Cell surface Lactobacillus plantarum LA 318 glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH) adheres to human colonic mucin
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.
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Several probiotic strains contain significant adhesins, including enolase (ENO), glyceraldehyde-3-phosphate dehydrogenase (GAPDH), and elongation factor Tu (EF-Tu).
“Several probiotic strains have been found to contain significant adhesins, including proteins like enolase (ENO), glyceraldehyde-3phosphate dehydrogenase (GAPDH), and elongation factor Tu (EF-Tu) [11].”
From EVALUATION OF ADHESIVE AND AGGREGATION PROPERTIES OF LACTIC ACID BACTERIA ISOLATED FROM DIFFERENT BIOTOPES (2025) · cites this paper as [11]
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“Several probiotic strains have been found to contain significant adhesins, including proteins like enolase (ENO), glyceraldehyde-3-phosphate dehydrogenase (GAPDH), and elongation factor Tu (EF-Tu) [11].”
- Authors
- Kinoshita, H., Uchida, H., Kawai, Y., Kawasaki, T., Wakahara, N., Matsuo, H., Watanabe, M., Kitazawa, H., Ohnuma, S., Miura, K., Horii, A., & Saito, T.
- Affiliations
- Tohoku University (JP)
- Corresponding author
- Saito, T.
- Venue
- Journal of Applied Microbiology
- Publisher
- Oxford University Press (OUP)
- Published
- 2008-06
- Volume
- 104
- Issue
- 6
- Pages
- 1667-1674
- ISSN
- 1364-5072 (ISSN-L)
- 1365-2672
- OpenAlex
- W2068018928
- Cited by
- 163
- References
- 0
- Citations by year
- 2026: 5 · 2025: 4 · 2024: 8 · 2023: 8 · 2022: 5 · 2021: 7 · 2020: 11 · 2019: 9 · 2018: 8 · 2017: 9 · 2016: 12 · 2015: 12 · 2014: 8 · 2013: 9 · 2012: 12
- FWCI
- 19.23
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Applied Microbiology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Probiotics and Fermented Foods
- Life Sciences › Immunology and Microbiology › Microbiology › Reproductive tract infections research
- Health Sciences › Nursing › Nutrition and Dietetics › Infant Nutrition and Health
- Keywords
- glyceraldehyde-3-phosphate dehydrogenase, cell adhesion, adhesins, intestinal colonization, probiotic bacteria, Lactobacillus plantarum WCFS1
- MeSH terms
- Amino Acid Sequence, Bacterial Adhesion, Bacteriological Techniques, Base Sequence, Colon, Electrophoresis, Polyacrylamide Gel, Glyceraldehyde-3-Phosphate Dehydrogenases, Humans, Intestinal Mucosa, Molecular Sequence Data, Mucins, Polymerase Chain Reaction, Sequence Homology, Amino Acid, DNA Primers, Probiotics, Lactobacillus plantarum, Lactiplantibacillus plantarum
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