<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Bradley T</submitter><funding>NIAID NIH HHS</funding><pagination>4663-4673</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC5136304</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>197(12)</volume><pubmed_abstract>The HIV-1 envelope protein (Env) has evolved to subvert the host immune system, hindering viral control by the host. The tryptophan metabolic enzyme kynureninase (KYNU) is mimicked by a portion of the HIV Env gp41 membrane proximal region (MPER) and is cross-reactive with the HIV broadly neutralizing Ab (bnAb) 2F5. Molecular mimicry of host proteins by pathogens can lead to autoimmune disease. In this article, we demonstrate that neither the 2F5 bnAb nor HIV MPER-KYNU cross-reactive Abs elicited by immunization with an MPER peptide-liposome vaccine in 2F5 bnAb V&lt;sub>H&lt;/sub>DJ&lt;sub>H&lt;/sub> and V&lt;sub>L&lt;/sub>J&lt;sub>L&lt;/sub> knock-in mice and rhesus macaques modified KYNU activity or disrupted tissue tryptophan metabolism. Thus, molecular mimicry by HIV-1 Env that promotes the evasion of host ant</pubmed_abstract><journal>Journal of immunology (Baltimore, Md. : 1950)</journal><pubmed_title>HIV-1 Envelope Mimicry of Host Enzyme Kynureninase Does Not Disrupt Tryptophan Metabolism.</pubmed_title><pmcid>PMC5136304</pmcid><funding_grant_id>UM1 AI100645</funding_grant_id><funding_grant_id>P30 AI064518</funding_grant_id><pubmed_authors>Moody MA</pubmed_authors><pubmed_authors>Zhang J</pubmed_authors><pubmed_authors>Verkoczy L</pubmed_authors><pubmed_authors>Bradley T</pubmed_authors><pubmed_authors>Bowman CM</pubmed_authors><pubmed_authors>Zhang R</pubmed_authors><pubmed_authors>Scearce RM</pubmed_authors><pubmed_authors>Ilkayeva O</pubmed_authors><pubmed_authors>Haynes BF</pubmed_authors><pubmed_authors>Liao HX</pubmed_authors><pubmed_authors>Reed SG</pubmed_authors><pubmed_authors>Sutherland LL</pubmed_authors><pubmed_authors>Newgard CB</pubmed_authors><pubmed_authors>Holl TM</pubmed_authors><pubmed_authors>Santra S</pubmed_authors><pubmed_authors>Vandergrift N</pubmed_authors><pubmed_authors>Kelsoe G</pubmed_authors><pubmed_authors>Yang G</pubmed_authors><pubmed_authors>Kepler TB</pubmed_authors><pubmed_authors>Parks R</pubmed_authors><pubmed_authors>Alam SM</pubmed_authors><pubmed_authors>Everitt JI</pubmed_authors><pubmed_authors>McLendon R</pubmed_authors><pubmed_authors>Bouton-Verville H</pubmed_authors><pubmed_authors>Fox CB</pubmed_authors></additional><is_claimable>false</is_claimable><name>HIV-1 Envelope Mimicry of Host Enzyme Kynureninase Does Not Disrupt Tryptophan Metabolism.</name><description>The HIV-1 envelope protein (Env) has evolved to subvert the host immune system, hindering viral control by the host. The tryptophan metabolic enzyme kynureninase (KYNU) is mimicked by a portion of the HIV Env gp41 membrane proximal region (MPER) and is cross-reactive with the HIV broadly neutralizing Ab (bnAb) 2F5. Molecular mimicry of host proteins by pathogens can lead to autoimmune disease. In this article, we demonstrate that neither the 2F5 bnAb nor HIV MPER-KYNU cross-reactive Abs elicited by immunization with an MPER peptide-liposome vaccine in 2F5 bnAb V&lt;sub>H&lt;/sub>DJ&lt;sub>H&lt;/sub> and V&lt;sub>L&lt;/sub>J&lt;sub>L&lt;/sub> knock-in mice and rhesus macaques modified KYNU activity or disrupted tissue tryptophan metabolism. Thus, molecular mimicry by HIV-1 Env that promotes the evasion of host ant</description><dates><release>2016-01-01T00:00:00Z</release><publication>2016 Dec</publication><modification>2026-05-03T22:37:42.676Z</modification><creation>2019-03-27T02:30:42Z</creation></dates><accession>S-EPMC5136304</accession><cross_references><pubmed>27849170</pubmed><doi>10.4049/jimmunol.1601484</doi></cross_references></HashMap>