PRMT5 epigenetically regulates the E3 ubiquitin ligase ITCH to influence lipid accumulation during mycobacterial infection
Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis (TB), triggers enhanced accumulation of lipids to generate foamy macrophages (FMs). This process has been often attributed to the surge in the expression of lipid influx genes with a concomitant decrease in those involved in lipid...
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description | Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis (TB), triggers enhanced accumulation of lipids to generate foamy macrophages (FMs). This process has been often attributed to the surge in the expression of lipid influx genes with a concomitant decrease in those involved in lipid efflux. Here, we define an Mtb-orchestrated modulation of the ubiquitination of lipid accumulation markers to enhance lipid accretion during infection. We find that Mtb infection represses the expression of the E3 ubiquitin ligase, ITCH, resulting in the sustenance of key lipid accrual molecules viz. ADRP and CD36, that are otherwise targeted by ITCH for proteasomal degradation. In line, overexpressing ITCH in Mtb-infected cells was found to suppress Mtb-induced lipid accumulation. Molecular analyses including loss-of-function and ChIP assays demonstrated a role for the concerted action of the transcription factor YY1 and the arginine methyl transferase PRMT5 in restricting the expression of Itch gene by conferring repressive symmetrical H4R3me2 marks on its promoter. Consequently, siRNA-mediated depletion of YY1 or PRMT5 rescued ITCH expression, thereby compromising the levels of Mtb-induced ADRP and CD36 and limiting FM formation during infection. Accumulation of lipids within the host has been implicated as a pro-mycobacterial process that aids in pathogen persistence and dormancy. In line, we found that perturbation of PRMT5 enzyme activity resulted in compromised lipid levels and reduced mycobacterial survival in mouse peritoneal macrophages (ex vivo) and in a therapeutic mouse model of TB infection (in vivo). These findings provide new insights into the role of PRMT5 and YY1 in augmenting mycobacterial pathogenesis. Thus, we posit that our observations could help design novel adjunct therapies and combinatorial drug regimen for effective anti-TB strategies. |
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This process has been often attributed to the surge in the expression of lipid influx genes with a concomitant decrease in those involved in lipid efflux. Here, we define an Mtb-orchestrated modulation of the ubiquitination of lipid accumulation markers to enhance lipid accretion during infection. We find that Mtb infection represses the expression of the E3 ubiquitin ligase, ITCH, resulting in the sustenance of key lipid accrual molecules viz. ADRP and CD36, that are otherwise targeted by ITCH for proteasomal degradation. In line, overexpressing ITCH in Mtb-infected cells was found to suppress Mtb-induced lipid accumulation. Molecular analyses including loss-of-function and ChIP assays demonstrated a role for the concerted action of the transcription factor YY1 and the arginine methyl transferase PRMT5 in restricting the expression of Itch gene by conferring repressive symmetrical H4R3me2 marks on its promoter. Consequently, siRNA-mediated depletion of YY1 or PRMT5 rescued ITCH expression, thereby compromising the levels of Mtb-induced ADRP and CD36 and limiting FM formation during infection. Accumulation of lipids within the host has been implicated as a pro-mycobacterial process that aids in pathogen persistence and dormancy. In line, we found that perturbation of PRMT5 enzyme activity resulted in compromised lipid levels and reduced mycobacterial survival in mouse peritoneal macrophages (ex vivo) and in a therapeutic mouse model of TB infection (in vivo). These findings provide new insights into the role of PRMT5 and YY1 in augmenting mycobacterial pathogenesis. Thus, we posit that our observations could help design novel adjunct therapies and combinatorial drug regimen for effective anti-TB strategies.</description><identifier>ISSN: 1553-7374</identifier><identifier>ISSN: 1553-7366</identifier><identifier>EISSN: 1553-7374</identifier><identifier>DOI: 10.1371/journal.ppat.1010095</identifier><identifier>PMID: 35658060</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Accretion ; Accumulation ; Binding sites ; Biology and Life Sciences ; Biosynthesis ; CD36 antigen ; Cell survival ; Combinatorial analysis ; COVID-19 ; Depletion ; Deposition ; Dormancy ; Drug development ; Efflux ; Enzymatic activity ; Enzyme activity ; Epigenetics ; Gene expression ; Granulomas ; Infections ; Infectious diseases ; Itch gene ; Lipids ; Localization ; Macrophages ; Medicine and Health Sciences ; Microscopy ; Pathogenesis ; Pathogens ; Perturbation ; Proteasomes ; Proteins ; Research and Analysis Methods ; siRNA ; Tuberculosis ; Ubiquitin ; Ubiquitin-protein ligase ; Ubiquitination ; YY1 protein</subject><ispartof>PLoS pathogens, 2022-06, Vol.18 (6), p.e1010095-e1010095</ispartof><rights>2022 Borbora et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2022 Borbora et al 2022 Borbora et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c526t-91e5be8cc7736ebb2749da22fd7ee73fdd68929ea0055d220bb287a151f992873</citedby><cites>FETCH-LOGICAL-c526t-91e5be8cc7736ebb2749da22fd7ee73fdd68929ea0055d220bb287a151f992873</cites><orcidid>0000-0002-0006-5707</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC9200362/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC9200362/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2101,2927,23865,27923,27924,53790,53792,79471,79472</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/35658060$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Sassetti, Christopher M.</contributor><creatorcontrib>Borbora, Salik Miskat</creatorcontrib><creatorcontrib>Rajmani, Raju S</creatorcontrib><creatorcontrib>Balaji, Kithiganahalli Narayanaswamy</creatorcontrib><title>PRMT5 epigenetically regulates the E3 ubiquitin ligase ITCH to influence lipid accumulation during mycobacterial infection</title><title>PLoS pathogens</title><addtitle>PLoS Pathog</addtitle><description>Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis (TB), triggers enhanced accumulation of lipids to generate foamy macrophages (FMs). This process has been often attributed to the surge in the expression of lipid influx genes with a concomitant decrease in those involved in lipid efflux. Here, we define an Mtb-orchestrated modulation of the ubiquitination of lipid accumulation markers to enhance lipid accretion during infection. We find that Mtb infection represses the expression of the E3 ubiquitin ligase, ITCH, resulting in the sustenance of key lipid accrual molecules viz. ADRP and CD36, that are otherwise targeted by ITCH for proteasomal degradation. In line, overexpressing ITCH in Mtb-infected cells was found to suppress Mtb-induced lipid accumulation. Molecular analyses including loss-of-function and ChIP assays demonstrated a role for the concerted action of the transcription factor YY1 and the arginine methyl transferase PRMT5 in restricting the expression of Itch gene by conferring repressive symmetrical H4R3me2 marks on its promoter. Consequently, siRNA-mediated depletion of YY1 or PRMT5 rescued ITCH expression, thereby compromising the levels of Mtb-induced ADRP and CD36 and limiting FM formation during infection. Accumulation of lipids within the host has been implicated as a pro-mycobacterial process that aids in pathogen persistence and dormancy. In line, we found that perturbation of PRMT5 enzyme activity resulted in compromised lipid levels and reduced mycobacterial survival in mouse peritoneal macrophages (ex vivo) and in a therapeutic mouse model of TB infection (in vivo). These findings provide new insights into the role of PRMT5 and YY1 in augmenting mycobacterial pathogenesis. Thus, we posit that our observations could help design novel adjunct therapies and combinatorial drug regimen for effective anti-TB strategies.</description><subject>Accretion</subject><subject>Accumulation</subject><subject>Binding sites</subject><subject>Biology and Life Sciences</subject><subject>Biosynthesis</subject><subject>CD36 antigen</subject><subject>Cell survival</subject><subject>Combinatorial analysis</subject><subject>COVID-19</subject><subject>Depletion</subject><subject>Deposition</subject><subject>Dormancy</subject><subject>Drug development</subject><subject>Efflux</subject><subject>Enzymatic activity</subject><subject>Enzyme activity</subject><subject>Epigenetics</subject><subject>Gene expression</subject><subject>Granulomas</subject><subject>Infections</subject><subject>Infectious diseases</subject><subject>Itch gene</subject><subject>Lipids</subject><subject>Localization</subject><subject>Macrophages</subject><subject>Medicine and Health Sciences</subject><subject>Microscopy</subject><subject>Pathogenesis</subject><subject>Pathogens</subject><subject>Perturbation</subject><subject>Proteasomes</subject><subject>Proteins</subject><subject>Research and Analysis Methods</subject><subject>siRNA</subject><subject>Tuberculosis</subject><subject>Ubiquitin</subject><subject>Ubiquitin-protein ligase</subject><subject>Ubiquitination</subject><subject>YY1 protein</subject><issn>1553-7374</issn><issn>1553-7366</issn><issn>1553-7374</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>DOA</sourceid><recordid>eNptUltrFDEUHkSxtfoPRAO--LJrLpNk5kUopepCRZH6HM4kZ6ZZspNpMiOsv94Zd1ta8SmHfJdz4SuK14yumdDswzZOqYewHgYY14wySmv5pDhlUoqVFrp8-qA-KV7kvKW0ZIKp58WJkEpWVNHT4vf3H1-vJcHBd9jj6C2EsCcJuynAiJmMN0guBZkafzv50fck-A4yks31xRcyRuL7NkzYW5yBwTsC1k67RetjT9yUfN-R3d7GBuyIyUNYFGgX-GXxrIWQ8dXxPSt-frqcbVdX3z5vLs6vVlZyNa5qhrLBylqthcKm4bqsHXDeOo2oReucqmpeI1AqpeOczpRKA5Osreu5EmfF24PvEGI2x7Nlw1VNNedMy5mxOTBchK0Zkt9B2psI3vz9iKkzkObbBDQKQeoSSsorVlLKalTMQeUcU1o0sHh9PHabmh06i_2YIDwyfYz0_sZ08ZepOaVC8dng_dEgxdsJ82h2PlsMAXqM0zK3FrLWlVQz9d0_1P9vVx5YNsWcE7b3wzBqlijdqcwSJXOM0ix783CRe9FddsQfMuDInA</recordid><startdate>20220601</startdate><enddate>20220601</enddate><creator>Borbora, Salik Miskat</creator><creator>Rajmani, Raju S</creator><creator>Balaji, Kithiganahalli Narayanaswamy</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>COVID</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope><orcidid>https://orcid.org/0000-0002-0006-5707</orcidid></search><sort><creationdate>20220601</creationdate><title>PRMT5 epigenetically regulates the E3 ubiquitin ligase ITCH to influence lipid accumulation during mycobacterial infection</title><author>Borbora, Salik Miskat ; Rajmani, Raju S ; Balaji, Kithiganahalli Narayanaswamy</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c526t-91e5be8cc7736ebb2749da22fd7ee73fdd68929ea0055d220bb287a151f992873</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Accretion</topic><topic>Accumulation</topic><topic>Binding sites</topic><topic>Biology and Life Sciences</topic><topic>Biosynthesis</topic><topic>CD36 antigen</topic><topic>Cell survival</topic><topic>Combinatorial analysis</topic><topic>COVID-19</topic><topic>Depletion</topic><topic>Deposition</topic><topic>Dormancy</topic><topic>Drug development</topic><topic>Efflux</topic><topic>Enzymatic activity</topic><topic>Enzyme activity</topic><topic>Epigenetics</topic><topic>Gene expression</topic><topic>Granulomas</topic><topic>Infections</topic><topic>Infectious diseases</topic><topic>Itch gene</topic><topic>Lipids</topic><topic>Localization</topic><topic>Macrophages</topic><topic>Medicine and Health Sciences</topic><topic>Microscopy</topic><topic>Pathogenesis</topic><topic>Pathogens</topic><topic>Perturbation</topic><topic>Proteasomes</topic><topic>Proteins</topic><topic>Research and Analysis Methods</topic><topic>siRNA</topic><topic>Tuberculosis</topic><topic>Ubiquitin</topic><topic>Ubiquitin-protein ligase</topic><topic>Ubiquitination</topic><topic>YY1 protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Borbora, Salik Miskat</creatorcontrib><creatorcontrib>Rajmani, Raju S</creatorcontrib><creatorcontrib>Balaji, Kithiganahalli Narayanaswamy</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>Coronavirus Research Database</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PLoS pathogens</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Borbora, Salik Miskat</au><au>Rajmani, Raju S</au><au>Balaji, Kithiganahalli Narayanaswamy</au><au>Sassetti, Christopher M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>PRMT5 epigenetically regulates the E3 ubiquitin ligase ITCH to influence lipid accumulation during mycobacterial infection</atitle><jtitle>PLoS pathogens</jtitle><addtitle>PLoS Pathog</addtitle><date>2022-06-01</date><risdate>2022</risdate><volume>18</volume><issue>6</issue><spage>e1010095</spage><epage>e1010095</epage><pages>e1010095-e1010095</pages><issn>1553-7374</issn><issn>1553-7366</issn><eissn>1553-7374</eissn><abstract>Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis (TB), triggers enhanced accumulation of lipids to generate foamy macrophages (FMs). This process has been often attributed to the surge in the expression of lipid influx genes with a concomitant decrease in those involved in lipid efflux. Here, we define an Mtb-orchestrated modulation of the ubiquitination of lipid accumulation markers to enhance lipid accretion during infection. We find that Mtb infection represses the expression of the E3 ubiquitin ligase, ITCH, resulting in the sustenance of key lipid accrual molecules viz. ADRP and CD36, that are otherwise targeted by ITCH for proteasomal degradation. In line, overexpressing ITCH in Mtb-infected cells was found to suppress Mtb-induced lipid accumulation. Molecular analyses including loss-of-function and ChIP assays demonstrated a role for the concerted action of the transcription factor YY1 and the arginine methyl transferase PRMT5 in restricting the expression of Itch gene by conferring repressive symmetrical H4R3me2 marks on its promoter. Consequently, siRNA-mediated depletion of YY1 or PRMT5 rescued ITCH expression, thereby compromising the levels of Mtb-induced ADRP and CD36 and limiting FM formation during infection. Accumulation of lipids within the host has been implicated as a pro-mycobacterial process that aids in pathogen persistence and dormancy. In line, we found that perturbation of PRMT5 enzyme activity resulted in compromised lipid levels and reduced mycobacterial survival in mouse peritoneal macrophages (ex vivo) and in a therapeutic mouse model of TB infection (in vivo). These findings provide new insights into the role of PRMT5 and YY1 in augmenting mycobacterial pathogenesis. Thus, we posit that our observations could help design novel adjunct therapies and combinatorial drug regimen for effective anti-TB strategies.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>35658060</pmid><doi>10.1371/journal.ppat.1010095</doi><orcidid>https://orcid.org/0000-0002-0006-5707</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | Accretion Accumulation Binding sites Biology and Life Sciences Biosynthesis CD36 antigen Cell survival Combinatorial analysis COVID-19 Depletion Deposition Dormancy Drug development Efflux Enzymatic activity Enzyme activity Epigenetics Gene expression Granulomas Infections Infectious diseases Itch gene Lipids Localization Macrophages Medicine and Health Sciences Microscopy Pathogenesis Pathogens Perturbation Proteasomes Proteins Research and Analysis Methods siRNA Tuberculosis Ubiquitin Ubiquitin-protein ligase Ubiquitination YY1 protein |
title | PRMT5 epigenetically regulates the E3 ubiquitin ligase ITCH to influence lipid accumulation during mycobacterial infection |
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