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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todo:paper_19326203_v9_n10_p_Allievi2023-10-03T16:35:39Z Contribution of S-layer proteins to the mosquitocidal activity of Lysinibacillus sphaericus Allievi, M.C. Palomino, M.M. Acosta, M.P. Lanati, L. Ruzal, S.M. Sánchez-Rivas, C. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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, M.C. Palomino, M.M. Acosta, M.P. Lanati, L. Ruzal, S.M. Sánchez-Rivas, C. 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. |
format |
JOUR |
author |
Allievi, M.C. Palomino, M.M. Acosta, M.P. Lanati, L. Ruzal, S.M. Sánchez-Rivas, C. |
author_facet |
Allievi, M.C. Palomino, M.M. Acosta, M.P. Lanati, L. Ruzal, S.M. Sánchez-Rivas, C. |
author_sort |
Allievi, M.C. |
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 |
url |
http://hdl.handle.net/20.500.12110/paper_19326203_v9_n10_p_Allievi |
work_keys_str_mv |
AT allievimc contributionofslayerproteinstothemosquitocidalactivityoflysinibacillussphaericus AT palominomm contributionofslayerproteinstothemosquitocidalactivityoflysinibacillussphaericus AT acostamp contributionofslayerproteinstothemosquitocidalactivityoflysinibacillussphaericus AT lanatil contributionofslayerproteinstothemosquitocidalactivityoflysinibacillussphaericus AT ruzalsm contributionofslayerproteinstothemosquitocidalactivityoflysinibacillussphaericus AT sanchezrivasc contributionofslayerproteinstothemosquitocidalactivityoflysinibacillussphaericus |
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1782024083620233216 |