<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Vasquez MT</submitter><funding>HHS | NIH | National Institute of General Medical Sciences</funding><funding>NIAID NIH HHS</funding><funding>Burroughs Wellcome Fund</funding><funding>Cystic Fibrosis Foundation</funding><funding>NCI NIH HHS</funding><funding>HHS | NIH | National Institute of Allergy and Infectious Diseases</funding><funding>Department of Health, Australian Government | National Health and Medical Research Council</funding><funding>NIGMS NIH HHS</funding><pagination>17241-17250</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC7863875</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>295(50)</volume><pubmed_abstract>Leukocidin ED (LukED) is a pore-forming toxin produced by &lt;i>Staphylococcus aureus&lt;/i>, which lyses host cells and promotes virulence of the bacteria. LukED enables &lt;i>S. aureus&lt;/i> to acquire iron by lysing erythrocytes, which depends on targeting the host receptor Duffy antigen receptor for chemokines (DARC). The toxin also targets DARC on the endothelium, contributing to the lethality observed during bloodstream infection in mice. LukED is comprised of two monomers: LukE and LukD. LukE binds to DARC and facilitates hemolysis, but the closely related Panton-Valentine leukocidin S (LukS-PV) does not bind to DARC and is not hemolytic. The interaction of LukE with DARC and the role this plays in hemolysis are incompletely characterized. To determine the domain(s) of LukE that are critical f</pubmed_abstract><journal>The Journal of biological chemistry</journal><pubmed_title>Identification of a domain critical for &lt;i>Staphylococcus aureus&lt;/i> LukED receptor targeting and lysis of erythrocytes.</pubmed_title><pmcid>PMC7863875</pmcid><funding_grant_id>HHSN272201400019C</funding_grant_id><funding_grant_id>F31 AI112290</funding_grant_id><funding_grant_id>R01 AI105129</funding_grant_id><funding_grant_id>T32 GM007308</funding_grant_id><funding_grant_id>LACEY19F0</funding_grant_id><funding_grant_id>R01AI105129</funding_grant_id><funding_grant_id>F30 AI124606</funding_grant_id><funding_grant_id>T32 AI007180 and F31 AI112290</funding_grant_id><funding_grant_id>1013513</funding_grant_id><funding_grant_id>P30 CA016087</funding_grant_id><funding_grant_id>1138466</funding_grant_id><funding_grant_id>R01 AI105129-04S1</funding_grant_id><funding_grant_id>T32 AI007180</funding_grant_id><pubmed_authors>Reyes-Robles T</pubmed_authors><pubmed_authors>Torres VJ</pubmed_authors><pubmed_authors>Jennings MP</pubmed_authors><pubmed_authors>Lacey KA</pubmed_authors><pubmed_authors>Vasquez MT</pubmed_authors><pubmed_authors>Lubkin A</pubmed_authors><pubmed_authors>Day CJ</pubmed_authors></additional><is_claimable>false</is_claimable><name>Identification of a domain critical for &lt;i>Staphylococcus aureus&lt;/i> LukED receptor targeting and lysis of erythrocytes.</name><description>Leukocidin ED (LukED) is a pore-forming toxin produced by &lt;i>Staphylococcus aureus&lt;/i>, which lyses host cells and promotes virulence of the bacteria. LukED enables &lt;i>S. aureus&lt;/i> to acquire iron by lysing erythrocytes, which depends on targeting the host receptor Duffy antigen receptor for chemokines (DARC). The toxin also targets DARC on the endothelium, contributing to the lethality observed during bloodstream infection in mice. LukED is comprised of two monomers: LukE and LukD. LukE binds to DARC and facilitates hemolysis, but the closely related Panton-Valentine leukocidin S (LukS-PV) does not bind to DARC and is not hemolytic. The interaction of LukE with DARC and the role this plays in hemolysis are incompletely characterized. To determine the domain(s) of LukE that are critical f</description><dates><release>2020-01-01T00:00:00Z</release><publication>2020 Dec</publication><modification>2026-05-02T11:43:06.679Z</modification><creation>2022-02-11T12:05:14.828Z</creation></dates><accession>S-EPMC7863875</accession><cross_references><pubmed>33051210</pubmed><doi>10.1074/jbc.ra120.015757</doi><doi>10.1074/jbc.RA120.015757</doi></cross_references></HashMap>