Bactericidal Permeability-Increasing Proteins Shape Host-Microbe Interactions

ABSTRACT We characterized bactericidal permeability-increasing proteins (BPIs) of the squid Euprymna scolopes, EsBPI2 and EsBPI4. They have molecular characteristics typical of other animal BPIs, are closely related to one another, and nest phylogenetically among invertebrate BPIs. Purified EsBPIs h...

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Autores principales:	Fangmin Chen, Benjamin C. Krasity, Suzanne M. Peyer, Sabrina Koehler, Edward G. Ruby, Xiaoping Zhang, Margaret J. McFall-Ngai
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2017
Materias:	Vibrio fischeri antimicrobial peptides bioinformatics confocal microscopy symbiosis Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/7f9a90c757f5480faf5413ca5730e6d4
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spelling	oai:doaj.org-article:7f9a90c757f5480faf5413ca5730e6d42021-11-15T15:50:59ZBactericidal Permeability-Increasing Proteins Shape Host-Microbe Interactions10.1128/mBio.00040-172150-7511https://doaj.org/article/7f9a90c757f5480faf5413ca5730e6d42017-05-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mBio.00040-17https://doaj.org/toc/2150-7511ABSTRACT We characterized bactericidal permeability-increasing proteins (BPIs) of the squid Euprymna scolopes, EsBPI2 and EsBPI4. They have molecular characteristics typical of other animal BPIs, are closely related to one another, and nest phylogenetically among invertebrate BPIs. Purified EsBPIs had antimicrobial activity against the squid’s symbiont, Vibrio fischeri, which colonizes light organ crypt epithelia. Activity of both proteins was abrogated by heat treatment and coincubation with specific antibodies. Pretreatment under acidic conditions similar to those during symbiosis initiation rendered V. fischeri more resistant to the antimicrobial activity of the proteins. Immunocytochemistry localized EsBPIs to the symbiotic organ and other epithelial surfaces interacting with ambient seawater. The proteins differed in intracellular distribution. Further, whereas EsBPI4 was restricted to epithelia, EsBPI2 also occurred in blood and in a transient juvenile organ that mediates hatching. The data provide evidence that these BPIs play different defensive roles early in the life of E. scolopes, modulating interactions with the symbiont. IMPORTANCE This study describes new functions for bactericidal permeability-increasing proteins (BPIs), members of the lipopolysaccharide-binding protein (LBP)/BPI protein family. The data provide evidence that these proteins play a dual role in the modulation of symbiotic bacteria. In the squid-vibrio model, these proteins both control the symbiont populations in the light organ tissues where symbiont cells occur in dense monoculture and, concomitantly, inhibit the symbiont from colonizing other epithelial surfaces of the animal.Fangmin ChenBenjamin C. KrasitySuzanne M. PeyerSabrina KoehlerEdward G. RubyXiaoping ZhangMargaret J. McFall-NgaiAmerican Society for MicrobiologyarticleVibrio fischeriantimicrobial peptidesbioinformaticsconfocal microscopysymbiosisMicrobiologyQR1-502ENmBio, Vol 8, Iss 2 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Vibrio fischeri antimicrobial peptides bioinformatics confocal microscopy symbiosis Microbiology QR1-502
spellingShingle	Vibrio fischeri antimicrobial peptides bioinformatics confocal microscopy symbiosis Microbiology QR1-502 Fangmin Chen Benjamin C. Krasity Suzanne M. Peyer Sabrina Koehler Edward G. Ruby Xiaoping Zhang Margaret J. McFall-Ngai Bactericidal Permeability-Increasing Proteins Shape Host-Microbe Interactions
description	ABSTRACT We characterized bactericidal permeability-increasing proteins (BPIs) of the squid Euprymna scolopes, EsBPI2 and EsBPI4. They have molecular characteristics typical of other animal BPIs, are closely related to one another, and nest phylogenetically among invertebrate BPIs. Purified EsBPIs had antimicrobial activity against the squid’s symbiont, Vibrio fischeri, which colonizes light organ crypt epithelia. Activity of both proteins was abrogated by heat treatment and coincubation with specific antibodies. Pretreatment under acidic conditions similar to those during symbiosis initiation rendered V. fischeri more resistant to the antimicrobial activity of the proteins. Immunocytochemistry localized EsBPIs to the symbiotic organ and other epithelial surfaces interacting with ambient seawater. The proteins differed in intracellular distribution. Further, whereas EsBPI4 was restricted to epithelia, EsBPI2 also occurred in blood and in a transient juvenile organ that mediates hatching. The data provide evidence that these BPIs play different defensive roles early in the life of E. scolopes, modulating interactions with the symbiont. IMPORTANCE This study describes new functions for bactericidal permeability-increasing proteins (BPIs), members of the lipopolysaccharide-binding protein (LBP)/BPI protein family. The data provide evidence that these proteins play a dual role in the modulation of symbiotic bacteria. In the squid-vibrio model, these proteins both control the symbiont populations in the light organ tissues where symbiont cells occur in dense monoculture and, concomitantly, inhibit the symbiont from colonizing other epithelial surfaces of the animal.
format	article
author	Fangmin Chen Benjamin C. Krasity Suzanne M. Peyer Sabrina Koehler Edward G. Ruby Xiaoping Zhang Margaret J. McFall-Ngai
author_facet	Fangmin Chen Benjamin C. Krasity Suzanne M. Peyer Sabrina Koehler Edward G. Ruby Xiaoping Zhang Margaret J. McFall-Ngai
author_sort	Fangmin Chen
title	Bactericidal Permeability-Increasing Proteins Shape Host-Microbe Interactions
title_short	Bactericidal Permeability-Increasing Proteins Shape Host-Microbe Interactions
title_full	Bactericidal Permeability-Increasing Proteins Shape Host-Microbe Interactions
title_fullStr	Bactericidal Permeability-Increasing Proteins Shape Host-Microbe Interactions
title_full_unstemmed	Bactericidal Permeability-Increasing Proteins Shape Host-Microbe Interactions
title_sort	bactericidal permeability-increasing proteins shape host-microbe interactions
publisher	American Society for Microbiology
publishDate	2017
url	https://doaj.org/article/7f9a90c757f5480faf5413ca5730e6d4
work_keys_str_mv	AT fangminchen bactericidalpermeabilityincreasingproteinsshapehostmicrobeinteractions AT benjaminckrasity bactericidalpermeabilityincreasingproteinsshapehostmicrobeinteractions AT suzannempeyer bactericidalpermeabilityincreasingproteinsshapehostmicrobeinteractions AT sabrinakoehler bactericidalpermeabilityincreasingproteinsshapehostmicrobeinteractions AT edwardgruby bactericidalpermeabilityincreasingproteinsshapehostmicrobeinteractions AT xiaopingzhang bactericidalpermeabilityincreasingproteinsshapehostmicrobeinteractions AT margaretjmcfallngai bactericidalpermeabilityincreasingproteinsshapehostmicrobeinteractions
_version_	1718427408289234944

Bactericidal Permeability-Increasing Proteins Shape Host-Microbe Interactions

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