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

Autores
Acosta, M.P.; Palomino, M.M.; Allievi, M.C.; Rivas, C.S.; Ruzal, S.M.
Año de publicación
2008
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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.
Fuente
Appl. Environ. Microbiol. 2008;74(24):7824-7827
Materia
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
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/2.5/ar
Repositorio
Biblioteca Digital (UBA-FCEN)
Institución
Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
OAI Identificador
paperaa:paper_00992240_v74_n24_p7824_Acosta
Acceder
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oai_identifier_str paperaa:paper_00992240_v74_n24_p7824_Acosta
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling Murein hydrolase activity in the surface layer of Lactobacillus acidophilus ATCC 4356Acosta, M.P.Palomino, M.M.Allievi, M.C.Rivas, C.S.Ruzal, S.M.BacilliBacteriologySalmonellaAmino acid sequenceC-terminal domainsCloning and expressionEnzymatic activitiesFunctional verificationHydrolase activitiesLactobacillus acidophilusSalmonella entericaHydrolasesbacterial enzymehydrolasepeptidoglycan hydrolaseunclassified drugamino acidbacteriumbioassayenzyme activityfunctional rolegene expressionamino acid sequencearticlecarboxy terminal sequenceenzyme activityenzyme analysisLactobacillus acidophilusnonhumannucleotide sequenceSalmonella entericaWestern blottingzymographyBacillus subtilisLactobacillus acidophilusSalmonella entericaWe 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.2008info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12110/paper_00992240_v74_n24_p7824_AcostaAppl. Environ. Microbiol. 2008;74(24):7824-7827reponame:Biblioteca Digital (UBA-FCEN)instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesinstacron:UBA-FCENenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/2.5/ar2025-09-04T09:48:44Zpaperaa:paper_00992240_v74_n24_p7824_AcostaInstitucionalhttps://digital.bl.fcen.uba.ar/Universidad públicaNo correspondehttps://digital.bl.fcen.uba.ar/cgi-bin/oaiserver.cgiana@bl.fcen.uba.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:18962025-09-04 09:48:46.163Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse
dc.title.none.fl_str_mv Murein hydrolase activity in the surface layer of Lactobacillus acidophilus ATCC 4356
title Murein hydrolase activity in the surface layer of Lactobacillus acidophilus ATCC 4356
spellingShingle Murein hydrolase activity in the surface layer of Lactobacillus acidophilus ATCC 4356
Acosta, M.P.
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
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
dc.creator.none.fl_str_mv Acosta, M.P.
Palomino, M.M.
Allievi, M.C.
Rivas, C.S.
Ruzal, S.M.
author Acosta, M.P.
author_facet Acosta, M.P.
Palomino, M.M.
Allievi, M.C.
Rivas, C.S.
Ruzal, S.M.
author_role author
author2 Palomino, M.M.
Allievi, M.C.
Rivas, C.S.
Ruzal, S.M.
author2_role author
author
author
author
dc.subject.none.fl_str_mv 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
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
dc.description.none.fl_txt_mv 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.
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.
publishDate 2008
dc.date.none.fl_str_mv 2008
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/20.500.12110/paper_00992240_v74_n24_p7824_Acosta
url http://hdl.handle.net/20.500.12110/paper_00992240_v74_n24_p7824_Acosta
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/2.5/ar
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/2.5/ar
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv Appl. Environ. Microbiol. 2008;74(24):7824-7827
reponame:Biblioteca Digital (UBA-FCEN)
instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron:UBA-FCEN
reponame_str Biblioteca Digital (UBA-FCEN)
collection Biblioteca Digital (UBA-FCEN)
instname_str Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron_str UBA-FCEN
institution UBA-FCEN
repository.name.fl_str_mv Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
repository.mail.fl_str_mv ana@bl.fcen.uba.ar
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score 12.623145

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