Maize root lectins mediate the interaction with Herbaspirillum seropedicae via N-acetyl glucosamine residues of lipopolysaccharides.

Herbaspirillum seropedicae is a plant growth-promoting diazotrophic betaproteobacterium which associates with important crops, such as maize, wheat, rice and sugar-cane. We have previously reported that intact lipopolysaccharide (LPS) is required for H. seropedicae attachment and endophytic coloniza...

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Autores principales:	Eduardo Balsanelli, Thalita Regina Tuleski, Valter Antonio de Baura, Marshall Geoffrey Yates, Leda Satie Chubatsu, Fabio de Oliveira Pedrosa, Emanuel Maltempi de Souza, Rose Adele Monteiro
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/e0cb826084d74910b9ead8c31b8a38d7
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spelling	oai:doaj.org-article:e0cb826084d74910b9ead8c31b8a38d72021-11-18T08:51:45ZMaize root lectins mediate the interaction with Herbaspirillum seropedicae via N-acetyl glucosamine residues of lipopolysaccharides.1932-620310.1371/journal.pone.0077001https://doaj.org/article/e0cb826084d74910b9ead8c31b8a38d72013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24130823/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Herbaspirillum seropedicae is a plant growth-promoting diazotrophic betaproteobacterium which associates with important crops, such as maize, wheat, rice and sugar-cane. We have previously reported that intact lipopolysaccharide (LPS) is required for H. seropedicae attachment and endophytic colonization of maize roots. In this study, we present evidence that the LPS biosynthesis gene waaL (codes for the O-antigen ligase) is induced during rhizosphere colonization by H. seropedicae. Furthermore a waaL mutant strain lacking the O-antigen portion of the LPS is severely impaired in colonization. Since N-acetyl glucosamine inhibits H. seropedicae attachment to maize roots, lectin-like proteins from maize roots (MRLs) were isolated and mass spectrometry (MS) analysis showed that MRL-1 and MRL-2 correspond to maize proteins with a jacalin-like lectin domain, while MRL-3 contains a B-chain lectin domain. These proteins showed agglutination activity against wild type H. seropedicae, but failed to agglutinate the waaL mutant strain. The agglutination reaction was severely diminished in the presence of N-acetyl glucosamine. Moreover addition of the MRL proteins as competitors in H. seropedicae attachment assays decreased 80-fold the adhesion of the wild type to maize roots. The results suggest that N-acetyl glucosamine residues of the LPS O-antigen bind to maize root lectins, an essential step for efficient bacterial attachment and colonization.Eduardo BalsanelliThalita Regina TuleskiValter Antonio de BauraMarshall Geoffrey YatesLeda Satie ChubatsuFabio de Oliveira PedrosaEmanuel Maltempi de SouzaRose Adele MonteiroPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 10, p e77001 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Eduardo Balsanelli Thalita Regina Tuleski Valter Antonio de Baura Marshall Geoffrey Yates Leda Satie Chubatsu Fabio de Oliveira Pedrosa Emanuel Maltempi de Souza Rose Adele Monteiro Maize root lectins mediate the interaction with Herbaspirillum seropedicae via N-acetyl glucosamine residues of lipopolysaccharides.
description	Herbaspirillum seropedicae is a plant growth-promoting diazotrophic betaproteobacterium which associates with important crops, such as maize, wheat, rice and sugar-cane. We have previously reported that intact lipopolysaccharide (LPS) is required for H. seropedicae attachment and endophytic colonization of maize roots. In this study, we present evidence that the LPS biosynthesis gene waaL (codes for the O-antigen ligase) is induced during rhizosphere colonization by H. seropedicae. Furthermore a waaL mutant strain lacking the O-antigen portion of the LPS is severely impaired in colonization. Since N-acetyl glucosamine inhibits H. seropedicae attachment to maize roots, lectin-like proteins from maize roots (MRLs) were isolated and mass spectrometry (MS) analysis showed that MRL-1 and MRL-2 correspond to maize proteins with a jacalin-like lectin domain, while MRL-3 contains a B-chain lectin domain. These proteins showed agglutination activity against wild type H. seropedicae, but failed to agglutinate the waaL mutant strain. The agglutination reaction was severely diminished in the presence of N-acetyl glucosamine. Moreover addition of the MRL proteins as competitors in H. seropedicae attachment assays decreased 80-fold the adhesion of the wild type to maize roots. The results suggest that N-acetyl glucosamine residues of the LPS O-antigen bind to maize root lectins, an essential step for efficient bacterial attachment and colonization.
format	article
author	Eduardo Balsanelli Thalita Regina Tuleski Valter Antonio de Baura Marshall Geoffrey Yates Leda Satie Chubatsu Fabio de Oliveira Pedrosa Emanuel Maltempi de Souza Rose Adele Monteiro
author_facet	Eduardo Balsanelli Thalita Regina Tuleski Valter Antonio de Baura Marshall Geoffrey Yates Leda Satie Chubatsu Fabio de Oliveira Pedrosa Emanuel Maltempi de Souza Rose Adele Monteiro
author_sort	Eduardo Balsanelli
title	Maize root lectins mediate the interaction with Herbaspirillum seropedicae via N-acetyl glucosamine residues of lipopolysaccharides.
title_short	Maize root lectins mediate the interaction with Herbaspirillum seropedicae via N-acetyl glucosamine residues of lipopolysaccharides.
title_full	Maize root lectins mediate the interaction with Herbaspirillum seropedicae via N-acetyl glucosamine residues of lipopolysaccharides.
title_fullStr	Maize root lectins mediate the interaction with Herbaspirillum seropedicae via N-acetyl glucosamine residues of lipopolysaccharides.
title_full_unstemmed	Maize root lectins mediate the interaction with Herbaspirillum seropedicae via N-acetyl glucosamine residues of lipopolysaccharides.
title_sort	maize root lectins mediate the interaction with herbaspirillum seropedicae via n-acetyl glucosamine residues of lipopolysaccharides.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/e0cb826084d74910b9ead8c31b8a38d7
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Maize root lectins mediate the interaction with Herbaspirillum seropedicae via N-acetyl glucosamine residues of lipopolysaccharides.

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