Understanding the adhesion mechanism of a mucin binding domain from Lactobacillus fermentum and its role in enteropathogen exclusion

Chatterjee, Maitrayee; Pushkaran, Anju Choorakottayil; Vasudevan, Anil; Menon, Krishnakumar N.; Biswas, Raja; Mohan, C. Gopi

doi:10.1016/j.ijbiomac.2017.10.107

Cited by 38 publications

(26 citation statements)

References 43 publications

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“…In addition, ovomucin could provide an important innate immune barrier against various toxins and pathogens, and the sialic acid at the end of the glycans is essential in the recognition of avian influenza viruses [ [24] , [25] , [26] ]. Therefore, the high abundance of ovomucin in the CEVM provides a strong natural defense, protecting the chicken embryo (or preserving the egg yolk).…”

Section: Resultsmentioning

confidence: 99%

A puzzle piece of protein N-glycosylation in chicken egg: N-glycoproteome of chicken egg vitelline membrane

Xiao

Wang

Cheng

et al. 2020

International Journal of Biological Macromolecules

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The chicken egg vitelline membrane (CEVM) is an important structure for the transmembrane transport of egg yolk components, protection of the blastodisc, and separation of egg white and egg yolk. In this study, the N-glycoproteome of the CEVM was mapped and analyzed in depth. Total protein of the CEVM was digested, and the glycopeptides were enriched by a hydrophilic interaction liquid chromatography microcolumn and identified by nano liquid chromatography/tandem mass spectrometry. A total of 435 N-glycosylation sites on 208 N-glycoproteins were identified in CEVM. Gene Ontology enrichment analysis showed that CEVM N-glycoproteins are mainly involved in the regulation of proteinases/inhibitors and transmembrane transport of lipids. Mucin-5B is the primary N-glycoprotein in the CEVM. Comparison of the main N-glycoproteins between the CEVM and other egg parts revealed the tissue specificity of N-glycosylation of egg proteins. The results provide insights into protein N-glycosylation in the chicken egg, CEVM functions and underlying mechanisms.

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Section: Resultsmentioning

confidence: 99%

A puzzle piece of protein N-glycosylation in chicken egg: N-glycoproteome of chicken egg vitelline membrane

Xiao

Wang

Cheng

et al. 2020

International Journal of Biological Macromolecules

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“…It has been demonstrated that L. fermentum BCS87 32-Mmubp, a component of an ABC transporter system, is a mucus and mucin binding protein, suggesting that membrane transport proteins may have more than one function [ 20 ]. Chatterjee et al [ 21 ] have shown that a 93-amino acid mucin binding domain (MBD93) of the LAF_0673 protein from L. fermentum IFO 3956 is sufficient for mucin binding and protection from enteric pathogens invasion (Table 2 ). Recently, immunomodulatory activity of MUB from L. acidophilus has been reported.…”

Section: Introductionmentioning

confidence: 99%

Lactobacillus Cell Surface Proteins Involved in Interaction with Mucus and Extracellular Matrix Components

2020

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The gut microbiota is a complex microbial ecosystem where bacteria, through mutual interactions, cooperate in maintaining of wellbeing and health. Lactobacilli are among the most important constituents of human and animal intestinal microbiota and include many probiotic strains. Their presence ensures protection from invasion of pathogens, as well as stimulation of the immune system and protection of the intestinal flora, often exerted through the ability to interact with mucus and extracellular matrix components. The main factors responsible for mediating adhesion of pathogens and commensals to the gut are cell surface proteins that recognize host targets, as mucus layer and extracellular matrix proteins. In the last years, several adhesins have been reported to be involved in lactobacilli–host interaction often miming the same mechanism used by pathogens.

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“…In contrast, EF-Tu interacts with a sulfated galactose residue of mucin, whereas the mucin-binding domain (MucBD) recognizes terminal sialic acid and sulfated carbohydrate moieties [18]. In addition, a 93-amino acid mucin-binding domain (MBD93) from Lactobacillus fermentum interacts strongly with terminally expressed mucin glycans including GalNAc, GlcNAc, Gal, and sialic acid through its surface amino acid residues, Ser 57 , Pro 58 , Ile 60 , Tyr 63 , and Ala 65 , a process that involves hydrogen bonds [46]. Homology modeling followed by docking analysis revealed that GAPDH of L. reuteri interacts with mucin through the key surface residues Met 1 , Ser 2 , Val 3 , Ser 29 , Asp 30 , and Ile 31 .…”

Section: Discussionmentioning

confidence: 99%

Glyceraldehyde-3-Phosphate Dehydrogenase Increases the Adhesion of Lactobacillus reuteri to Host Mucin to Enhance Probiotic Effects

Deng

Dai

Zhang

et al. 2020

IJMS

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The ability to adhere to the intestinal mucus layer is an important property of probiotic bacteria. Lactobacillus reuteri strains ZJ615 and ZJ617 show low and high adhesion, respectively, to intestinal epithelial cells. In this study, we quantified bacterial cell wall-associated glyceraldehyde-3-phosphate dehydrogenases (cw-GAPDH) and bacterial cell membrane permeability in both strains using immunoblotting and flow cytometry, respectively. Highly adhesive L. reuteri ZJ617 possessed significantly more cw-GAPDH, higher cell membrane permeability, and significantly higher adhesive ability toward mucin compared with low-adhesive L. reuteri ZJ615. In vitro adhesion studies and analysis of interaction kinetics using the Octet, the system revealed significantly decreased interaction between L. reuteri and mucin when mucin was oxidized when bacterial surface proteins were removed when bacteria were heat-inactivated at 80 °C for 30 min, and when the interaction was blocked with an anti-GAPDH antibody. SWISS-MODEL analysis suggested intensive interactions between mucin glycans (GalNAcα1-O-Ser, GalNAcαSer, and Galβ3GalNAc) and GAPDH. Furthermore, in vivo studies revealed significantly higher numbers of bacteria adhering to the jejunum, ileum, and colon of piglets orally inoculated with L. reuteri ZJ617 compared with those inoculated with L. reuteri ZJ615; this led to a significantly decreased rate of diarrhea in piglets inoculated with L. reuteri ZJ617. In conclusion, there are strong correlations among the abundance of cw-GAPDH in L. reuteri, the ability of the bacterium to adhere to the host, and the health benefits of this probiotic.

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Understanding the adhesion mechanism of a mucin binding domain from Lactobacillus fermentum and its role in enteropathogen exclusion

Cited by 38 publications

References 43 publications

A puzzle piece of protein N-glycosylation in chicken egg: N-glycoproteome of chicken egg vitelline membrane

A puzzle piece of protein N-glycosylation in chicken egg: N-glycoproteome of chicken egg vitelline membrane

Lactobacillus Cell Surface Proteins Involved in Interaction with Mucus and Extracellular Matrix Components

Glyceraldehyde-3-Phosphate Dehydrogenase Increases the Adhesion of Lactobacillus reuteri to Host Mucin to Enhance Probiotic Effects

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