Murein hydrolase activity in the surface layer of Lactobacillus acidophilus ATCC 4356

We describe a new enzymatic functionality for the surface layer (S-layer) of Lactobacillus acidophilus ATCC 4356, namely, an endopeptidase activity against the cell wall of Salmonella enterica serovar Newport, assayed via zymograms and identified by Western blotting. Based on amino acid sequence com...

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Autores principales: Acosta, M.P., Palomino, M.M., Allievi, M.C., Rivas, C.S., Ruzal, S.M.
Formato: JOUR
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Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00992240_v74_n24_p7824_Acosta
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spelling todo:paper_00992240_v74_n24_p7824_Acosta2023-10-03T14:57:08Z Murein hydrolase activity in the surface layer of Lactobacillus acidophilus ATCC 4356 Acosta, M.P. Palomino, M.M. Allievi, M.C. Rivas, C.S. Ruzal, S.M. Bacilli Bacteriology Salmonella Amino acid sequence C-terminal domains Cloning and expression Enzymatic activities Functional verification Hydrolase activities Lactobacillus acidophilus Salmonella enterica Hydrolases bacterial enzyme hydrolase peptidoglycan hydrolase unclassified drug amino acid bacterium bioassay enzyme activity functional role gene expression amino acid sequence article carboxy terminal sequence enzyme activity enzyme analysis Lactobacillus acidophilus nonhuman nucleotide sequence Salmonella enterica Western blotting zymography Bacillus subtilis Lactobacillus acidophilus Salmonella enterica We describe a new enzymatic functionality for the surface layer (S-layer) of Lactobacillus acidophilus ATCC 4356, namely, an endopeptidase activity against the cell wall of Salmonella enterica serovar Newport, assayed via zymograms and identified by Western blotting. Based on amino acid sequence comparisons, the hydrolase activity was predicted to be located at the C terminus. Subsequent cloning and expression of the C-terminal domain in Bacillus subtilis resulted in the functional verification of the enzymatic activity. Copyright © 2008, American Society for Microbiology. All Rights Reserved. Fil:Acosta, M.P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Palomino, M.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Allievi, M.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Ruzal, S.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00992240_v74_n24_p7824_Acosta
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Bacilli
Bacteriology
Salmonella
Amino acid sequence
C-terminal domains
Cloning and expression
Enzymatic activities
Functional verification
Hydrolase activities
Lactobacillus acidophilus
Salmonella enterica
Hydrolases
bacterial enzyme
hydrolase
peptidoglycan hydrolase
unclassified drug
amino acid
bacterium
bioassay
enzyme activity
functional role
gene expression
amino acid sequence
article
carboxy terminal sequence
enzyme activity
enzyme analysis
Lactobacillus acidophilus
nonhuman
nucleotide sequence
Salmonella enterica
Western blotting
zymography
Bacillus subtilis
Lactobacillus acidophilus
Salmonella enterica
spellingShingle Bacilli
Bacteriology
Salmonella
Amino acid sequence
C-terminal domains
Cloning and expression
Enzymatic activities
Functional verification
Hydrolase activities
Lactobacillus acidophilus
Salmonella enterica
Hydrolases
bacterial enzyme
hydrolase
peptidoglycan hydrolase
unclassified drug
amino acid
bacterium
bioassay
enzyme activity
functional role
gene expression
amino acid sequence
article
carboxy terminal sequence
enzyme activity
enzyme analysis
Lactobacillus acidophilus
nonhuman
nucleotide sequence
Salmonella enterica
Western blotting
zymography
Bacillus subtilis
Lactobacillus acidophilus
Salmonella enterica
Acosta, M.P.
Palomino, M.M.
Allievi, M.C.
Rivas, C.S.
Ruzal, S.M.
Murein hydrolase activity in the surface layer of Lactobacillus acidophilus ATCC 4356
topic_facet Bacilli
Bacteriology
Salmonella
Amino acid sequence
C-terminal domains
Cloning and expression
Enzymatic activities
Functional verification
Hydrolase activities
Lactobacillus acidophilus
Salmonella enterica
Hydrolases
bacterial enzyme
hydrolase
peptidoglycan hydrolase
unclassified drug
amino acid
bacterium
bioassay
enzyme activity
functional role
gene expression
amino acid sequence
article
carboxy terminal sequence
enzyme activity
enzyme analysis
Lactobacillus acidophilus
nonhuman
nucleotide sequence
Salmonella enterica
Western blotting
zymography
Bacillus subtilis
Lactobacillus acidophilus
Salmonella enterica
description We describe a new enzymatic functionality for the surface layer (S-layer) of Lactobacillus acidophilus ATCC 4356, namely, an endopeptidase activity against the cell wall of Salmonella enterica serovar Newport, assayed via zymograms and identified by Western blotting. Based on amino acid sequence comparisons, the hydrolase activity was predicted to be located at the C terminus. Subsequent cloning and expression of the C-terminal domain in Bacillus subtilis resulted in the functional verification of the enzymatic activity. Copyright © 2008, American Society for Microbiology. All Rights Reserved.
format JOUR
author Acosta, M.P.
Palomino, M.M.
Allievi, M.C.
Rivas, C.S.
Ruzal, S.M.
author_facet Acosta, M.P.
Palomino, M.M.
Allievi, M.C.
Rivas, C.S.
Ruzal, S.M.
author_sort Acosta, M.P.
title Murein hydrolase activity in the surface layer of Lactobacillus acidophilus ATCC 4356
title_short Murein hydrolase activity in the surface layer of Lactobacillus acidophilus ATCC 4356
title_full Murein hydrolase activity in the surface layer of Lactobacillus acidophilus ATCC 4356
title_fullStr Murein hydrolase activity in the surface layer of Lactobacillus acidophilus ATCC 4356
title_full_unstemmed Murein hydrolase activity in the surface layer of Lactobacillus acidophilus ATCC 4356
title_sort murein hydrolase activity in the surface layer of lactobacillus acidophilus atcc 4356
url http://hdl.handle.net/20.500.12110/paper_00992240_v74_n24_p7824_Acosta
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AT palominomm mureinhydrolaseactivityinthesurfacelayeroflactobacillusacidophilusatcc4356
AT allievimc mureinhydrolaseactivityinthesurfacelayeroflactobacillusacidophilusatcc4356
AT rivascs mureinhydrolaseactivityinthesurfacelayeroflactobacillusacidophilusatcc4356
AT ruzalsm mureinhydrolaseactivityinthesurfacelayeroflactobacillusacidophilusatcc4356
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