ArticleApplied and environmental microbiology2004
Identification and characterization of the novel LysM domain-containing surface protein Sep from Lactobacillus fermentum BR11 and its use as a peptide fusion partner in Lactobacillus and Lactococcus.
Article in Applied and environmental microbiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 42 citations in OpenAlex.
- Development of a lactose-complemented antibiotic-free host-vector platform for stable enzyme expression in Limosilactobacillus fermentum 217 - 82.World journal of microbiology & biotechnology · 2026Article
- Novel LysM motifs for antigen display on lactobacilli for mucosal immunization.Scientific reports · 2021Article
- Immobilization of β-Galactosidases on theCatalysts (Basel, Switzerland) · 2019Article
- The aggregation-promoting factor in Lactobacillus delbrueckii ssp. bulgaricus: confirmation of the presence and expression of the apf gene and in silico analysis of the corresponding protein.World journal of microbiology & biotechnology · 2018Article
- Display of recombinant proteins at the surface of lactic acid bacteria: strategies and applications.Microbial cell factories · 2016Review
- Lactic acid bacteria--20 years exploring their potential as live vectors for mucosal vaccination.Applied microbiology and biotechnology · 2015Review
- Exploiting the peptidoglycan-binding motif, LysM, for medical and industrial applications.Applied microbiology and biotechnology · 2014Review
- Molecular characterization of host-specific biofilm formation in a vertebrate gut symbiont.PLoS genetics · 2013Article
- In situ gastrointestinal protection against anthrax edema toxin by single-chain antibody fragment producing lactobacilli.BMC biotechnology · 2011Article
- Murein and pseudomurein cell wall binding domains of bacteria and archaea--a comparative view.Applied microbiology and biotechnology · 2011Review
- Inhibition of Staphylococcus aureus by lysostaphin-expressing Lactobacillus plantarum WCFS1 in a modified genital tract secretion medium.Applied and environmental microbiology · 2011Article
- Integrative expression system for delivery of antibody fragments by lactobacilli.Applied and environmental microbiology · 2011Article
- Characterization of a novel family of fibronectin-binding proteins with M23 peptidase domains from Treponema denticola.Molecular oral microbiology · 2010Article
- Functional roles of aggregation-promoting-like factor in stress tolerance and adherence of Lactobacillus acidophilus NCFM.Applied and environmental microbiology · 2010Article
- Characterization of a novel LysM domain from Lactobacillus fermentum bacteriophage endolysin and its use as an anchor to display heterologous proteins on the surfaces of lactic acid bacteria.Applied and environmental microbiology · 2010Article
- Development of a LytE-based high-density surface display system in Bacillus subtilis.Microbial biotechnology · 2008Article
- System using tandem repeats of the cA peptidoglycan-binding domain from Lactococcus lactis for display of both N- and C-terminal fusions on cell surfaces of lactic acid bacteria.Applied and environmental microbiology · 2008Article
- Display of alpha-amylase on the surface of Lactobacillus casei cells by use of the PgsA anchor protein, and production of lactic acid from starch.Applied and environmental microbiology · 2006Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Examination of supernatant fractions from broth cultures of Lactobacillus fermentum BR11 revealed the presence of a number of proteins, including a 27-kDa protein termed Sep. The amino-terminal sequence of Sep was determined, and the gene encoding it was cloned and sequenced. Sep is a 205-amino-acid protein and contains a 30-amino-acid secretion signal and has overall homology (between 39 and 92% identity) with similarly sized proteins of Lactobacillus reuteri, Enterococcus faecium, Streptococcus pneumoniae, Streptococcus agalactiae, and Lactobacillus plantarum. The carboxy-terminal 81 amino acids of Sep also have strong homology (86% identity) to the carboxy termini of the aggregation-promoting factor (APF) surface proteins of Lactobacillus gasseri and Lactobacillus johnsonii. The mature amino terminus of Sep contains a putative peptidoglycan-binding LysM domain, thereby making it distinct from APF proteins. We have identified a common motif within LysM domains that is shared with carbohydrate binding YG motifs which are found in streptococcal glucan-binding proteins and glucosyltransferases. Sep was investigated as a heterologous peptide expression vector in L. fermentum, Lactobacillus rhamnosus GG and Lactococcus lactis MG1363. Modified Sep containing an amino-terminal six-histidine epitope was found associated with the cells but was largely present in the supernatant in the L. fermentum, L. rhamnosus, and L. lactis hosts. Sep as well as the previously described surface protein BspA were used to express and secrete in L. fermentum or L. rhamnosus a fragment of human E-cadherin, which contains the receptor region for Listeria monocytogenes. This study demonstrates that Sep has potential for heterologous protein expression and export in lactic acid bacteria.
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