Loading…

Protecting enzymatic function through directed packaging into bacterial outer membrane vesicles

Bacteria possess innate machinery to transport extracellular cargo between cells as well as package virulence factors to infect host cells by secreting outer membrane vesicles (OMVs) that contain small molecules, proteins and genetic material. These robust proteoliposomes have evolved naturally to b...

Full description

Saved in:

Bibliographic Details
Published in:	Scientific reports 2016-04, Vol.6 (1), p.24866-24866, Article 24866
Main Authors:	Alves, Nathan J., Turner, Kendrick B., Medintz, Igor L., Walper, Scott A.
Format:	Article
Language:	English
Subjects:	631/45/607 631/61/54/1754 82/80 Bacteria Bacteria - enzymology Bacteria - metabolism Bacterial vesicles Biodegradation E coli Environmental restoration Enzyme Stability Enzymes Extracellular Vesicles - enzymology Freeze Drying Freeze-thawing Genetic engineering Gram-positive bacteria Humanities and Social Sciences Laboratories Membrane vesicles multidisciplinary Nanoparticles Packaging Phosphoric Triester Hydrolases - metabolism Phosphoric Triester Hydrolases - secretion Phosphotriesterase Plasmids Proteins Proteolipids - metabolism Science Storage conditions Temperature Time Factors Virulence Virulence factors
Citations:	Items that this one cites Items that cite this one
Online Access:	Get full text
Tags:	Add Tag No Tags, Be the first to tag this record!

cited_by	cdi_FETCH-LOGICAL-c438t-d9124faac9e1a4a4ca32b79dbbae8b499edc63e51b14cee24652799cfedbc8af3
cites	cdi_FETCH-LOGICAL-c438t-d9124faac9e1a4a4ca32b79dbbae8b499edc63e51b14cee24652799cfedbc8af3
container_end_page	24866
container_issue	1
container_start_page	24866
container_title	Scientific reports
container_volume	6
creator	Alves, Nathan J. Turner, Kendrick B. Medintz, Igor L. Walper, Scott A.
description	Bacteria possess innate machinery to transport extracellular cargo between cells as well as package virulence factors to infect host cells by secreting outer membrane vesicles (OMVs) that contain small molecules, proteins and genetic material. These robust proteoliposomes have evolved naturally to be resistant to degradation and provide a supportive environment to extend the activity of encapsulated cargo. In this study, we sought to exploit bacterial OMV formation to package and maintain the activity of an enzyme, phosphotriesterase (PTE), under challenging storage conditions encountered for real world applications. Here we show that OMV packaged PTE maintains activity over free PTE when subjected to elevated temperatures (>100-fold more activity after 14 days at 37 °C), iterative freeze-thaw cycles (3.4-fold post four-cycles) and lyophilization (43-fold). We also demonstrate how lyophilized OMV packaged PTE can be utilized as a cell free reagent for long term environmental remediation of pesticide/chemical warfare contaminated areas.
doi_str_mv	10.1038/srep24866
format	article
fullrecord	<record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4846811</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1785215961</sourcerecordid><originalsourceid>FETCH-LOGICAL-c438t-d9124faac9e1a4a4ca32b79dbbae8b499edc63e51b14cee24652799cfedbc8af3</originalsourceid><addsrcrecordid>eNplkU1r3DAQhkVpaEKSQ_9AEfTSBja1ZNmWLoUS8gWB9JCcxUgee5Xa0kayA8mvr5ZNlk07lxlmHt6Z4SXkMytOWVHKHyniigtZ1x_IAS9EteAl5x936n1ynNJDkaPiSjD1iezzhrGmEeUB0b9jmNBOzvcU_cvzCJOztJt9bgVPp2UMc7-krYsZwpauwP6Bfk07PwVqIHejg4GGORd0xNFE8EifMDk7YDoiex0MCY9f8yG5vzi_O7ta3NxeXp_9ullYUcpp0SrGRQdgFTIQICyU3DSqNQZQGqEUtrYusWKGCYvIRV3xRinbYWushK48JD83uqvZjBlGP0UY9Cq6EeKzDuD0-4l3S92HJy2kqCVjWeDbq0AMjzOmSY8uWRyG_E2Yk2aNrDirVL1Gv_6DPoQ5-vyeZlLJumlqXmTq-4ayMaRsUrc9hhV67ZzeOpfZL7vXb8k3nzJwsgFSHvke487K_9T-Aj56pko</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1898677620</pqid></control><display><type>article</type><title>Protecting enzymatic function through directed packaging into bacterial outer membrane vesicles</title><source>PubMed (Medline)</source><source>Full-Text Journals in Chemistry (Open access)</source><source>Publicly Available Content (ProQuest)</source><source>Springer Nature - nature.com Journals - Fully Open Access</source><creator>Alves, Nathan J. ; Turner, Kendrick B. ; Medintz, Igor L. ; Walper, Scott A.</creator><creatorcontrib>Alves, Nathan J. ; Turner, Kendrick B. ; Medintz, Igor L. ; Walper, Scott A.</creatorcontrib><description>Bacteria possess innate machinery to transport extracellular cargo between cells as well as package virulence factors to infect host cells by secreting outer membrane vesicles (OMVs) that contain small molecules, proteins and genetic material. These robust proteoliposomes have evolved naturally to be resistant to degradation and provide a supportive environment to extend the activity of encapsulated cargo. In this study, we sought to exploit bacterial OMV formation to package and maintain the activity of an enzyme, phosphotriesterase (PTE), under challenging storage conditions encountered for real world applications. Here we show that OMV packaged PTE maintains activity over free PTE when subjected to elevated temperatures (>100-fold more activity after 14 days at 37 °C), iterative freeze-thaw cycles (3.4-fold post four-cycles) and lyophilization (43-fold). We also demonstrate how lyophilized OMV packaged PTE can be utilized as a cell free reagent for long term environmental remediation of pesticide/chemical warfare contaminated areas.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/srep24866</identifier><identifier>PMID: 27117743</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/45/607 ; 631/61/54/1754 ; 82/80 ; Bacteria ; Bacteria - enzymology ; Bacteria - metabolism ; Bacterial vesicles ; Biodegradation ; E coli ; Environmental restoration ; Enzyme Stability ; Enzymes ; Extracellular Vesicles - enzymology ; Freeze Drying ; Freeze-thawing ; Genetic engineering ; Gram-positive bacteria ; Humanities and Social Sciences ; Laboratories ; Membrane vesicles ; multidisciplinary ; Nanoparticles ; Packaging ; Phosphoric Triester Hydrolases - metabolism ; Phosphoric Triester Hydrolases - secretion ; Phosphotriesterase ; Plasmids ; Proteins ; Proteolipids - metabolism ; Science ; Storage conditions ; Temperature ; Time Factors ; Virulence ; Virulence factors</subject><ispartof>Scientific reports, 2016-04, Vol.6 (1), p.24866-24866, Article 24866</ispartof><rights>The Author(s) 2016</rights><rights>Copyright Nature Publishing Group Apr 2016</rights><rights>Copyright © 2016, Macmillan Publishers Limited 2016 Macmillan Publishers Limited</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c438t-d9124faac9e1a4a4ca32b79dbbae8b499edc63e51b14cee24652799cfedbc8af3</citedby><cites>FETCH-LOGICAL-c438t-d9124faac9e1a4a4ca32b79dbbae8b499edc63e51b14cee24652799cfedbc8af3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/1898677620/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/1898677620?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,25732,27903,27904,36991,36992,44569,53770,53772,74873</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27117743$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Alves, Nathan J.</creatorcontrib><creatorcontrib>Turner, Kendrick B.</creatorcontrib><creatorcontrib>Medintz, Igor L.</creatorcontrib><creatorcontrib>Walper, Scott A.</creatorcontrib><title>Protecting enzymatic function through directed packaging into bacterial outer membrane vesicles</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>Bacteria possess innate machinery to transport extracellular cargo between cells as well as package virulence factors to infect host cells by secreting outer membrane vesicles (OMVs) that contain small molecules, proteins and genetic material. These robust proteoliposomes have evolved naturally to be resistant to degradation and provide a supportive environment to extend the activity of encapsulated cargo. In this study, we sought to exploit bacterial OMV formation to package and maintain the activity of an enzyme, phosphotriesterase (PTE), under challenging storage conditions encountered for real world applications. Here we show that OMV packaged PTE maintains activity over free PTE when subjected to elevated temperatures (>100-fold more activity after 14 days at 37 °C), iterative freeze-thaw cycles (3.4-fold post four-cycles) and lyophilization (43-fold). We also demonstrate how lyophilized OMV packaged PTE can be utilized as a cell free reagent for long term environmental remediation of pesticide/chemical warfare contaminated areas.</description><subject>631/45/607</subject><subject>631/61/54/1754</subject><subject>82/80</subject><subject>Bacteria</subject><subject>Bacteria - enzymology</subject><subject>Bacteria - metabolism</subject><subject>Bacterial vesicles</subject><subject>Biodegradation</subject><subject>E coli</subject><subject>Environmental restoration</subject><subject>Enzyme Stability</subject><subject>Enzymes</subject><subject>Extracellular Vesicles - enzymology</subject><subject>Freeze Drying</subject><subject>Freeze-thawing</subject><subject>Genetic engineering</subject><subject>Gram-positive bacteria</subject><subject>Humanities and Social Sciences</subject><subject>Laboratories</subject><subject>Membrane vesicles</subject><subject>multidisciplinary</subject><subject>Nanoparticles</subject><subject>Packaging</subject><subject>Phosphoric Triester Hydrolases - metabolism</subject><subject>Phosphoric Triester Hydrolases - secretion</subject><subject>Phosphotriesterase</subject><subject>Plasmids</subject><subject>Proteins</subject><subject>Proteolipids - metabolism</subject><subject>Science</subject><subject>Storage conditions</subject><subject>Temperature</subject><subject>Time Factors</subject><subject>Virulence</subject><subject>Virulence factors</subject><issn>2045-2322</issn><issn>2045-2322</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><recordid>eNplkU1r3DAQhkVpaEKSQ_9AEfTSBja1ZNmWLoUS8gWB9JCcxUgee5Xa0kayA8mvr5ZNlk07lxlmHt6Z4SXkMytOWVHKHyniigtZ1x_IAS9EteAl5x936n1ynNJDkaPiSjD1iezzhrGmEeUB0b9jmNBOzvcU_cvzCJOztJt9bgVPp2UMc7-krYsZwpauwP6Bfk07PwVqIHejg4GGORd0xNFE8EifMDk7YDoiex0MCY9f8yG5vzi_O7ta3NxeXp_9ullYUcpp0SrGRQdgFTIQICyU3DSqNQZQGqEUtrYusWKGCYvIRV3xRinbYWushK48JD83uqvZjBlGP0UY9Cq6EeKzDuD0-4l3S92HJy2kqCVjWeDbq0AMjzOmSY8uWRyG_E2Yk2aNrDirVL1Gv_6DPoQ5-vyeZlLJumlqXmTq-4ayMaRsUrc9hhV67ZzeOpfZL7vXb8k3nzJwsgFSHvke487K_9T-Aj56pko</recordid><startdate>20160427</startdate><enddate>20160427</enddate><creator>Alves, Nathan J.</creator><creator>Turner, Kendrick B.</creator><creator>Medintz, Igor L.</creator><creator>Walper, Scott A.</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>C6C</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20160427</creationdate><title>Protecting enzymatic function through directed packaging into bacterial outer membrane vesicles</title><author>Alves, Nathan J. ; Turner, Kendrick B. ; Medintz, Igor L. ; Walper, Scott A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c438t-d9124faac9e1a4a4ca32b79dbbae8b499edc63e51b14cee24652799cfedbc8af3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>631/45/607</topic><topic>631/61/54/1754</topic><topic>82/80</topic><topic>Bacteria</topic><topic>Bacteria - enzymology</topic><topic>Bacteria - metabolism</topic><topic>Bacterial vesicles</topic><topic>Biodegradation</topic><topic>E coli</topic><topic>Environmental restoration</topic><topic>Enzyme Stability</topic><topic>Enzymes</topic><topic>Extracellular Vesicles - enzymology</topic><topic>Freeze Drying</topic><topic>Freeze-thawing</topic><topic>Genetic engineering</topic><topic>Gram-positive bacteria</topic><topic>Humanities and Social Sciences</topic><topic>Laboratories</topic><topic>Membrane vesicles</topic><topic>multidisciplinary</topic><topic>Nanoparticles</topic><topic>Packaging</topic><topic>Phosphoric Triester Hydrolases - metabolism</topic><topic>Phosphoric Triester Hydrolases - secretion</topic><topic>Phosphotriesterase</topic><topic>Plasmids</topic><topic>Proteins</topic><topic>Proteolipids - metabolism</topic><topic>Science</topic><topic>Storage conditions</topic><topic>Temperature</topic><topic>Time Factors</topic><topic>Virulence</topic><topic>Virulence factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Alves, Nathan J.</creatorcontrib><creatorcontrib>Turner, Kendrick B.</creatorcontrib><creatorcontrib>Medintz, Igor L.</creatorcontrib><creatorcontrib>Walper, Scott A.</creatorcontrib><collection>SpringerOpen</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>ProQuest Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>ProQuest Science Journals</collection><collection>ProQuest Biological Science Journals</collection><collection>Publicly Available Content (ProQuest)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Alves, Nathan J.</au><au>Turner, Kendrick B.</au><au>Medintz, Igor L.</au><au>Walper, Scott A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Protecting enzymatic function through directed packaging into bacterial outer membrane vesicles</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2016-04-27</date><risdate>2016</risdate><volume>6</volume><issue>1</issue><spage>24866</spage><epage>24866</epage><pages>24866-24866</pages><artnum>24866</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>Bacteria possess innate machinery to transport extracellular cargo between cells as well as package virulence factors to infect host cells by secreting outer membrane vesicles (OMVs) that contain small molecules, proteins and genetic material. These robust proteoliposomes have evolved naturally to be resistant to degradation and provide a supportive environment to extend the activity of encapsulated cargo. In this study, we sought to exploit bacterial OMV formation to package and maintain the activity of an enzyme, phosphotriesterase (PTE), under challenging storage conditions encountered for real world applications. Here we show that OMV packaged PTE maintains activity over free PTE when subjected to elevated temperatures (>100-fold more activity after 14 days at 37 °C), iterative freeze-thaw cycles (3.4-fold post four-cycles) and lyophilization (43-fold). We also demonstrate how lyophilized OMV packaged PTE can be utilized as a cell free reagent for long term environmental remediation of pesticide/chemical warfare contaminated areas.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>27117743</pmid><doi>10.1038/srep24866</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record>
fulltext	fulltext
identifier	ISSN: 2045-2322
ispartof	Scientific reports, 2016-04, Vol.6 (1), p.24866-24866, Article 24866
issn	2045-2322 2045-2322
language	eng
recordid	cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4846811
source	PubMed (Medline); Full-Text Journals in Chemistry (Open access); Publicly Available Content (ProQuest); Springer Nature - nature.com Journals - Fully Open Access
subjects	631/45/607 631/61/54/1754 82/80 Bacteria Bacteria - enzymology Bacteria - metabolism Bacterial vesicles Biodegradation E coli Environmental restoration Enzyme Stability Enzymes Extracellular Vesicles - enzymology Freeze Drying Freeze-thawing Genetic engineering Gram-positive bacteria Humanities and Social Sciences Laboratories Membrane vesicles multidisciplinary Nanoparticles Packaging Phosphoric Triester Hydrolases - metabolism Phosphoric Triester Hydrolases - secretion Phosphotriesterase Plasmids Proteins Proteolipids - metabolism Science Storage conditions Temperature Time Factors Virulence Virulence factors
title	Protecting enzymatic function through directed packaging into bacterial outer membrane vesicles
url	http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-22T19%3A56%3A53IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Protecting%20enzymatic%20function%20through%20directed%20packaging%20into%20bacterial%20outer%20membrane%20vesicles&rft.jtitle=Scientific%20reports&rft.au=Alves,%20Nathan%20J.&rft.date=2016-04-27&rft.volume=6&rft.issue=1&rft.spage=24866&rft.epage=24866&rft.pages=24866-24866&rft.artnum=24866&rft.issn=2045-2322&rft.eissn=2045-2322&rft_id=info:doi/10.1038/srep24866&rft_dat=%3Cproquest_pubme%3E1785215961%3C/proquest_pubme%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c438t-d9124faac9e1a4a4ca32b79dbbae8b499edc63e51b14cee24652799cfedbc8af3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=1898677620&rft_id=info:pmid/27117743&rfr_iscdi=true