ArticleBMC microbiology2008
Identification and characterization of domains responsible for self-assembly and cell wall binding of the surface layer protein of Lactobacillus brevis ATCC 8287.
Article in BMC microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- Nonspecific Binding of a Putative S-Layer Protein to Plant Cell Wall Polysaccharides-Implication for Growth Competence ofInternational journal of molecular sciences · 2025Article
- Surface Display of Avian H5 and H9 Hemagglutinin Antigens on Non-Genetically ModifiedMicroorganisms · 2025Article
- Crystal structure of the C1 domain of the surface-layer protein SlpM from Lactobacillus brevis: a module involved in protein self-assembly.Acta crystallographica. Section F, Structural biology communications · 2025Article
- A new age in structural S-layer biology: Experimental and in silico milestones.The Journal of biological chemistry · 2025Review
- The molecular architecture ofProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Surface layer proteins in species of the family Lactobacillaceae.Microbial biotechnology · 2023Article
- Expression of heterologous heparan sulphate binding protein of3 Biotech · 2023Article
- Surface Layer Protein Pattern ofNutrients · 2022Article
- Molecular Logic of Prokaryotic Surface Layer Structures.Trends in microbiology · 2021Review
- S-layers: The Proteinaceous Multifunctional Armors of Gram-Positive Pathogens.Frontiers in microbiology · 2021Review
- Characterization of two extracellular arabinanases in Lactobacillus crispatus.Applied microbiology and biotechnology · 2020Article
- S-Layer Protein ofFrontiers in microbiology · 2019Article
- Lipoteichoic acid mediates binding of a Lactobacillus S-layer protein.Glycobiology · 2018Article
- The Adhesion of Lactobacillus salivarius REN to a Human Intestinal Epithelial Cell Line Requires S-layer Proteins.Scientific reports · 2017Article
- Differential protection by cell wall components of Lactobacillus amylovorus DSM 16698BMC microbiology · 2016Article
- Truncation Derivatives of the S-Layer Protein of Sporosarcina ureae ATCC 13881 (SslA): Towards Elucidation of the Protein Domain Responsible for Self-Assembly.Molecules (Basel, Switzerland) · 2016Article
- The N-Terminal GYPSY Motif Is Required for Pilin-Specific Sortase SrtC1 Functionality in Lactobacillus rhamnosus Strain GG.PloS one · 2016Article
- Hypothetical protein Avin_16040 as the S-layer protein of Azotobacter vinelandii and its involvement in plant root surface attachment.Applied and environmental microbiology · 2015Article
- Basic and clinical research on the regulation of the intestinal barrier by Lactobacillus and its active protein components: a review with experience of one center.Molecular biology reports · 2014Review
- S-layers: principles and applications.FEMS microbiology reviews · 2014Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundLactobacillus brevis ATCC 8287 is covered by a regular surface (S-) layer consisting of a 435 amino acid protein SlpA. This protein is completely unrelated in sequence to the previously characterized S-layer proteins of Lactobacillus acidophilus group.
resultsIn this work, the self-assembly and cell wall binding domains of SlpA were characterized. The C-terminal self-assembly domain encompassed residues 179-435 of mature SlpA, as demonstrated by the ability of N-terminally truncated recombinant SlpA to form a periodic structure indistinguishable from that formed by full length SlpA. Furthermore, a trypsin degradation analysis indicated the existence of a protease resistant C-terminal domain of 214 amino acids. By producing a set of C-terminally truncated recombinant SlpA (rSlpA) proteins the cell wall binding region was mapped to the N-terminal part of SlpA, where the first 145 amino acids of mature SlpA alone were sufficient for binding to isolated cell wall fragments of L. brevis ATCC 8287. The binding of full length rSlpA to the cell walls was not affected by the treatment of the walls with 5% trichloroacetic acid (TCA), indicating that cell wall structures other than teichoic acids are involved, a feature not shared by the Lactobacillus acidophilus group S-layer proteins characterized so far. Conserved carbohydrate binding motifs were identified in the positively charged N-terminal regions of six Lactobacillus brevis S-layer proteins.
conclusionThis study identifies SlpA as a two-domain protein in which the order of the functional domains is reversed compared to other characterized Lactobacillus S-layer proteins, and emphasizes the diversity of potential cell wall receptors despite similar carbohydrate binding sequence motifs in Lactobacillus S-layer proteins.
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