Exploring lectin-like activity of the S-layer protein of Lactobacillus acidophilus ATCC 4356

The surface layer (S-layer) protein of Lactobacillus acidophilus is a crystalline array of self-assembling, proteinaceous subunits non-covalently bound to the outmost bacterial cell wall envelope and is involved in the adherence of bacteria to host cells. We have previously described that the S-laye...

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Veröffentlicht in:Applied microbiology and biotechnology 2019-06, Vol.103 (12), p.4839-4857
Hauptverfasser: Fina Martin, Joaquina, Palomino, Maria Mercedes, Cutine, Anabella M., Modenutti, Carlos P., Fernández Do Porto, Dario A., Allievi, Mariana C., Zanini, Sofia H., Mariño, Karina V., Barquero, Andrea A., Ruzal, Sandra M.
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container_end_page 4857
container_issue 12
container_start_page 4839
container_title Applied microbiology and biotechnology
container_volume 103
creator Fina Martin, Joaquina
Palomino, Maria Mercedes
Cutine, Anabella M.
Modenutti, Carlos P.
Fernández Do Porto, Dario A.
Allievi, Mariana C.
Zanini, Sofia H.
Mariño, Karina V.
Barquero, Andrea A.
Ruzal, Sandra M.
description The surface layer (S-layer) protein of Lactobacillus acidophilus is a crystalline array of self-assembling, proteinaceous subunits non-covalently bound to the outmost bacterial cell wall envelope and is involved in the adherence of bacteria to host cells. We have previously described that the S-layer protein of L. acidophilus possesses anti-viral and anti-bacterial properties. In this work, we extracted and purified S-layer proteins from L. acidophilus ATCC 4356 cells to study their interaction with cell wall components from prokaryotic (i.e., peptidoglycan and lipoteichoic acids) and eukaryotic origin (i.e., mucin and chitin), as well as with viruses, bacteria, yeast, and blood cells. Using chimeric S-layer fused to green fluorescent protein (GFP) from different parts of the protein, we analyzed their binding capacity. Our results show that the C-terminal part of the S-layer protein presents lectin-like activity, interacting with different glycoepitopes. We further demonstrate that lipoteichoic acid (LTA) serves as an anchor for the S-layer protein. Finally, a structure for the C-terminal part of S-layer and possible binding sites were predicted by a homology-based model.
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subjects Antiviral agents
Bacteria
Bacterial Adhesion
Bacterial proteins
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Binding Sites
Biomedical and Life Sciences
Biotechnologically Relevant Enzymes and Proteins
Biotechnology
Blood cells
Cell walls
Chitin
Fluorescence
Green fluorescent protein
Green Fluorescent Proteins - genetics
Homology
Lactobacillus acidophilus
Lactobacillus acidophilus - metabolism
Lectins - metabolism
Life Sciences
Lipoteichoic acid
Membrane Glycoproteins - isolation & purification
Membrane Glycoproteins - metabolism
Microbial Genetics and Genomics
Microbiology
Mucin
Peptidoglycans
Physiological aspects
Protein Binding
Protein structure
Proteins
Surface layers
Yeast
Yeasts
Yogurt
title Exploring lectin-like activity of the S-layer protein of Lactobacillus acidophilus ATCC 4356
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