Phage display reveals 52 novel extracellular and transmembrane proteins from Lactobacillus reuteri DSM 20016T

Wall, Torun; Roos, Stefan; Jacobsson, Karin; Rosander, Anna; Jonsson, Hans

doi:10.1099/mic.0.26530-0

Cited by 22 publications

(22 citation statements)

References 52 publications

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“…The remaining LysM proteins (Lr0537, Lr0858, Lr1267) were of unknown function, but conserved in bacteria and similar to each other. Lr0858 is a homologue to the previously identified Lre0018 from L. reuteri strain DSM 20016 [7]. The proteins are similar to Sep from Lactobacillus fermentum BR11 [41] and to the Apf proteins from L. johnsonii and Lactobacillus gasseri [42] (Fig.…”

Section: Resultsmentioning

confidence: 61%

The cell surface of Lactobacillus reuteri ATCC 55730 highlighted by identification of 126 extracellular proteins from the genome sequence

Båth

Roos

Wall

et al. 2005

FEMS Microbiology Letters

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Bioinformatical analyses of a draft genome sequence of the commensal bacterium Lactobacillus reuteri ATCC 55730 revealed 126 genes encoding putative extracellular proteins. The function, localization and distribution in bacterial species were predicted. Interestingly, few proteins possessed LPXTG motifs or C-terminal transmembrane anchors. Instead eight proteins were putatively anchored by GW repeats and several secreted proteins were likely to be re-associated to the surface. The majority of the extracellular proteins were widely distributed, i.e., found universally or in gram-positive bacteria, but 24 were only detected in L. reuteri. Further, the number of transporters was lower, while the number of enzyme was higher than in related species.

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Section: Resultsmentioning

confidence: 61%

The cell surface of Lactobacillus reuteri ATCC 55730 highlighted by identification of 126 extracellular proteins from the genome sequence

Båth

Roos

Wall

et al. 2005

FEMS Microbiology Letters

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“…2A). Antibodies raised against this protein detected a phagemid that contained the start of an open reading frame (5,905 bp) encoding a high-molecular-mass protein (Lsp) that had considerable nucleotide base sequence homology (86% identity (36), indicating that the protein was transported to the cell surface. Surprisingly, the cloned partial lsp gene encoded a protein of Ͼ208 kDa, which is larger than the protein that was eluted from the SDS-PAGE gel.…”

Section: Resultsmentioning

confidence: 99%

A High-Molecular-Mass Surface Protein (Lsp) and Methionine Sulfoxide Reductase B (MsrB) Contribute to the Ecological Performance of Lactobacillus reuteri in the Murine Gut

Walter

Chagnaud

Tannock

et al. 2005

Appl Environ Microbiol

114

125

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Members of the genus Lactobacillus are common inhabitants of the gut, yet little is known about the traits that contribute to their ecological performance in gastrointestinal ecosystems. Lactobacillus reuteri 100-23 persists in the gut of the reconstituted Lactobacillus-free mouse after a single oral inoculation. Recently, three genes of this strain that were specifically induced (in vivo induced) in the murine gut were identified (38). We report here the detection of a gene of L. reuteri 100-23 that encodes a high-molecular-mass surface protein (Lsp) that shows homology to proteins involved in the adherence of other bacteria to epithelial cells and in biofilm formation. The three in vivo-induced genes and lsp of L. reuteri 100-23 were inactivated by insertional mutagenesis in order to study their biological importance in the murine gastrointestinal tract. Competition experiments showed that mutation of lsp and a gene encoding methionine sulfoxide reductase (MsrB) reduced ecological performance. Mutation of lsp impaired the adherence of the bacteria to the epithelium of the mouse forestomach and altered colonization dynamics. Homologues of lsp and msrB are present in the genomes of several strains of Lactobacillus and may play an important role in the maintenance of these bacteria in gut ecosystems.The guts of mammals are colonized by a complex collection of microorganisms (the gut microbiota) that influence biochemical, physiological, immunological, and nonspecific disease resistance characteristics of the host (10). The bacterial composition of this ecosystem has been shown to be remarkably stable over time (43). Members of the gut microbiota have presumably coevolved with their host species and must possess traits that enable them to establish and maintain themselves in a lotic (flowing) and competitive environment. On the other hand, there are microbes present in the gastrointestinal tract that have a transient existence (allochthonous components), and this situation raises questions about what factors distinguish resident members of the microbiota from allochthonous members (27).Lactobacillus reuteri strain 100-23 is a true (autochthonous) resident of the murine gut because it adheres to the nonsecretory epithelium of the forestomach and persists at constant population levels in particular regions of the gut throughout the life of the murine host (13, 39).We maintain a colony of mice whose gut microbiota is devoid of lactobacilli but is otherwise equivalent to that of conventional mice (32). These reconstituted Lactobacillus-free (RLF) mice permit the study of Lactobacillus traits against a standardized bacteriological background. L. reuteri 100-23 and the RLF mouse gut therefore provide an appropriate model system with which to study the molecular basis of Lactobacillus autochthony.While L. reuteri 100-23 inhabits the murine gut, genes encoding methionine sulfoxide reductase (msrB), xylose isomerase (xylA), and a protein with low similarity to methionine synthase II (met) are specifically induced (38). Add...

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“…To this end, genome library of VMKB44 strain in pG8SAET phagemid vector containing about 4×10 6 clones with inserts of 100 to 3000 n. p. was created. According to the previously determined criteria [2,7], this library size is sufficient for presentation of all open reading frames of the bacterial genome in fusions with the pVIII protein and signal peptide genes in the vector.…”

Section: Resultsmentioning

confidence: 99%

Search for Protein Adhesin Gene in Bifidobacterium Longum Genome Using Surface Phage Display Technology

et al. 2008

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A fragment of the nucleotide sequence encoding polypeptide binding to HT-29 epithelial cells was cloned from VMKB44 Bifidobacterium longum genome library using surface phage display technology. Sequencing of this polypeptide consisting of 26 amino acid residues showed that it is an extracellular fragment of a large BL0155 transmembrane protein belonging to the ABC transport protein superfamily. The genes encoding homologues of this protein were detected in genomes of not only bifidobacteria of different species, but also in many other enteric commencals and pathogens.

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Phage display reveals 52 novel extracellular and transmembrane proteins from Lactobacillus reuteri DSM 20016T

Cited by 22 publications

References 52 publications

The cell surface of Lactobacillus reuteri ATCC 55730 highlighted by identification of 126 extracellular proteins from the genome sequence

The cell surface of Lactobacillus reuteri ATCC 55730 highlighted by identification of 126 extracellular proteins from the genome sequence

A High-Molecular-Mass Surface Protein (Lsp) and Methionine Sulfoxide Reductase B (MsrB) Contribute to the Ecological Performance of Lactobacillus reuteri in the Murine Gut

Search for Protein Adhesin Gene in Bifidobacterium Longum Genome Using Surface Phage Display Technology

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