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One repeat of the cell wall binding domain is sufficient for anchoring the Lactobacillus acidophilus surface layer protein

Attachments

Author: Smit, E. · Pouwels, P.H.
Type:article
Date:2002
Source:Journal of Bacteriology, 16, 184, 4617-4619
Identifier: 236651
doi: doi:10.1128/JB.184.16.4617-4619.2002
Keywords: Health · Cell membrane protein · Sac1 protein · Unclassified drug · Vitronectin · Amino terminal sequence · Bacterial cell wall · Bacterial genetics · Bacterium adherence · Carboxy terminal sequence · Controlled study · Nonhuman · Protein domain · Bacterial Proteins · Cell Wall · Disinfectants · Lactobacillus acidophilus · Membrane Glycoproteins · Membrane Proteins · Phenol · Protein Binding · Protein Structure, Tertiary · Sonication · Actinobacteria (class) · Bacteria (microorganisms) · Lactobacillus · Lactobacillus acidophilus · Uncultured actinomycete

Abstract

The N-terminal repeat (SAC1) of the S-protein of Lactobacillus acidophilus bound efficiently and specifically to cell wall fragments (CWFs) when fused to green fluorescent protein, whereas the C-terminal repeat (SAC2) did not. Treatment of CWFs with hydrofluoric acid, but not phenol, prevented binding. Apparently, SAC1 is necessary and sufficient for cell wall binding. Our data suggest that SAC anchors the S-protein to a cell wall teichoic acid. Chemicals/CAS: Bacterial Proteins; Disinfectants; Membrane Glycoproteins; Membrane Proteins; Phenol, 108-95-2; surface array protein, bacteria