Cooperative, synergistic and antagonistic haemolytic interactions between haemolysin BL, phosphatidylcholine phospholipase C and sphingomyelinase from Bacillus cereus.
Identifieur interne : 002092 ( Main/Corpus ); précédent : 002091; suivant : 002093Cooperative, synergistic and antagonistic haemolytic interactions between haemolysin BL, phosphatidylcholine phospholipase C and sphingomyelinase from Bacillus cereus.
Auteurs : Douglas J. Beecher ; Amy C L. WongSource :
- Microbiology (Reading, England) [ 1350-0872 ] ; 2000.
English descriptors
- KwdEn :
- Animals (MeSH), Bacillus cereus (enzymology), Bacterial Proteins (metabolism), Cattle (MeSH), Drug Antagonism (MeSH), Drug Synergism (MeSH), Erythrocytes (metabolism), Hemolysin Proteins (MeSH), Hemolysis (MeSH), Hemolytic Plaque Technique (MeSH), Humans (MeSH), Sphingomyelin Phosphodiesterase (metabolism), Type C Phospholipases (metabolism).
- MESH :
- chemical , metabolism : Bacterial Proteins, Sphingomyelin Phosphodiesterase, Type C Phospholipases.
- enzymology : Bacillus cereus.
- metabolism : Erythrocytes.
- Animals, Cattle, Drug Antagonism, Drug Synergism, Hemolysin Proteins, Hemolysis, Hemolytic Plaque Technique, Humans.
Abstract
Haemolysis of erythrocytes from different species (sheep, bovine, swine and human), caused by various combinations of phosphatidylcholine (PC)-preferring phospholipase C (PC-PLC), sphingomyelinase (SMase) and the three-component, pore-forming toxin haemolysin BL (HBL) from Bacillus cereus was analysed. The lytic potency of HBL did not correlate with phospholipid (PL) content, but lysis by the individual or combined enzymes did. SMase alone lysed ruminant erythrocytes, which contain 46-53% sphingomyelin (SM). The cooperative action of PC-PLC and SMase was needed to lyse swine and human erythrocytes (22-31% PC and 28-25% SM). SMase synergistically enhanced haemolysis caused by HBL for all erythrocytes tested, which all contained >25% SM. PC-PLC enhanced HBL haemolysis only in cells containing significant amounts of PC (swine, 22% PC; human, 31% PC). Unexpectedly, PC-PLC inhibited HBL lysis of sheep erythrocytes (<2% PC) and enhanced the discontinuous haemolysis pattern that is characteristic of HBL in sheep blood agar. Inhibition and pattern enhancement was abolished by washing PC-PLC-treated erythrocytes or by adding EDTA, suggesting that enzymic alteration of the membrane is not involved, but that zinc in the active site is required, perhaps to facilitate binding. These observations highlight the potential for cooperative and synergistic interactions among virulence factors in B. cereus infections and dependence of these effects on tissue composition.
DOI: 10.1099/00221287-146-12-3033
PubMed: 11101661
Links to Exploration step
pubmed:11101661Le document en format XML
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Wong</name><affiliation><nlm:affiliation>Food Research Institute, Department of Food Microbiology and Toxicology, University of Wisconsin-Madison, 1925 Willow Drive, Madison WI 53706, USA1.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2000">2000</date><idno type="RBID">pubmed:11101661</idno><idno type="pmid">11101661</idno><idno type="doi">10.1099/00221287-146-12-3033</idno><idno type="wicri:Area/Main/Corpus">002092</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">002092</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Cooperative, synergistic and antagonistic haemolytic interactions between haemolysin BL, phosphatidylcholine phospholipase C and sphingomyelinase from Bacillus cereus.</title><author><name sortKey="Beecher, Douglas J" sort="Beecher, Douglas J" uniqKey="Beecher D" first="Douglas J" last="Beecher">Douglas J. Beecher</name><affiliation><nlm:affiliation>Food Research Institute, Department of Food Microbiology and Toxicology, University of Wisconsin-Madison, 1925 Willow Drive, Madison WI 53706, USA1.</nlm:affiliation></affiliation></author><author><name sortKey="Wong, Amy C L" sort="Wong, Amy C L" uniqKey="Wong A" first="Amy C L" last="Wong">Amy C L. Wong</name><affiliation><nlm:affiliation>Food Research Institute, Department of Food Microbiology and Toxicology, University of Wisconsin-Madison, 1925 Willow Drive, Madison WI 53706, USA1.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Microbiology (Reading, England)</title><idno type="ISSN">1350-0872</idno><imprint><date when="2000" type="published">2000</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Bacillus cereus (enzymology)</term><term>Bacterial Proteins (metabolism)</term><term>Cattle (MeSH)</term><term>Drug Antagonism (MeSH)</term><term>Drug Synergism (MeSH)</term><term>Erythrocytes (metabolism)</term><term>Hemolysin Proteins (MeSH)</term><term>Hemolysis (MeSH)</term><term>Hemolytic Plaque Technique (MeSH)</term><term>Humans (MeSH)</term><term>Sphingomyelin Phosphodiesterase (metabolism)</term><term>Type C Phospholipases (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Bacterial Proteins</term><term>Sphingomyelin Phosphodiesterase</term><term>Type C Phospholipases</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Bacillus cereus</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Erythrocytes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cattle</term><term>Drug Antagonism</term><term>Drug Synergism</term><term>Hemolysin Proteins</term><term>Hemolysis</term><term>Hemolytic Plaque Technique</term><term>Humans</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Haemolysis of erythrocytes from different species (sheep, bovine, swine and human), caused by various combinations of phosphatidylcholine (PC)-preferring phospholipase C (PC-PLC), sphingomyelinase (SMase) and the three-component, pore-forming toxin haemolysin BL (HBL) from Bacillus cereus was analysed. The lytic potency of HBL did not correlate with phospholipid (PL) content, but lysis by the individual or combined enzymes did. SMase alone lysed ruminant erythrocytes, which contain 46-53% sphingomyelin (SM). The cooperative action of PC-PLC and SMase was needed to lyse swine and human erythrocytes (22-31% PC and 28-25% SM). SMase synergistically enhanced haemolysis caused by HBL for all erythrocytes tested, which all contained >25% SM. PC-PLC enhanced HBL haemolysis only in cells containing significant amounts of PC (swine, 22% PC; human, 31% PC). Unexpectedly, PC-PLC inhibited HBL lysis of sheep erythrocytes (<2% PC) and enhanced the discontinuous haemolysis pattern that is characteristic of HBL in sheep blood agar. Inhibition and pattern enhancement was abolished by washing PC-PLC-treated erythrocytes or by adding EDTA, suggesting that enzymic alteration of the membrane is not involved, but that zinc in the active site is required, perhaps to facilitate binding. These observations highlight the potential for cooperative and synergistic interactions among virulence factors in B. cereus infections and dependence of these effects on tissue composition.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11101661</PMID><DateCompleted><Year>2001</Year><Month>02</Month><Day>15</Day></DateCompleted><DateRevised><Year>2020</Year><Month>08</Month><Day>26</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1350-0872</ISSN><JournalIssue CitedMedium="Print"><Volume>146 Pt 12</Volume><PubDate><Year>2000</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Microbiology (Reading, England)</Title><ISOAbbreviation>Microbiology (Reading)</ISOAbbreviation></Journal><ArticleTitle>Cooperative, synergistic and antagonistic haemolytic interactions between haemolysin BL, phosphatidylcholine phospholipase C and sphingomyelinase from Bacillus cereus.</ArticleTitle><Pagination><MedlinePgn>3033-3039</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1099/00221287-146-12-3033</ELocationID><Abstract><AbstractText>Haemolysis of erythrocytes from different species (sheep, bovine, swine and human), caused by various combinations of phosphatidylcholine (PC)-preferring phospholipase C (PC-PLC), sphingomyelinase (SMase) and the three-component, pore-forming toxin haemolysin BL (HBL) from Bacillus cereus was analysed. The lytic potency of HBL did not correlate with phospholipid (PL) content, but lysis by the individual or combined enzymes did. SMase alone lysed ruminant erythrocytes, which contain 46-53% sphingomyelin (SM). The cooperative action of PC-PLC and SMase was needed to lyse swine and human erythrocytes (22-31% PC and 28-25% SM). SMase synergistically enhanced haemolysis caused by HBL for all erythrocytes tested, which all contained >25% SM. PC-PLC enhanced HBL haemolysis only in cells containing significant amounts of PC (swine, 22% PC; human, 31% PC). Unexpectedly, PC-PLC inhibited HBL lysis of sheep erythrocytes (<2% PC) and enhanced the discontinuous haemolysis pattern that is characteristic of HBL in sheep blood agar. Inhibition and pattern enhancement was abolished by washing PC-PLC-treated erythrocytes or by adding EDTA, suggesting that enzymic alteration of the membrane is not involved, but that zinc in the active site is required, perhaps to facilitate binding. These observations highlight the potential for cooperative and synergistic interactions among virulence factors in B. cereus infections and dependence of these effects on tissue composition.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Beecher</LastName><ForeName>Douglas J</ForeName><Initials>DJ</Initials><AffiliationInfo><Affiliation>Food Research Institute, Department of Food Microbiology and Toxicology, University of Wisconsin-Madison, 1925 Willow Drive, Madison WI 53706, USA1.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wong</LastName><ForeName>Amy C L</ForeName><Initials>ACL</Initials><AffiliationInfo><Affiliation>Food Research Institute, Department of Food Microbiology and Toxicology, University of Wisconsin-Madison, 1925 Willow Drive, Madison WI 53706, USA1.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Microbiology (Reading)</MedlineTA><NlmUniqueID>9430468</NlmUniqueID><ISSNLinking>1350-0872</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006460">Hemolysin Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C083961">hemolysin BL protein, Bacillus</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.4.-</RegistryNumber><NameOfSubstance UI="D010738">Type C Phospholipases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.4.12</RegistryNumber><NameOfSubstance UI="D013108">Sphingomyelin Phosphodiesterase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.4.3</RegistryNumber><NameOfSubstance UI="C105598">phosphatidylcholine-specific phospholipase C</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001409" MajorTopicYN="N">Bacillus cereus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001426" MajorTopicYN="N">Bacterial Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002417" MajorTopicYN="N">Cattle</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004336" MajorTopicYN="N">Drug Antagonism</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004357" MajorTopicYN="N">Drug Synergism</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004912" MajorTopicYN="N">Erythrocytes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006460" MajorTopicYN="N">Hemolysin Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006461" MajorTopicYN="Y">Hemolysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006462" MajorTopicYN="N">Hemolytic Plaque Technique</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013108" MajorTopicYN="N">Sphingomyelin Phosphodiesterase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010738" MajorTopicYN="N">Type C Phospholipases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2000</Year><Month>12</Month><Day>2</Day><Hour>11</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2001</Year><Month>3</Month><Day>3</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2000</Year><Month>12</Month><Day>2</Day><Hour>11</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">11101661</ArticleId><ArticleId IdType="doi">10.1099/00221287-146-12-3033</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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