contribution to journalArticlepeer-review

114 Citations (Scopus)

Abstract

Aims: To characterize the adhesion molecule of Lactobacillus plantarum LA 318 that shows high adhesion to human colonic mucin (HCM). Methods and Results: The adhesion test used the BIACORE assay where PBS-washed bacterial cells showed a significant decrease in adherence to HCM than distilled water-washed cells. A component in the PBS wash fraction adhered to the HCM and a main protein was detected as a c. 40-kDa band using SDS-PAGE. Using homology comparisons of the N-terminal amino acid sequences compared with sequence databases, this protein was identified as glyceraldehyde-3-phosphate dehydrogenase (GAPDH). The DNA sequence of LA 318 GAPDH was 100% identical to the GAPDH (gapB) of L. plantarum WCFS1. The purified GAPDH adhered to HCM. Conclusions: We found the adhesin of L. plantarum LA 318 to HCM in its culture PBS wash fraction. The molecule was identified as GAPDH. Because LA 318 possesses the same adhesin as many pathogens, the lactobacilli GAPDH may compete with pathogens infecting the intestine. Significance and Impact of the Study: This is the first report showing GAPDH expressed on the cell surface of lactobacilli adheres to mucin suggesting L. plantarum LA 318 adheres to HCM using GAPDH binding activity to colonize the human intestinal mucosa.

Original languageEnglish
Pages (from-to)1667-1674
Number of pages8
JournalJournal of Applied Microbiology
Volume104
Issue number6
DOIs
Publication statusPublished - 2008 Jun

Keywords

  • Adhesion
  • BIACORE
  • Glyceraldehyde-3-phosphate dehydrogenase
  • Human colonic mucin
  • Lactobacillus plantarum
  • Probiotics

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology

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