Photocatalytic Protein Damage by Silver Nanoparticles Circumvents Bacterial Stress Response and Multidrug Resistance.
Identifieur interne : 000271 ( Main/Corpus ); précédent : 000270; suivant : 000272Photocatalytic Protein Damage by Silver Nanoparticles Circumvents Bacterial Stress Response and Multidrug Resistance.
Auteurs : Tianyuan Shi ; Qiuxia Wei ; Zhen Wang ; Gong Zhang ; Xuesong Sun ; Qing-Yu HeSource :
- mSphere [ 2379-5042 ] ; 2019.
English descriptors
- KwdEn :
- Anti-Bacterial Agents (pharmacology), Catalysis (MeSH), Drug Resistance, Multiple, Bacterial (radiation effects), Escherichia coli (drug effects), Escherichia coli (radiation effects), Light (MeSH), Metal Nanoparticles (chemistry), Microbial Sensitivity Tests (MeSH), Oxidative Stress (MeSH), Protein Aggregates (MeSH), Silver (chemistry), Silver (pharmacology).
- MESH :
- chemical , chemistry : Silver.
- chemical , pharmacology : Anti-Bacterial Agents, Silver.
- chemistry : Metal Nanoparticles.
- drug effects : Escherichia coli.
- radiation effects : Drug Resistance, Multiple, Bacterial, Escherichia coli.
- Catalysis, Light, Microbial Sensitivity Tests, Oxidative Stress, Protein Aggregates.
Abstract
Silver nanoparticles (AgNPs) are known for their broad-spectrum antibacterial properties, especially against antibiotic-resistant bacteria. However, the bactericidal mechanism of AgNPs remains unclear. In this study, we found that the bactericidal ability of AgNPs is induced by light. In contrast to previous postulates, visible light is unable to trigger silver ion release from AgNPs or to promote AgNPs to induce reactive oxygen species (ROS) in Escherichia coli In fact, we revealed that light excited AgNPs to induce protein aggregation in a concentration-dependent manner in E. coli, indicating that the bactericidal ability of AgNPs relies on the light-catalyzed oxidation of cellular proteins via direct binding to proteins, which was verified by fluorescence spectra. AgNPs likely absorb the light energy and transfer it to the proteins, leading to the oxidation of proteins and thus promoting the death of the bacteria. Isobaric tags for relative and absolute quantitation (iTRAQ)-based proteomics revealed that the bacteria failed to develop effective resistance to the light-excited AgNPs. This direct physical mechanism is unlikely to be counteracted by any known drug resistance mechanisms of bacteria and therefore may serve as a last resort against drug resistance. This mechanism also provides a practical hint regarding the antimicrobial application of AgNPs-light exposure improves the efficacy of AgNPs.IMPORTANCE Although silver nanoparticles (AgNPs) are well known for their antibacterial properties, the mechanism by which they kill bacterial cells remains a topic of debate. In this study, we uncovered the bactericidal mechanism of AgNPs, which is induced by light. We tested the efficacy of AgNPs against a panel of antimicrobial-resistant pathogens as well as Escherichia coli under conditions of light and darkness and revealed that light excited the AgNPs to promote protein aggregation within the bacterial cells. Our report makes a significant contribution to the literature because this mechanism bypasses microbial drug resistance mechanisms, thus presenting a viable option for the treatment of multidrug-resistant bacteria.
DOI: 10.1128/mSphere.00175-19
PubMed: 31043515
PubMed Central: PMC6495337
Links to Exploration step
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sortKey="Wang, Zhen" sort="Wang, Zhen" uniqKey="Wang Z" first="Zhen" last="Wang">Zhen Wang</name><affiliation><nlm:affiliation>Key Laboratory of Functional Protein Research of Guangdong Higher Education Institutes, Institute of Life and Health Engineering, College of Life Science and Technology, Jinan University, Guangzhou, China.</nlm:affiliation></affiliation></author><author><name sortKey="Zhang, Gong" sort="Zhang, Gong" uniqKey="Zhang G" first="Gong" last="Zhang">Gong Zhang</name><affiliation><nlm:affiliation>Key Laboratory of Functional Protein Research of Guangdong Higher Education Institutes, Institute of Life and Health Engineering, College of Life Science and Technology, Jinan University, Guangzhou, China.</nlm:affiliation></affiliation></author><author><name sortKey="Sun, Xuesong" sort="Sun, Xuesong" uniqKey="Sun X" first="Xuesong" last="Sun">Xuesong Sun</name><affiliation><nlm:affiliation>Key Laboratory of Functional Protein Research of Guangdong Higher Education Institutes, Institute of Life and Health Engineering, College of Life Science and Technology, Jinan University, Guangzhou, China tsunxs@jnu.edu.cn tqyhe@jnu.edu.cn.</nlm:affiliation></affiliation></author><author><name sortKey="He, Qing Yu" sort="He, Qing Yu" uniqKey="He Q" first="Qing-Yu" last="He">Qing-Yu He</name><affiliation><nlm:affiliation>Key Laboratory of Functional Protein Research of Guangdong Higher Education Institutes, Institute of Life and Health Engineering, College of Life Science and Technology, Jinan University, Guangzhou, China tsunxs@jnu.edu.cn tqyhe@jnu.edu.cn.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2019">2019</date><idno type="RBID">pubmed:31043515</idno><idno type="pmid">31043515</idno><idno type="doi">10.1128/mSphere.00175-19</idno><idno type="pmc">PMC6495337</idno><idno type="wicri:Area/Main/Corpus">000271</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000271</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Photocatalytic Protein Damage by Silver Nanoparticles Circumvents Bacterial Stress Response and Multidrug Resistance.</title><author><name sortKey="Shi, Tianyuan" sort="Shi, Tianyuan" uniqKey="Shi T" first="Tianyuan" last="Shi">Tianyuan Shi</name><affiliation><nlm:affiliation>Key Laboratory of Functional Protein Research of Guangdong Higher Education Institutes, Institute of Life and Health Engineering, College of Life Science and Technology, Jinan University, Guangzhou, China.</nlm:affiliation></affiliation></author><author><name sortKey="Wei, Qiuxia" sort="Wei, Qiuxia" uniqKey="Wei Q" first="Qiuxia" last="Wei">Qiuxia Wei</name><affiliation><nlm:affiliation>Key Laboratory of Functional Protein Research of Guangdong Higher Education Institutes, Institute of Life and Health Engineering, College of Life Science and Technology, Jinan University, Guangzhou, China.</nlm:affiliation></affiliation></author><author><name sortKey="Wang, Zhen" sort="Wang, Zhen" uniqKey="Wang Z" first="Zhen" last="Wang">Zhen Wang</name><affiliation><nlm:affiliation>Key Laboratory of Functional Protein Research of Guangdong Higher Education Institutes, Institute of Life and Health Engineering, College of Life Science and Technology, Jinan University, Guangzhou, China.</nlm:affiliation></affiliation></author><author><name sortKey="Zhang, Gong" sort="Zhang, Gong" uniqKey="Zhang G" first="Gong" last="Zhang">Gong Zhang</name><affiliation><nlm:affiliation>Key Laboratory of Functional Protein Research of Guangdong Higher Education Institutes, Institute of Life and Health Engineering, College of Life Science and Technology, Jinan University, Guangzhou, China.</nlm:affiliation></affiliation></author><author><name sortKey="Sun, Xuesong" sort="Sun, Xuesong" uniqKey="Sun X" first="Xuesong" last="Sun">Xuesong Sun</name><affiliation><nlm:affiliation>Key Laboratory of Functional Protein Research of Guangdong Higher Education Institutes, Institute of Life and Health Engineering, College of Life Science and Technology, Jinan University, Guangzhou, China tsunxs@jnu.edu.cn tqyhe@jnu.edu.cn.</nlm:affiliation></affiliation></author><author><name sortKey="He, Qing Yu" sort="He, Qing Yu" uniqKey="He Q" first="Qing-Yu" last="He">Qing-Yu He</name><affiliation><nlm:affiliation>Key Laboratory of Functional Protein Research of Guangdong Higher Education Institutes, Institute of Life and Health Engineering, College of Life Science and Technology, Jinan University, Guangzhou, China tsunxs@jnu.edu.cn tqyhe@jnu.edu.cn.</nlm:affiliation></affiliation></author></analytic><series><title level="j">mSphere</title><idno type="eISSN">2379-5042</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Anti-Bacterial Agents (pharmacology)</term><term>Catalysis (MeSH)</term><term>Drug Resistance, Multiple, Bacterial (radiation effects)</term><term>Escherichia coli (drug effects)</term><term>Escherichia coli (radiation effects)</term><term>Light (MeSH)</term><term>Metal Nanoparticles (chemistry)</term><term>Microbial Sensitivity Tests (MeSH)</term><term>Oxidative Stress (MeSH)</term><term>Protein Aggregates (MeSH)</term><term>Silver (chemistry)</term><term>Silver (pharmacology)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Silver</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Anti-Bacterial Agents</term><term>Silver</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Metal Nanoparticles</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="radiation effects" xml:lang="en"><term>Drug Resistance, Multiple, Bacterial</term><term>Escherichia coli</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Catalysis</term><term>Light</term><term>Microbial Sensitivity Tests</term><term>Oxidative Stress</term><term>Protein Aggregates</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Silver nanoparticles (AgNPs) are known for their broad-spectrum antibacterial properties, especially against antibiotic-resistant bacteria. However, the bactericidal mechanism of AgNPs remains unclear. In this study, we found that the bactericidal ability of AgNPs is induced by light. In contrast to previous postulates, visible light is unable to trigger silver ion release from AgNPs or to promote AgNPs to induce reactive oxygen species (ROS) in <i>Escherichia coli</i> In fact, we revealed that light excited AgNPs to induce protein aggregation in a concentration-dependent manner in <i>E. coli</i>, indicating that the bactericidal ability of AgNPs relies on the light-catalyzed oxidation of cellular proteins via direct binding to proteins, which was verified by fluorescence spectra. AgNPs likely absorb the light energy and transfer it to the proteins, leading to the oxidation of proteins and thus promoting the death of the bacteria. Isobaric tags for relative and absolute quantitation (iTRAQ)-based proteomics revealed that the bacteria failed to develop effective resistance to the light-excited AgNPs. This direct physical mechanism is unlikely to be counteracted by any known drug resistance mechanisms of bacteria and therefore may serve as a last resort against drug resistance. This mechanism also provides a practical hint regarding the antimicrobial application of AgNPs-light exposure improves the efficacy of AgNPs.<b>IMPORTANCE</b> Although silver nanoparticles (AgNPs) are well known for their antibacterial properties, the mechanism by which they kill bacterial cells remains a topic of debate. In this study, we uncovered the bactericidal mechanism of AgNPs, which is induced by light. We tested the efficacy of AgNPs against a panel of antimicrobial-resistant pathogens as well as <i>Escherichia coli</i> under conditions of light and darkness and revealed that light excited the AgNPs to promote protein aggregation within the bacterial cells. Our report makes a significant contribution to the literature because this mechanism bypasses microbial drug resistance mechanisms, thus presenting a viable option for the treatment of multidrug-resistant bacteria.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31043515</PMID><DateCompleted><Year>2019</Year><Month>06</Month><Day>03</Day></DateCompleted><DateRevised><Year>2020</Year><Month>03</Month><Day>09</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2379-5042</ISSN><JournalIssue CitedMedium="Internet"><Volume>4</Volume><Issue>3</Issue><PubDate><Year>2019</Year><Month>05</Month><Day>01</Day></PubDate></JournalIssue><Title>mSphere</Title><ISOAbbreviation>mSphere</ISOAbbreviation></Journal><ArticleTitle>Photocatalytic Protein Damage by Silver Nanoparticles Circumvents Bacterial Stress Response and Multidrug Resistance.</ArticleTitle><ELocationID EIdType="pii" ValidYN="Y">e00175-19</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1128/mSphere.00175-19</ELocationID><Abstract><AbstractText>Silver nanoparticles (AgNPs) are known for their broad-spectrum antibacterial properties, especially against antibiotic-resistant bacteria. However, the bactericidal mechanism of AgNPs remains unclear. In this study, we found that the bactericidal ability of AgNPs is induced by light. In contrast to previous postulates, visible light is unable to trigger silver ion release from AgNPs or to promote AgNPs to induce reactive oxygen species (ROS) in <i>Escherichia coli</i> In fact, we revealed that light excited AgNPs to induce protein aggregation in a concentration-dependent manner in <i>E. coli</i>, indicating that the bactericidal ability of AgNPs relies on the light-catalyzed oxidation of cellular proteins via direct binding to proteins, which was verified by fluorescence spectra. AgNPs likely absorb the light energy and transfer it to the proteins, leading to the oxidation of proteins and thus promoting the death of the bacteria. Isobaric tags for relative and absolute quantitation (iTRAQ)-based proteomics revealed that the bacteria failed to develop effective resistance to the light-excited AgNPs. This direct physical mechanism is unlikely to be counteracted by any known drug resistance mechanisms of bacteria and therefore may serve as a last resort against drug resistance. This mechanism also provides a practical hint regarding the antimicrobial application of AgNPs-light exposure improves the efficacy of AgNPs.<b>IMPORTANCE</b> Although silver nanoparticles (AgNPs) are well known for their antibacterial properties, the mechanism by which they kill bacterial cells remains a topic of debate. In this study, we uncovered the bactericidal mechanism of AgNPs, which is induced by light. We tested the efficacy of AgNPs against a panel of antimicrobial-resistant pathogens as well as <i>Escherichia coli</i> under conditions of light and darkness and revealed that light excited the AgNPs to promote protein aggregation within the bacterial cells. Our report makes a significant contribution to the literature because this mechanism bypasses microbial drug resistance mechanisms, thus presenting a viable option for the treatment of multidrug-resistant bacteria.</AbstractText><CopyrightInformation>Copyright © 2019 Shi et al.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y" EqualContrib="Y"><LastName>Shi</LastName><ForeName>Tianyuan</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Key Laboratory of Functional Protein Research of Guangdong Higher Education Institutes, Institute of Life and Health Engineering, College of Life Science and Technology, Jinan University, Guangzhou, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y" EqualContrib="Y"><LastName>Wei</LastName><ForeName>Qiuxia</ForeName><Initials>Q</Initials><AffiliationInfo><Affiliation>Key Laboratory of Functional Protein Research of Guangdong Higher Education Institutes, Institute of Life and Health Engineering, College of Life Science and Technology, Jinan University, Guangzhou, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Zhen</ForeName><Initials>Z</Initials><AffiliationInfo><Affiliation>Key Laboratory of Functional Protein Research of Guangdong Higher Education Institutes, Institute of Life and Health Engineering, College of Life Science and Technology, Jinan University, Guangzhou, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y" EqualContrib="Y"><LastName>Zhang</LastName><ForeName>Gong</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Key Laboratory of Functional Protein Research of Guangdong Higher Education Institutes, Institute of Life and Health Engineering, College of Life Science and Technology, Jinan University, Guangzhou, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y" EqualContrib="Y"><LastName>Sun</LastName><ForeName>Xuesong</ForeName><Initials>X</Initials><Identifier Source="ORCID">0000-0002-5425-321X</Identifier><AffiliationInfo><Affiliation>Key Laboratory of Functional Protein Research of Guangdong Higher Education Institutes, Institute of Life and Health Engineering, College of Life Science and Technology, Jinan University, Guangzhou, China tsunxs@jnu.edu.cn tqyhe@jnu.edu.cn.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y" EqualContrib="Y"><LastName>He</LastName><ForeName>Qing-Yu</ForeName><Initials>QY</Initials><AffiliationInfo><Affiliation>Key Laboratory of Functional Protein Research of Guangdong Higher Education Institutes, Institute of Life and Health Engineering, College of Life Science and Technology, Jinan University, Guangzhou, China tsunxs@jnu.edu.cn tqyhe@jnu.edu.cn.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. 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|texte= Photocatalytic Protein Damage by Silver Nanoparticles Circumvents Bacterial Stress Response and Multidrug Resistance.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Corpus/RBID.i -Sk "pubmed:31043515" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Corpus/biblio.hfd \
| NlmPubMed2Wicri -a SilverBacteriV1
| This area was generated with Dilib version V0.6.38. |  |