Contribution of S-layer proteins to the mosquitocidal activity of Lysinibacillus sphaericus

Lysinibacillus sphaericus strains belonging the antigenic group H5a5b produce spores with larvicidal activity against larvae of Culex mosquitoes. C7, a new isolated strain, which presents similar biochemical characteristics and Bin toxins in their spores as the reference strain 2362, was, however, m...

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Autores principales:	Allievi, Mariana Claudia, Palomino, María Mercedes, Ruzal, Sandra Mónica
Publicado:	2014
Materias:	bacterial toxin bacterial toxin BinA bacterial toxin BinB chitin envelope protein polymer protein S layer unclassified drug membrane protein protein binding S-layer proteins Aedes aegypti arthropod life cycle stage Article bacterial spore bacterial strain bacterium culture computer model controlled study crystal structure Culex entomopathogenic bacterium hemolysis immunofluorescence test insecticidal activity larval stage Lysinibacillus sphaericus molecular weight mosquitocidal activity nonhuman pathogenicity polyacrylamide gel electrophoresis protein carbohydrate interaction protein determination protein domain protein expression protein function protein localization protein processing sporogenesis toxicity testing toxin analysis Western blotting Aedes amino acid sequence animal Bacillaceae chemistry drug effects metabolism molecular genetics protein multimerization Amino Acid Sequence Animals Chitin Membrane Glycoproteins Molecular Sequence Data Protein Binding Protein Multimerization Spores, Bacterial
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_19326203_v9_n10_p_Allievi http://hdl.handle.net/20.500.12110/paper_19326203_v9_n10_p_Allievi
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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spelling	paper:paper_19326203_v9_n10_p_Allievi2023-06-08T16:31:20Z Contribution of S-layer proteins to the mosquitocidal activity of Lysinibacillus sphaericus Allievi, Mariana Claudia Palomino, María Mercedes Ruzal, Sandra Mónica bacterial toxin bacterial toxin BinA bacterial toxin BinB chitin envelope protein polymer protein S layer unclassified drug membrane protein protein binding S-layer proteins Aedes aegypti arthropod life cycle stage Article bacterial spore bacterial strain bacterium culture computer model controlled study crystal structure Culex entomopathogenic bacterium hemolysis immunofluorescence test insecticidal activity larval stage Lysinibacillus sphaericus molecular weight mosquitocidal activity nonhuman pathogenicity polyacrylamide gel electrophoresis protein carbohydrate interaction protein determination protein domain protein expression protein function protein localization protein processing sporogenesis toxicity testing toxin analysis Western blotting Aedes amino acid sequence animal Bacillaceae chemistry Culex drug effects metabolism molecular genetics protein multimerization Aedes Amino Acid Sequence Animals Bacillaceae Chitin Culex Membrane Glycoproteins Molecular Sequence Data Protein Binding Protein Multimerization Spores, Bacterial Lysinibacillus sphaericus strains belonging the antigenic group H5a5b produce spores with larvicidal activity against larvae of Culex mosquitoes. C7, a new isolated strain, which presents similar biochemical characteristics and Bin toxins in their spores as the reference strain 2362, was, however, more active against larvae of Culex mosquitoes. The contribution of the surface layer protein (S-layer) to this behaviour was envisaged since this envelope protein has been implicated in the pathogenicity of several bacilli, and we had previously reported its association to spores. Microscopic observation by immunofluorescence detection with anti S-layer antibody in the spores confirms their attachment. S-layers and BinA and BinB toxins formed high molecular weight multimers in spores as shown by SDS-PAGE and western blot detection. Purified S-layer from both L. sphaericus C7 and 2362 strain cultures was by itself toxic against Culex sp larvae, however, that from C7 strain was also toxic against Aedes aegypti. Synergistic effect between purified S-layer and spore-crystal preparations was observed against Culex sp. and Aedes aegypti larvae. This effect was more evident with the C7 strain. In silico analyses of the S-layer sequence suggest the presence of chitin-binding and hemolytic domains. Both biochemical characteristics were detected for both Slayers strains that must justify their contribution to pathogenicity. Copyright: © 2014 Varanda et al. Fil:Allievi, M.C. 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:Ruzal, S.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2014 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_19326203_v9_n10_p_Allievi http://hdl.handle.net/20.500.12110/paper_19326203_v9_n10_p_Allievi
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	bacterial toxin bacterial toxin BinA bacterial toxin BinB chitin envelope protein polymer protein S layer unclassified drug membrane protein protein binding S-layer proteins Aedes aegypti arthropod life cycle stage Article bacterial spore bacterial strain bacterium culture computer model controlled study crystal structure Culex entomopathogenic bacterium hemolysis immunofluorescence test insecticidal activity larval stage Lysinibacillus sphaericus molecular weight mosquitocidal activity nonhuman pathogenicity polyacrylamide gel electrophoresis protein carbohydrate interaction protein determination protein domain protein expression protein function protein localization protein processing sporogenesis toxicity testing toxin analysis Western blotting Aedes amino acid sequence animal Bacillaceae chemistry Culex drug effects metabolism molecular genetics protein multimerization Aedes Amino Acid Sequence Animals Bacillaceae Chitin Culex Membrane Glycoproteins Molecular Sequence Data Protein Binding Protein Multimerization Spores, Bacterial
spellingShingle	bacterial toxin bacterial toxin BinA bacterial toxin BinB chitin envelope protein polymer protein S layer unclassified drug membrane protein protein binding S-layer proteins Aedes aegypti arthropod life cycle stage Article bacterial spore bacterial strain bacterium culture computer model controlled study crystal structure Culex entomopathogenic bacterium hemolysis immunofluorescence test insecticidal activity larval stage Lysinibacillus sphaericus molecular weight mosquitocidal activity nonhuman pathogenicity polyacrylamide gel electrophoresis protein carbohydrate interaction protein determination protein domain protein expression protein function protein localization protein processing sporogenesis toxicity testing toxin analysis Western blotting Aedes amino acid sequence animal Bacillaceae chemistry Culex drug effects metabolism molecular genetics protein multimerization Aedes Amino Acid Sequence Animals Bacillaceae Chitin Culex Membrane Glycoproteins Molecular Sequence Data Protein Binding Protein Multimerization Spores, Bacterial Allievi, Mariana Claudia Palomino, María Mercedes Ruzal, Sandra Mónica Contribution of S-layer proteins to the mosquitocidal activity of Lysinibacillus sphaericus
topic_facet	bacterial toxin bacterial toxin BinA bacterial toxin BinB chitin envelope protein polymer protein S layer unclassified drug membrane protein protein binding S-layer proteins Aedes aegypti arthropod life cycle stage Article bacterial spore bacterial strain bacterium culture computer model controlled study crystal structure Culex entomopathogenic bacterium hemolysis immunofluorescence test insecticidal activity larval stage Lysinibacillus sphaericus molecular weight mosquitocidal activity nonhuman pathogenicity polyacrylamide gel electrophoresis protein carbohydrate interaction protein determination protein domain protein expression protein function protein localization protein processing sporogenesis toxicity testing toxin analysis Western blotting Aedes amino acid sequence animal Bacillaceae chemistry Culex drug effects metabolism molecular genetics protein multimerization Aedes Amino Acid Sequence Animals Bacillaceae Chitin Culex Membrane Glycoproteins Molecular Sequence Data Protein Binding Protein Multimerization Spores, Bacterial
description	Lysinibacillus sphaericus strains belonging the antigenic group H5a5b produce spores with larvicidal activity against larvae of Culex mosquitoes. C7, a new isolated strain, which presents similar biochemical characteristics and Bin toxins in their spores as the reference strain 2362, was, however, more active against larvae of Culex mosquitoes. The contribution of the surface layer protein (S-layer) to this behaviour was envisaged since this envelope protein has been implicated in the pathogenicity of several bacilli, and we had previously reported its association to spores. Microscopic observation by immunofluorescence detection with anti S-layer antibody in the spores confirms their attachment. S-layers and BinA and BinB toxins formed high molecular weight multimers in spores as shown by SDS-PAGE and western blot detection. Purified S-layer from both L. sphaericus C7 and 2362 strain cultures was by itself toxic against Culex sp larvae, however, that from C7 strain was also toxic against Aedes aegypti. Synergistic effect between purified S-layer and spore-crystal preparations was observed against Culex sp. and Aedes aegypti larvae. This effect was more evident with the C7 strain. In silico analyses of the S-layer sequence suggest the presence of chitin-binding and hemolytic domains. Both biochemical characteristics were detected for both Slayers strains that must justify their contribution to pathogenicity. Copyright: © 2014 Varanda et al.
author	Allievi, Mariana Claudia Palomino, María Mercedes Ruzal, Sandra Mónica
author_facet	Allievi, Mariana Claudia Palomino, María Mercedes Ruzal, Sandra Mónica
author_sort	Allievi, Mariana Claudia
title	Contribution of S-layer proteins to the mosquitocidal activity of Lysinibacillus sphaericus
title_short	Contribution of S-layer proteins to the mosquitocidal activity of Lysinibacillus sphaericus
title_full	Contribution of S-layer proteins to the mosquitocidal activity of Lysinibacillus sphaericus
title_fullStr	Contribution of S-layer proteins to the mosquitocidal activity of Lysinibacillus sphaericus
title_full_unstemmed	Contribution of S-layer proteins to the mosquitocidal activity of Lysinibacillus sphaericus
title_sort	contribution of s-layer proteins to the mosquitocidal activity of lysinibacillus sphaericus
publishDate	2014
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_19326203_v9_n10_p_Allievi http://hdl.handle.net/20.500.12110/paper_19326203_v9_n10_p_Allievi
work_keys_str_mv	AT allievimarianaclaudia contributionofslayerproteinstothemosquitocidalactivityoflysinibacillussphaericus AT palominomariamercedes contributionofslayerproteinstothemosquitocidalactivityoflysinibacillussphaericus AT ruzalsandramonica contributionofslayerproteinstothemosquitocidalactivityoflysinibacillussphaericus
_version_	1768542860659916800

Contribution of S-layer proteins to the mosquitocidal activity of Lysinibacillus sphaericus

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