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: Mariana Claudia Allievi, María Mercedes Palomino, Mariano Prado Acosta, Leonardo Lanati, Sandra Mónica Ruzal, Carmen Sánchez-Rivas
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Publicado: Public Library of Science (PLoS) 2014
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spelling oai:doaj.org-article:bacdbfd127814a098f8f69183e5274892021-11-25T05:55:07ZContribution of S-layer proteins to the mosquitocidal activity of Lysinibacillus sphaericus.1932-620310.1371/journal.pone.0111114https://doaj.org/article/bacdbfd127814a098f8f69183e5274892014-01-01T00:00:00Zhttps://doi.org/10.1371/journal.pone.0111114https://doaj.org/toc/1932-6203Lysinibacillus 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 S-layers strains that must justify their contribution to pathogenicity.Mariana Claudia AllieviMaría Mercedes PalominoMariano Prado AcostaLeonardo LanatiSandra Mónica RuzalCarmen Sánchez-RivasPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 10, p e111114 (2014)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Mariana Claudia Allievi
María Mercedes Palomino
Mariano Prado Acosta
Leonardo Lanati
Sandra Mónica Ruzal
Carmen Sánchez-Rivas
Contribution of S-layer proteins to the mosquitocidal activity of Lysinibacillus sphaericus.
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 S-layers strains that must justify their contribution to pathogenicity.
format article
author Mariana Claudia Allievi
María Mercedes Palomino
Mariano Prado Acosta
Leonardo Lanati
Sandra Mónica Ruzal
Carmen Sánchez-Rivas
author_facet Mariana Claudia Allievi
María Mercedes Palomino
Mariano Prado Acosta
Leonardo Lanati
Sandra Mónica Ruzal
Carmen Sánchez-Rivas
author_sort Mariana Claudia Allievi
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.
publisher Public Library of Science (PLoS)
publishDate 2014
url https://doaj.org/article/bacdbfd127814a098f8f69183e527489
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