Characterization of the S-Layer Glycoproteins of Two Lactobacilli

Möschl, Alexander; Schäffer, Christina; Sleytr, Uwe B.; Messner, Paul; Christian, Rudolf; Schulz, Gerhard

doi:10.1007/978-1-4757-9032-0_27

Cited by 33 publications

(31 citation statements)

References 9 publications

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“…Lactobacillus buchneri 41021/251 [83] a the variable region of the 16S rDNA confirmed that the similarity values for the wild-type strain and the variant are 100 %. These findings indicated that despite evolutionary relationship, other factors such as growth conditions or environmental stress are determinative for sequence identities of structurally homologous domains of S layer proteins.…”

Section: Bacteriasupporting

confidence: 76%

Crystalline Bacterial Cell Surface Layers (S Layers): From Supramolecular Cell Structure to Biomimetics and Nanotechnology

Sleytr

Messner

Pum

et al. 1999

Angewandte Chemie Intl Edit

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412

258

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An astonishingly broad application potential in biotechnology, biomimetics, and nanotechnology is revealed by studies on the structure, chemistry, biosynthesis, genetics, self-assembly, and function of supramolecular surface layers (S layers). These are monomolecular, crystalline assemblies of protein or glycoprotein subunits and represent one of the most commonly observed surface structures of prokaryotic cell envelopes (see schematic representation of an archaebacterial cell envelope).

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Section: Bacteriasupporting

confidence: 76%

Crystalline Bacterial Cell Surface Layers (S Layers): From Supramolecular Cell Structure to Biomimetics and Nanotechnology

Sleytr

Messner

Pum

et al. 1999

Angewandte Chemie Intl Edit

Self Cite

412

258

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“…Although glycosylation is commonly found in S-layer proteins, most of S-layers from lactobacilli appear to be non-glycosylated (AvallJääskeläinen and Palva 2005), and to date a detailed glycan structure has been reported only for S-layer from Lactobacillus buchneri (Möschl et al 1993).…”

Section: Introductionmentioning

confidence: 98%

Heterogeneity of S-layer proteins from aggregating and non-aggregating Lactobacillus kefir strains

Mobili

Serradell

Trejo

et al. 2009

Antonie van Leeuwenhoek

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Since the presence of S-layer protein conditioned the autoaggregation capacity of some strains of Lactobacillus kefir, S-layer proteins from aggregating and non-aggregating L. kefir strains were characterized by immunochemical reactivity, MALDI-TOF spectrometry and glycosylation analysis. Two anti-S-layer monoclonal antibodies (Mab5F8 and Mab1F8) were produced; in an indirect enzyme-linked immunosorbent assay Mab1F8 recognized S-layer proteins from all L. kefir tested while Mab5F8 recognized only S-layer proteins from aggregating strains. Periodic Acid-Schiff staining of proteins after polyacrylamide gel electrophoresis under denaturing conditions revealed that all L. kefir S-layer proteins tested were glycosylated. Growth of bacteria in the presence of the N-glycosylation inhibitor tunicamycin suggested the presence of glycosydic chains O-linked to the protein backbone. MALDI-TOF peptide map fingerprint for S-layer proteins from 12 L. kefir strains showed very similar patterns for the aggregating strains, different from those for the non-aggregating ones. No positive match with other protein spectra in MSDB Database was found. Our results revealed a high heterogeneity among S-layer proteins from different L. kefir strains but also suggested a correlation between the structure of these S-layer glycoproteins and the aggregation properties of whole bacterial cells.

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“…In Grampositive pathogens, such as streptococci and staphylococci, several serine-rich fimbria-like adhesins undergo glycosylation (4,33,41). In lactobacilli, the only glycoproteins characterized to date are S-layer proteins, in addition to a peptide bacteriocin (27,29,44).…”

mentioning

confidence: 99%

The Major Autolysin Acm2 from Lactobacillus plantarum Undergoes Cytoplasmic O-Glycosylation

et al. 2012

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The major autolysin Acm2 from the probiotic strain Lactobacillus plantarum WCFS1 contains high proportions of alanine, serine, and threonine in its N-terminal so-called AST domain. It has been suggested that this extracellular protein might be glycosylated, but this has not been experimentally verified. We used high-resolution liquid chromatography-tandem mass spectrometry (LC-MS/MS) to study the possible occurrence of glycans on peptides generated from lactobacillary surface proteins by protease treatment. This approach yielded five glycopeptides in various glycoforms, all derived from the AST domain of Acm2. All five glycopeptides contained the hydroxy-amino acids serine and threonine, suggesting that Acm2 is O-glycosylated. By using lectin blotting with succinylated wheat germ agglutinin, and by comparing the wild-type strain with an Acm2-negative derivative (NZ3557), we found that the attached N-acetylhexosamines are most likely N-acetylglucosamines (GlcNAc). NZ3557 was further used as a genetic background to express an Acm2 variant lacking its secretion signal, resulting in intracellular expression of Acm2. We show that this intracellular version of Acm2 is also glycosylated, indicating that the GlcNAc modification is an intracellular process.

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Characterization of the S-Layer Glycoproteins of Two Lactobacilli

Cited by 33 publications

References 9 publications

Crystalline Bacterial Cell Surface Layers (S Layers): From Supramolecular Cell Structure to Biomimetics and Nanotechnology

Crystalline Bacterial Cell Surface Layers (S Layers): From Supramolecular Cell Structure to Biomimetics and Nanotechnology

Heterogeneity of S-layer proteins from aggregating and non-aggregating Lactobacillus kefir strains

The Major Autolysin Acm2 from Lactobacillus plantarum Undergoes Cytoplasmic O-Glycosylation

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