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.

Secretion of the housekeeping protein glyceraldehyde-3-phosphate dehydrogenase by the LEE-encoded type III secretion system in enteropathogenic Escherichia coli

“…It may be hypothesized that GAPDH secretion may confer to these strains an advantage in the context of gut colonization with respect to other components of the intestinal microbiota. In fact, GAPDH secretion and its interaction with extracellular host components such as mucin or extracellular matrix proteins are rather common among diverse pathogens and probiotic microorganisms (Hurmalainen et al, 2007;Kinoshita et al, 2008;Lama et al, 2009;Pancholi and Chhatwal, 2003).…”

Role of Mycoplasma pneumoniae glyceraldehyde-3-phosphate dehydrogenase (GAPDH) in mediating interactions with the human extracellular matrix

“…Besides their glycolytic activity in the cytosol, these enzymes have been found at the surface of micro-organisms, where they act as binding partners of proteins of the human Abbreviations: ECM, extracellular matrix; FCS, fetal calf serum; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; MMR, multiple mutation reaction. Microbiology (2011Microbiology ( ), 157, 2328 As a surface-associated protein, GAPDH can interact with not only one or more specified host factors like fibronectin, fibrinogen, albumin, laminin, collagen and plasminogen but also human colonic mucin, human epithelial and endothelial cells or fimbriae of other bacterial species in biofilms (Pancholi & Fischetti, 1992;Gozalbo et al, 1998;Bergmann et al, 2004;Barbosa et al, 2006;Egea et al, 2007;Kinoshita et al, 2008;Nagata et al, 2009;Purves et al, 2010;Tunio et al, 2010a).…”

Functional Characterization of a Mucus-Specific LPXTG Surface Adhesin from Probiotic Lactobacillus rhamnosus GG

“…Thus far, the precise molecular mechanisms that differentiate the colonization ability between autochthonous and allochthonous intestinal lactobacilli remain undefined (42), although they are likely to be partly dependent on a diverse range of cell surface adhesion molecule-mediated interactions with the host intestinal mucosa. With that being said, there are a growing number of reports in the literature that indicate that lactobacillar adherence to the intestinal mucosal layer is mediated by surface proteins with a mucus-binding capacity (15,21,22,25,30,32,33,41). Moreover, homology-driven genome mining in several Lactobacillus spp.…”