The bacterial peptide N-formyl-Met-Leu-Phe inhibits killing of Staphylococcus epidermidis by human neutrophils in fibrin gels.
Identifieur interne : 000C62 ( Main/Corpus ); précédent : 000C61; suivant : 000C63The bacterial peptide N-formyl-Met-Leu-Phe inhibits killing of Staphylococcus epidermidis by human neutrophils in fibrin gels.
Auteurs : Yongmei Li ; John D. Loike ; Julia A. Ember ; P Patrick Cleary ; Emily Lu ; Sadna Budhu ; Long Cao ; Samuel C. SilversteinSource :
- Journal of immunology (Baltimore, Md. : 1950) [ 0022-1767 ] ; 2002.
English descriptors
- KwdEn :
- Adhesins, Bacterial (MeSH), Adult (MeSH), Bacterial Proteins (pharmacology), Cell Migration Inhibition (MeSH), Chemotaxis, Leukocyte (drug effects), Chemotaxis, Leukocyte (physiology), Complement C3 (metabolism), Complement C5a (metabolism), Complement C5a (pharmacology), Complement System Proteins (physiology), Endopeptidases (pharmacology), Fibrin (MeSH), Gels (MeSH), Humans (MeSH), Immunoglobulin G (metabolism), Leukotriene B4 (pharmacology), N-Formylmethionine Leucyl-Phenylalanine (analogs & derivatives), N-Formylmethionine Leucyl-Phenylalanine (pharmacology), Neutrophils (drug effects), Neutrophils (enzymology), Neutrophils (microbiology), Neutrophils (physiology), Opsonin Proteins (metabolism), Phagocytosis (drug effects), Staphylococcus epidermidis (drug effects), Staphylococcus epidermidis (growth & development), Staphylococcus epidermidis (isolation & purification), Streptococcus pyogenes (MeSH).
- MESH :
- chemical , analogs & derivatives : N-Formylmethionine Leucyl-Phenylalanine.
- chemical , metabolism : Complement C3, Complement C5a, Immunoglobulin G, Opsonin Proteins.
- chemical , pharmacology : Bacterial Proteins, Complement C5a, Endopeptidases, Leukotriene B4, N-Formylmethionine Leucyl-Phenylalanine.
- chemical , physiology : Complement System Proteins.
- chemical : Adhesins, Bacterial, Fibrin, Gels.
- drug effects : Chemotaxis, Leukocyte, Neutrophils, Phagocytosis, Staphylococcus epidermidis.
- enzymology : Neutrophils.
- growth & development : Staphylococcus epidermidis.
- isolation & purification : Staphylococcus epidermidis.
- microbiology : Neutrophils.
- physiology : Chemotaxis, Leukocyte, Neutrophils.
- Adult, Cell Migration Inhibition, Humans, Streptococcus pyogenes.
Abstract
To study human neutrophil (polymorphonuclear leukocyte (PMN)) migration and killing of bacteria in an environment similar to that found in inflamed tissues in vivo, we have used fibrin gels. Fibrin gels (1500 microm thick) containing Staphylococcus epidermidis were formed in Boyden-type chemotaxis chambers. PMN migrated < 300 microm into these gels in 6 h and did not kill S. epidermidis when the gels contained heat-inactivated serum, C5-deficient serum, a streptococcal peptidase specific for a fragment of cleaved C5 (C5a), or anti-C5aR IgG. In contrast, in gels containing normal human serum, PMN migrated approximately 1000 microm into the gels in 4 h and into the full thickness of the gels in 6 h, and killed 90% of S. epidermidis in 6 h. fMLP reduced PMN migration into fibrin gels and allowed S. epidermidis to increase by approximately 300% in 4 h, whereas leukotriene B(4) stimulated PMN to migrate the full thickness of the gels and to kill 80% of S. epidermidis in 4 h. We conclude that both complement opsonization and C5a-stimulated chemotaxis are required for PMN bacterial killing in fibrin gels, and that fMLP inhibits PMN bactericidal activity in fibrin gels. The latter finding is surprising and suggests that in the presence of fibrin fMLP promotes bacterial virulence.
DOI: 10.4049/jimmunol.168.2.816
PubMed: 11777977
Links to Exploration step
pubmed:11777977Le document en format XML
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Ember</name></author><author><name sortKey="Cleary, P Patrick" sort="Cleary, P Patrick" uniqKey="Cleary P" first="P Patrick" last="Cleary">P Patrick Cleary</name></author><author><name sortKey="Lu, Emily" sort="Lu, Emily" uniqKey="Lu E" first="Emily" last="Lu">Emily Lu</name></author><author><name sortKey="Budhu, Sadna" sort="Budhu, Sadna" uniqKey="Budhu S" first="Sadna" last="Budhu">Sadna Budhu</name></author><author><name sortKey="Cao, Long" sort="Cao, Long" uniqKey="Cao L" first="Long" last="Cao">Long Cao</name></author><author><name sortKey="Silverstein, Samuel C" sort="Silverstein, Samuel C" uniqKey="Silverstein S" first="Samuel C" last="Silverstein">Samuel C. Silverstein</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2002">2002</date><idno type="RBID">pubmed:11777977</idno><idno type="pmid">11777977</idno><idno type="doi">10.4049/jimmunol.168.2.816</idno><idno type="wicri:Area/Main/Corpus">000C62</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000C62</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The bacterial peptide N-formyl-Met-Leu-Phe inhibits killing of Staphylococcus epidermidis by human neutrophils in fibrin gels.</title><author><name sortKey="Li, Yongmei" sort="Li, Yongmei" uniqKey="Li Y" first="Yongmei" last="Li">Yongmei Li</name><affiliation><nlm:affiliation>Department of Physiology and Cellular Biophysics, Columbia University College of Physicians and Surgeons, New York, NY 10032, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Loike, John D" sort="Loike, John D" uniqKey="Loike J" first="John D" last="Loike">John D. Loike</name></author><author><name sortKey="Ember, Julia A" sort="Ember, Julia A" uniqKey="Ember J" first="Julia A" last="Ember">Julia A. Ember</name></author><author><name sortKey="Cleary, P Patrick" sort="Cleary, P Patrick" uniqKey="Cleary P" first="P Patrick" last="Cleary">P Patrick Cleary</name></author><author><name sortKey="Lu, Emily" sort="Lu, Emily" uniqKey="Lu E" first="Emily" last="Lu">Emily Lu</name></author><author><name sortKey="Budhu, Sadna" sort="Budhu, Sadna" uniqKey="Budhu S" first="Sadna" last="Budhu">Sadna Budhu</name></author><author><name sortKey="Cao, Long" sort="Cao, Long" uniqKey="Cao L" first="Long" last="Cao">Long Cao</name></author><author><name sortKey="Silverstein, Samuel C" sort="Silverstein, Samuel C" uniqKey="Silverstein S" first="Samuel C" last="Silverstein">Samuel C. Silverstein</name></author></analytic><series><title level="j">Journal of immunology (Baltimore, Md. : 1950)</title><idno type="ISSN">0022-1767</idno><imprint><date when="2002" type="published">2002</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adhesins, Bacterial (MeSH)</term><term>Adult (MeSH)</term><term>Bacterial Proteins (pharmacology)</term><term>Cell Migration Inhibition (MeSH)</term><term>Chemotaxis, Leukocyte (drug effects)</term><term>Chemotaxis, Leukocyte (physiology)</term><term>Complement C3 (metabolism)</term><term>Complement C5a (metabolism)</term><term>Complement C5a (pharmacology)</term><term>Complement System Proteins (physiology)</term><term>Endopeptidases (pharmacology)</term><term>Fibrin (MeSH)</term><term>Gels (MeSH)</term><term>Humans (MeSH)</term><term>Immunoglobulin G (metabolism)</term><term>Leukotriene B4 (pharmacology)</term><term>N-Formylmethionine Leucyl-Phenylalanine (analogs & derivatives)</term><term>N-Formylmethionine Leucyl-Phenylalanine (pharmacology)</term><term>Neutrophils (drug effects)</term><term>Neutrophils (enzymology)</term><term>Neutrophils (microbiology)</term><term>Neutrophils (physiology)</term><term>Opsonin Proteins (metabolism)</term><term>Phagocytosis (drug effects)</term><term>Staphylococcus epidermidis (drug effects)</term><term>Staphylococcus epidermidis (growth & development)</term><term>Staphylococcus epidermidis (isolation & purification)</term><term>Streptococcus pyogenes (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>N-Formylmethionine Leucyl-Phenylalanine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Complement C3</term><term>Complement C5a</term><term>Immunoglobulin G</term><term>Opsonin Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Bacterial Proteins</term><term>Complement C5a</term><term>Endopeptidases</term><term>Leukotriene B4</term><term>N-Formylmethionine Leucyl-Phenylalanine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Complement System Proteins</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Adhesins, Bacterial</term><term>Fibrin</term><term>Gels</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Chemotaxis, Leukocyte</term><term>Neutrophils</term><term>Phagocytosis</term><term>Staphylococcus epidermidis</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Neutrophils</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Staphylococcus epidermidis</term></keywords><keywords scheme="MESH" qualifier="isolation & purification" xml:lang="en"><term>Staphylococcus epidermidis</term></keywords><keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Neutrophils</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Chemotaxis, Leukocyte</term><term>Neutrophils</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Adult</term><term>Cell Migration Inhibition</term><term>Humans</term><term>Streptococcus pyogenes</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">To study human neutrophil (polymorphonuclear leukocyte (PMN)) migration and killing of bacteria in an environment similar to that found in inflamed tissues in vivo, we have used fibrin gels. Fibrin gels (1500 microm thick) containing Staphylococcus epidermidis were formed in Boyden-type chemotaxis chambers. PMN migrated < 300 microm into these gels in 6 h and did not kill S. epidermidis when the gels contained heat-inactivated serum, C5-deficient serum, a streptococcal peptidase specific for a fragment of cleaved C5 (C5a), or anti-C5aR IgG. In contrast, in gels containing normal human serum, PMN migrated approximately 1000 microm into the gels in 4 h and into the full thickness of the gels in 6 h, and killed 90% of S. epidermidis in 6 h. fMLP reduced PMN migration into fibrin gels and allowed S. epidermidis to increase by approximately 300% in 4 h, whereas leukotriene B(4) stimulated PMN to migrate the full thickness of the gels and to kill 80% of S. epidermidis in 4 h. We conclude that both complement opsonization and C5a-stimulated chemotaxis are required for PMN bacterial killing in fibrin gels, and that fMLP inhibits PMN bactericidal activity in fibrin gels. The latter finding is surprising and suggests that in the presence of fibrin fMLP promotes bacterial virulence.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11777977</PMID><DateCompleted><Year>2002</Year><Month>01</Month><Day>31</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0022-1767</ISSN><JournalIssue CitedMedium="Print"><Volume>168</Volume><Issue>2</Issue><PubDate><Year>2002</Year><Month>Jan</Month><Day>15</Day></PubDate></JournalIssue><Title>Journal of immunology (Baltimore, Md. : 1950)</Title><ISOAbbreviation>J Immunol</ISOAbbreviation></Journal><ArticleTitle>The bacterial peptide N-formyl-Met-Leu-Phe inhibits killing of Staphylococcus epidermidis by human neutrophils in fibrin gels.</ArticleTitle><Pagination><MedlinePgn>816-24</MedlinePgn></Pagination><Abstract><AbstractText>To study human neutrophil (polymorphonuclear leukocyte (PMN)) migration and killing of bacteria in an environment similar to that found in inflamed tissues in vivo, we have used fibrin gels. Fibrin gels (1500 microm thick) containing Staphylococcus epidermidis were formed in Boyden-type chemotaxis chambers. PMN migrated < 300 microm into these gels in 6 h and did not kill S. epidermidis when the gels contained heat-inactivated serum, C5-deficient serum, a streptococcal peptidase specific for a fragment of cleaved C5 (C5a), or anti-C5aR IgG. In contrast, in gels containing normal human serum, PMN migrated approximately 1000 microm into the gels in 4 h and into the full thickness of the gels in 6 h, and killed 90% of S. epidermidis in 6 h. fMLP reduced PMN migration into fibrin gels and allowed S. epidermidis to increase by approximately 300% in 4 h, whereas leukotriene B(4) stimulated PMN to migrate the full thickness of the gels and to kill 80% of S. epidermidis in 4 h. We conclude that both complement opsonization and C5a-stimulated chemotaxis are required for PMN bacterial killing in fibrin gels, and that fMLP inhibits PMN bactericidal activity in fibrin gels. The latter finding is surprising and suggests that in the presence of fibrin fMLP promotes bacterial virulence.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Yongmei</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Department of Physiology and Cellular Biophysics, Columbia University College of Physicians and Surgeons, New York, NY 10032, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Loike</LastName><ForeName>John D</ForeName><Initials>JD</Initials></Author><Author ValidYN="Y"><LastName>Ember</LastName><ForeName>Julia A</ForeName><Initials>JA</Initials></Author><Author ValidYN="Y"><LastName>Cleary</LastName><ForeName>P Patrick</ForeName><Initials>PP</Initials></Author><Author ValidYN="Y"><LastName>Lu</LastName><ForeName>Emily</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Budhu</LastName><ForeName>Sadna</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Cao</LastName><ForeName>Long</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Silverstein</LastName><ForeName>Samuel C</ForeName><Initials>SC</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>5T32AI-07525</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>AI-20418</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Immunol</MedlineTA><NlmUniqueID>2985117R</NlmUniqueID><ISSNLinking>0022-1767</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018829">Adhesins, Bacterial</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D003176">Complement C3</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005782">Gels</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007074">Immunoglobulin G</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009895">Opsonin Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>1HGW4DR56D</RegistryNumber><NameOfSubstance UI="D007975">Leukotriene B4</NameOfSubstance></Chemical><Chemical><RegistryNumber>59880-97-6</RegistryNumber><NameOfSubstance UI="D009240">N-Formylmethionine Leucyl-Phenylalanine</NameOfSubstance></Chemical><Chemical><RegistryNumber>59881-05-9</RegistryNumber><NameOfSubstance UI="C023976">N-formylmethionyl-methionyl-phenylalanine</NameOfSubstance></Chemical><Chemical><RegistryNumber>80295-54-1</RegistryNumber><NameOfSubstance UI="D015936">Complement C5a</NameOfSubstance></Chemical><Chemical><RegistryNumber>9001-31-4</RegistryNumber><NameOfSubstance UI="D005337">Fibrin</NameOfSubstance></Chemical><Chemical><RegistryNumber>9007-36-7</RegistryNumber><NameOfSubstance UI="D003165">Complement System Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.-</RegistryNumber><NameOfSubstance UI="D010450">Endopeptidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.99.-</RegistryNumber><NameOfSubstance UI="C053088">C5a peptidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>AIM</CitationSubset><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D018829" MajorTopicYN="Y">Adhesins, Bacterial</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000328" MajorTopicYN="N">Adult</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001426" MajorTopicYN="N">Bacterial Proteins</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002464" MajorTopicYN="N">Cell Migration Inhibition</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002634" MajorTopicYN="N">Chemotaxis, Leukocyte</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003176" MajorTopicYN="N">Complement C3</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015936" MajorTopicYN="N">Complement C5a</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003165" MajorTopicYN="N">Complement System Proteins</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010450" MajorTopicYN="N">Endopeptidases</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005337" MajorTopicYN="Y">Fibrin</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005782" MajorTopicYN="N">Gels</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007074" MajorTopicYN="N">Immunoglobulin G</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007975" MajorTopicYN="N">Leukotriene B4</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009240" MajorTopicYN="N">N-Formylmethionine Leucyl-Phenylalanine</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="Y">analogs & derivatives</QualifierName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009504" MajorTopicYN="N">Neutrophils</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009895" MajorTopicYN="N">Opsonin Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010587" MajorTopicYN="N">Phagocytosis</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013212" MajorTopicYN="N">Staphylococcus epidermidis</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName><QualifierName UI="Q000254" MajorTopicYN="Y">growth & development</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013297" MajorTopicYN="N">Streptococcus pyogenes</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2002</Year><Month>1</Month><Day>5</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2002</Year><Month>2</Month><Day>1</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate 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