The moonlighting peroxiredoxin-glutaredoxin in Neisseria meningitidis binds plasminogen via a C-terminal lysine residue and contributes to survival in a whole blood model.
Identifieur interne : 000009 ( Main/Exploration ); précédent : 000008; suivant : 000010The moonlighting peroxiredoxin-glutaredoxin in Neisseria meningitidis binds plasminogen via a C-terminal lysine residue and contributes to survival in a whole blood model.
Auteurs : Mahab A K. Aljannat [Royaume-Uni] ; Neil J. Oldfield [Royaume-Uni] ; Hibah M. Albasri [Royaume-Uni] ; Louise K G. Dorrington [Royaume-Uni] ; Radhica L. Ohri [Royaume-Uni] ; Karl G. Wooldridge [Royaume-Uni] ; David P J. Turner [Royaume-Uni]Source :
- Microbial pathogenesis [ 1096-1208 ] ; 2020.
Descripteurs français
- KwdFr :
- Glutarédoxines (composition chimique), Glutarédoxines (génétique), Glutarédoxines (métabolisme), Humains (MeSH), Infections à méningocoques (diagnostic), Infections à méningocoques (microbiologie), Infections à méningocoques (mortalité), Infections à méningocoques (métabolisme), Interactions hôte-pathogène (MeSH), Liaison aux protéines (MeSH), Motifs et domaines d'intéraction protéique (MeSH), Mutation (MeSH), Neisseria meningitidis (physiologie), Peroxirédoxines (composition chimique), Peroxirédoxines (génétique), Peroxirédoxines (métabolisme), Peroxyde d'hydrogène (métabolisme), Plasminogène (composition chimique), Plasminogène (métabolisme), Pronostic (MeSH), Test ELISA (MeSH).
- MESH :
- composition chimique : Glutarédoxines, Peroxirédoxines, Plasminogène.
- diagnostic : Infections à méningocoques.
- génétique : Glutarédoxines, Peroxirédoxines.
- microbiologie : Infections à méningocoques.
- mortalité : Infections à méningocoques.
- métabolisme : Glutarédoxines, Infections à méningocoques, Peroxirédoxines, Peroxyde d'hydrogène, Plasminogène.
- physiologie : Neisseria meningitidis.
- Humains, Interactions hôte-pathogène, Liaison aux protéines, Motifs et domaines d'intéraction protéique, Mutation, Pronostic, Test ELISA.
English descriptors
- KwdEn :
- Enzyme-Linked Immunosorbent Assay (MeSH), Glutaredoxins (chemistry), Glutaredoxins (genetics), Glutaredoxins (metabolism), Host-Pathogen Interactions (MeSH), Humans (MeSH), Hydrogen Peroxide (metabolism), Meningococcal Infections (diagnosis), Meningococcal Infections (metabolism), Meningococcal Infections (microbiology), Meningococcal Infections (mortality), Mutation (MeSH), Neisseria meningitidis (physiology), Peroxiredoxins (chemistry), Peroxiredoxins (genetics), Peroxiredoxins (metabolism), Plasminogen (chemistry), Plasminogen (metabolism), Prognosis (MeSH), Protein Binding (MeSH), Protein Interaction Domains and Motifs (MeSH).
- MESH :
- chemical , chemistry : Glutaredoxins, Peroxiredoxins, Plasminogen.
- chemical , genetics : Glutaredoxins, Peroxiredoxins.
- chemical , metabolism : Glutaredoxins, Hydrogen Peroxide, Peroxiredoxins, Plasminogen.
- diagnosis : Meningococcal Infections.
- metabolism : Meningococcal Infections.
- microbiology : Meningococcal Infections.
- mortality : Meningococcal Infections.
- physiology : Neisseria meningitidis.
- Enzyme-Linked Immunosorbent Assay, Host-Pathogen Interactions, Humans, Mutation, Prognosis, Protein Binding, Protein Interaction Domains and Motifs.
Abstract
Neisseria meningitidis is a human-restricted bacterium that can invade the bloodstream and cross the blood-brain barrier resulting in life-threatening sepsis and meningitis. Meningococci express a cytoplasmic peroxiredoxin-glutaredoxin (Prx5-Grx) hybrid protein that has also been identified on the bacterial surface. Here, recombinant Prx5-Grx was confirmed as a plasminogen (Plg)-binding protein, in an interaction which could be inhibited by the lysine analogue ε-aminocapronic acid. rPrx5-Grx derivatives bearing a substituted C-terminal lysine residue (rPrx5-GrxK244A), but not the active site cysteine residue (rPrx5-GrxC185A) or the sub-terminal rPrx5-GrxK230A lysine residue, exhibited significantly reduced Plg-binding. The absence of Prx5-Grx did not significantly reduce the ability of whole meningococcal cells to bind Plg, but under hydrogen peroxide-mediated oxidative stress, the N. meningitidis Δpxn5-grx mutant survived significantly better than the wild-type or complemented strains. Significantly, using human whole blood as a model of meningococcal bacteremia, it was found that the N. meningitidis Δpxn5-grx mutant had a survival defect compared with the parental or complemented strain, confirming an important role for Prx5-Grx in meningococcal pathogenesis.
DOI: 10.1016/j.micpath.2019.103890
PubMed: 31765768
Affiliations:
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Aljannat</name><affiliation wicri:level="4"><nlm:affiliation>School of Life Sciences, University of Nottingham, Nottingham, NG7 2RD, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>School of Life Sciences, University of Nottingham, Nottingham, NG7 2RD</wicri:regionArea><orgName type="university">Université de Nottingham</orgName><placeName><settlement type="city">Nottingham</settlement><region type="nation">Angleterre</region><region type="région" nuts="1">Nottinghamshire</region></placeName></affiliation></author><author><name sortKey="Oldfield, Neil J" sort="Oldfield, Neil J" uniqKey="Oldfield N" first="Neil J" last="Oldfield">Neil J. Oldfield</name><affiliation wicri:level="4"><nlm:affiliation>School of Life Sciences, University of Nottingham, Nottingham, NG7 2RD, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>School of Life Sciences, University of Nottingham, Nottingham, NG7 2RD</wicri:regionArea><orgName type="university">Université de Nottingham</orgName><placeName><settlement type="city">Nottingham</settlement><region type="nation">Angleterre</region><region type="région" nuts="1">Nottinghamshire</region></placeName></affiliation></author><author><name sortKey="Albasri, Hibah M" sort="Albasri, Hibah M" uniqKey="Albasri H" first="Hibah M" last="Albasri">Hibah M. Albasri</name><affiliation wicri:level="4"><nlm:affiliation>School of Life Sciences, University of Nottingham, Nottingham, NG7 2RD, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>School of Life Sciences, University of Nottingham, Nottingham, NG7 2RD</wicri:regionArea><orgName type="university">Université de Nottingham</orgName><placeName><settlement type="city">Nottingham</settlement><region type="nation">Angleterre</region><region type="région" nuts="1">Nottinghamshire</region></placeName></affiliation></author><author><name sortKey="Dorrington, Louise K G" sort="Dorrington, Louise K G" uniqKey="Dorrington L" first="Louise K G" last="Dorrington">Louise K G. 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Electronic address: david.turner@nottingham.ac.uk.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>School of Life Sciences, University of Nottingham, Nottingham, NG7 2RD</wicri:regionArea><orgName type="university">Université de Nottingham</orgName><placeName><settlement type="city">Nottingham</settlement><region type="nation">Angleterre</region><region type="région" nuts="1">Nottinghamshire</region></placeName></affiliation></author></analytic><series><title level="j">Microbial pathogenesis</title><idno type="eISSN">1096-1208</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Enzyme-Linked Immunosorbent Assay (MeSH)</term><term>Glutaredoxins (chemistry)</term><term>Glutaredoxins (genetics)</term><term>Glutaredoxins (metabolism)</term><term>Host-Pathogen Interactions (MeSH)</term><term>Humans (MeSH)</term><term>Hydrogen Peroxide (metabolism)</term><term>Meningococcal Infections (diagnosis)</term><term>Meningococcal Infections (metabolism)</term><term>Meningococcal Infections (microbiology)</term><term>Meningococcal Infections (mortality)</term><term>Mutation (MeSH)</term><term>Neisseria meningitidis (physiology)</term><term>Peroxiredoxins (chemistry)</term><term>Peroxiredoxins (genetics)</term><term>Peroxiredoxins (metabolism)</term><term>Plasminogen (chemistry)</term><term>Plasminogen (metabolism)</term><term>Prognosis (MeSH)</term><term>Protein Binding (MeSH)</term><term>Protein Interaction Domains and Motifs (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Glutarédoxines (composition chimique)</term><term>Glutarédoxines (génétique)</term><term>Glutarédoxines (métabolisme)</term><term>Humains (MeSH)</term><term>Infections à méningocoques (diagnostic)</term><term>Infections à méningocoques (microbiologie)</term><term>Infections à méningocoques (mortalité)</term><term>Infections à méningocoques (métabolisme)</term><term>Interactions hôte-pathogène (MeSH)</term><term>Liaison aux protéines (MeSH)</term><term>Motifs et domaines d'intéraction protéique (MeSH)</term><term>Mutation (MeSH)</term><term>Neisseria meningitidis (physiologie)</term><term>Peroxirédoxines (composition chimique)</term><term>Peroxirédoxines (génétique)</term><term>Peroxirédoxines (métabolisme)</term><term>Peroxyde d'hydrogène (métabolisme)</term><term>Plasminogène (composition chimique)</term><term>Plasminogène (métabolisme)</term><term>Pronostic (MeSH)</term><term>Test ELISA (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutaredoxins</term><term>Peroxiredoxins</term><term>Plasminogen</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutaredoxins</term><term>Peroxiredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutaredoxins</term><term>Hydrogen Peroxide</term><term>Peroxiredoxins</term><term>Plasminogen</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glutarédoxines</term><term>Peroxirédoxines</term><term>Plasminogène</term></keywords><keywords scheme="MESH" qualifier="diagnosis" xml:lang="en"><term>Meningococcal Infections</term></keywords><keywords scheme="MESH" qualifier="diagnostic" xml:lang="fr"><term>Infections à méningocoques</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glutarédoxines</term><term>Peroxirédoxines</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Meningococcal Infections</term></keywords><keywords scheme="MESH" qualifier="microbiologie" xml:lang="fr"><term>Infections à méningocoques</term></keywords><keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Meningococcal Infections</term></keywords><keywords scheme="MESH" qualifier="mortality" xml:lang="en"><term>Meningococcal Infections</term></keywords><keywords scheme="MESH" qualifier="mortalité" xml:lang="fr"><term>Infections à méningocoques</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutarédoxines</term><term>Infections à méningocoques</term><term>Peroxirédoxines</term><term>Peroxyde d'hydrogène</term><term>Plasminogène</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Neisseria meningitidis</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Neisseria meningitidis</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Enzyme-Linked Immunosorbent Assay</term><term>Host-Pathogen Interactions</term><term>Humans</term><term>Mutation</term><term>Prognosis</term><term>Protein Binding</term><term>Protein Interaction Domains and Motifs</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Humains</term><term>Interactions hôte-pathogène</term><term>Liaison aux protéines</term><term>Motifs et domaines d'intéraction protéique</term><term>Mutation</term><term>Pronostic</term><term>Test ELISA</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Neisseria meningitidis is a human-restricted bacterium that can invade the bloodstream and cross the blood-brain barrier resulting in life-threatening sepsis and meningitis. Meningococci express a cytoplasmic peroxiredoxin-glutaredoxin (Prx5-Grx) hybrid protein that has also been identified on the bacterial surface. Here, recombinant Prx5-Grx was confirmed as a plasminogen (Plg)-binding protein, in an interaction which could be inhibited by the lysine analogue ε-aminocapronic acid. rPrx5-Grx derivatives bearing a substituted C-terminal lysine residue (rPrx5-Grx<sup>K244A</sup>), but not the active site cysteine residue (rPrx5-Grx<sup>C185A</sup>) or the sub-terminal rPrx5-Grx<sup>K230A</sup> lysine residue, exhibited significantly reduced Plg-binding. The absence of Prx5-Grx did not significantly reduce the ability of whole meningococcal cells to bind Plg, but under hydrogen peroxide-mediated oxidative stress, the N. meningitidis Δpxn5-grx mutant survived significantly better than the wild-type or complemented strains. Significantly, using human whole blood as a model of meningococcal bacteremia, it was found that the N. meningitidis Δpxn5-grx mutant had a survival defect compared with the parental or complemented strain, confirming an important role for Prx5-Grx in meningococcal pathogenesis.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31765768</PMID><DateCompleted><Year>2020</Year><Month>11</Month><Day>16</Day></DateCompleted><DateRevised><Year>2020</Year><Month>11</Month><Day>16</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1096-1208</ISSN><JournalIssue CitedMedium="Internet"><Volume>139</Volume><PubDate><Year>2020</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Microbial pathogenesis</Title><ISOAbbreviation>Microb Pathog</ISOAbbreviation></Journal><ArticleTitle>The moonlighting peroxiredoxin-glutaredoxin in Neisseria meningitidis binds plasminogen via a C-terminal lysine residue and contributes to survival in a whole blood model.</ArticleTitle><Pagination><MedlinePgn>103890</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0882-4010(19)31119-2</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.micpath.2019.103890</ELocationID><Abstract><AbstractText>Neisseria meningitidis is a human-restricted bacterium that can invade the bloodstream and cross the blood-brain barrier resulting in life-threatening sepsis and meningitis. Meningococci express a cytoplasmic peroxiredoxin-glutaredoxin (Prx5-Grx) hybrid protein that has also been identified on the bacterial surface. Here, recombinant Prx5-Grx was confirmed as a plasminogen (Plg)-binding protein, in an interaction which could be inhibited by the lysine analogue ε-aminocapronic acid. rPrx5-Grx derivatives bearing a substituted C-terminal lysine residue (rPrx5-Grx<sup>K244A</sup>), but not the active site cysteine residue (rPrx5-Grx<sup>C185A</sup>) or the sub-terminal rPrx5-Grx<sup>K230A</sup> lysine residue, exhibited significantly reduced Plg-binding. The absence of Prx5-Grx did not significantly reduce the ability of whole meningococcal cells to bind Plg, but under hydrogen peroxide-mediated oxidative stress, the N. meningitidis Δpxn5-grx mutant survived significantly better than the wild-type or complemented strains. Significantly, using human whole blood as a model of meningococcal bacteremia, it was found that the N. meningitidis Δpxn5-grx mutant had a survival defect compared with the parental or complemented strain, confirming an important role for Prx5-Grx in meningococcal pathogenesis.</AbstractText><CopyrightInformation>Copyright © 2019 Elsevier Ltd. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Aljannat</LastName><ForeName>Mahab A K</ForeName><Initials>MAK</Initials><AffiliationInfo><Affiliation>School of Life Sciences, University of Nottingham, Nottingham, NG7 2RD, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Oldfield</LastName><ForeName>Neil J</ForeName><Initials>NJ</Initials><AffiliationInfo><Affiliation>School of Life Sciences, University of Nottingham, Nottingham, NG7 2RD, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Albasri</LastName><ForeName>Hibah M</ForeName><Initials>HM</Initials><AffiliationInfo><Affiliation>School of Life Sciences, University of Nottingham, Nottingham, NG7 2RD, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dorrington</LastName><ForeName>Louise K G</ForeName><Initials>LKG</Initials><AffiliationInfo><Affiliation>School of Life Sciences, University of Nottingham, Nottingham, NG7 2RD, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ohri</LastName><ForeName>Radhica L</ForeName><Initials>RL</Initials><AffiliationInfo><Affiliation>School of Life Sciences, University of Nottingham, Nottingham, NG7 2RD, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wooldridge</LastName><ForeName>Karl G</ForeName><Initials>KG</Initials><AffiliationInfo><Affiliation>School of Life Sciences, University of Nottingham, Nottingham, NG7 2RD, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Turner</LastName><ForeName>David P J</ForeName><Initials>DPJ</Initials><AffiliationInfo><Affiliation>School of Life Sciences, University of Nottingham, Nottingham, NG7 2RD, UK. Electronic address: david.turner@nottingham.ac.uk.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>11</Month><Day>23</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Microb Pathog</MedlineTA><NlmUniqueID>8606191</NlmUniqueID><ISSNLinking>0882-4010</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>9001-91-6</RegistryNumber><NameOfSubstance UI="D010958">Plasminogen</NameOfSubstance></Chemical><Chemical><RegistryNumber>BBX060AN9V</RegistryNumber><NameOfSubstance UI="D006861">Hydrogen Peroxide</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.15</RegistryNumber><NameOfSubstance UI="D054464">Peroxiredoxins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D004797" MajorTopicYN="N">Enzyme-Linked Immunosorbent Assay</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054884" MajorTopicYN="Y">Host-Pathogen Interactions</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006861" MajorTopicYN="N">Hydrogen Peroxide</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008589" MajorTopicYN="N">Meningococcal Infections</DescriptorName><QualifierName UI="Q000175" MajorTopicYN="N">diagnosis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000382" MajorTopicYN="Y">microbiology</QualifierName><QualifierName UI="Q000401" MajorTopicYN="N">mortality</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009345" MajorTopicYN="N">Neisseria meningitidis</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054464" MajorTopicYN="N">Peroxiredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010958" MajorTopicYN="N">Plasminogen</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011379" MajorTopicYN="N">Prognosis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054730" MajorTopicYN="N">Protein Interaction Domains and Motifs</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Neisseria meningitidis</Keyword><Keyword MajorTopicYN="N">Pathogenesis</Keyword><Keyword MajorTopicYN="N">Peroxiredoxin</Keyword><Keyword MajorTopicYN="N">Plasminogen</Keyword><Keyword MajorTopicYN="N">Protein moonlighting</Keyword><Keyword MajorTopicYN="N">Whole blood model</Keyword></KeywordList><CoiStatement>Declaration of competing interest The authors declare that there are no conflicts of interest.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>06</Month><Day>27</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2019</Year><Month>11</Month><Day>20</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2019</Year><Month>11</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2019</Year><Month>11</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>11</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2019</Year><Month>11</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">31765768</ArticleId><ArticleId IdType="pii">S0882-4010(19)31119-2</ArticleId><ArticleId IdType="doi">10.1016/j.micpath.2019.103890</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Royaume-Uni</li></country><region><li>Angleterre</li><li>Nottinghamshire</li></region><settlement><li>Nottingham</li></settlement><orgName><li>Université de Nottingham</li></orgName></list><tree><country name="Royaume-Uni"><region name="Angleterre"><name sortKey="Aljannat, Mahab A K" sort="Aljannat, Mahab A K" uniqKey="Aljannat M" first="Mahab A K" last="Aljannat">Mahab A K. Aljannat</name></region><name sortKey="Albasri, Hibah M" sort="Albasri, Hibah M" uniqKey="Albasri H" first="Hibah M" last="Albasri">Hibah M. Albasri</name><name sortKey="Dorrington, Louise K G" sort="Dorrington, Louise K G" uniqKey="Dorrington L" first="Louise K G" last="Dorrington">Louise K G. Dorrington</name><name sortKey="Ohri, Radhica L" sort="Ohri, Radhica L" uniqKey="Ohri R" first="Radhica L" last="Ohri">Radhica L. Ohri</name><name sortKey="Oldfield, Neil J" sort="Oldfield, Neil J" uniqKey="Oldfield N" first="Neil J" last="Oldfield">Neil J. Oldfield</name><name sortKey="Turner, David P J" sort="Turner, David P J" uniqKey="Turner D" first="David P J" last="Turner">David P J. Turner</name><name sortKey="Wooldridge, Karl G" sort="Wooldridge, Karl G" uniqKey="Wooldridge K" first="Karl G" last="Wooldridge">Karl G. Wooldridge</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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