Differential Abundance of Protein Acylation in Mycobacterium tuberculosis Under Exposure to Nitrosative Stress
ABSTRACT Background: Human macrophages generate antimicrobial reactive nitrogen species in response to infection by Mycobacterium tuberculosis (Mtb). Exposure to these redox‐reactive compounds induces stress response in Mtb, which can affect posttranslational modifications (PTM). Methods: Here, we p...
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| Veröffentlicht in: | Proteomics. Clinical applications 2024-11, Vol.18 (6), p.e202300212-n/a |
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Background: Human macrophages generate antimicrobial reactive nitrogen species in response to infection by Mycobacterium tuberculosis (Mtb). Exposure to these redox‐reactive compounds induces stress response in Mtb, which can affect posttranslational modifications (PTM). Methods: Here, we present the global analysis of the PTM acylation of Mtb proteins in response to a sublethal dose of nitrosative stress in the form of nitric oxide (NO) using label free quantification. Results: A total of 6437 acylation events were identified on 1496 Mtb proteins, and O‐acylation accounted for 92.2% of the events identified, while 7.8% were N‐acylation events. About 22% of the sites identified were found to be acylated by more than one acyl‐group. Furthermore, the abundance of each acyl‐group decreased as their molecular weight increased. Quantitative PTM analysis revealed differential abundance of acylation in proteins involved in stress response, iron ion homeostasis, growth, energy metabolism, and antimicrobial resistance (AMR) induced by nitrosative stress over time. Conclusions: The results reveal a potential role of Mtb protein acylation in the bacterial stress responses and AMR. To our knowledge, this is the first report on global O‐acylation profile of Mtb in response to NO. This will significantly improve our understanding of the changes in Mtb acylation under nitrosative stress, highly relevant for global health. |
| doi_str_mv | 10.1002/prca.202300212 |
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Background: Human macrophages generate antimicrobial reactive nitrogen species in response to infection by Mycobacterium tuberculosis (Mtb). Exposure to these redox‐reactive compounds induces stress response in Mtb, which can affect posttranslational modifications (PTM). Methods: Here, we present the global analysis of the PTM acylation of Mtb proteins in response to a sublethal dose of nitrosative stress in the form of nitric oxide (NO) using label free quantification. Results: A total of 6437 acylation events were identified on 1496 Mtb proteins, and O‐acylation accounted for 92.2% of the events identified, while 7.8% were N‐acylation events. About 22% of the sites identified were found to be acylated by more than one acyl‐group. Furthermore, the abundance of each acyl‐group decreased as their molecular weight increased. Quantitative PTM analysis revealed differential abundance of acylation in proteins involved in stress response, iron ion homeostasis, growth, energy metabolism, and antimicrobial resistance (AMR) induced by nitrosative stress over time. Conclusions: The results reveal a potential role of Mtb protein acylation in the bacterial stress responses and AMR. To our knowledge, this is the first report on global O‐acylation profile of Mtb in response to NO. This will significantly improve our understanding of the changes in Mtb acylation under nitrosative stress, highly relevant for global health.</description><identifier>ISSN: 1862-8346</identifier><identifier>ISSN: 1862-8354</identifier><identifier>EISSN: 1862-8354</identifier><identifier>DOI: 10.1002/prca.202300212</identifier><identifier>PMID: 39082596</identifier><language>eng</language><publisher>Germany: Wiley Subscription Services, Inc</publisher><subject>Acylation ; Antimicrobial agents ; Antimicrobial resistance ; Bacterial Proteins - metabolism ; Cellular stress response ; Energy metabolism ; Homeostasis ; Humans ; Macrophages ; mass spectrometry ; Molecular weight ; Mycobacterium tuberculosis ; Mycobacterium tuberculosis - drug effects ; Mycobacterium tuberculosis - metabolism ; Nitric oxide ; Nitric Oxide - metabolism ; nitrosative stress ; Nitrosative Stress - drug effects ; posttranslational modifications ; protein acylation ; Protein Processing, Post-Translational ; Protein turnover ; Proteins ; Public health ; Reactive nitrogen species ; Sublethal dosage ; Tuberculosis</subject><ispartof>Proteomics. Clinical applications, 2024-11, Vol.18 (6), p.e202300212-n/a</ispartof><rights>2024 The Author(s). PROTEOMICS ‐ Clinical Applications published by Wiley‐VCH GmbH.</rights><rights>2024. This article is published under http://creativecommons.org/licenses/by-nc-nd/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>info:eu-repo/semantics/openAccess</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c3185-d84017ee170aca2d43f7ad31bdd6f9c939b7d823456a81b387ebc89c782c88733</cites><orcidid>0000-0001-5302-0919 ; 0000-0002-9759-5316 ; 0000-0002-1709-6921</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fprca.202300212$$EPDF$$P50$$Gwiley$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fprca.202300212$$EHTML$$P50$$Gwiley$$Hfree_for_read</linktohtml><link.rule.ids>230,314,778,782,883,1414,26550,27907,27908,45557,45558</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/39082596$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Birhanu, Alemayehu Godana</creatorcontrib><creatorcontrib>Riaz, Tahira</creatorcontrib><creatorcontrib>Støen, Mari</creatorcontrib><creatorcontrib>Tønjum, Tone</creatorcontrib><title>Differential Abundance of Protein Acylation in Mycobacterium tuberculosis Under Exposure to Nitrosative Stress</title><title>Proteomics. Clinical applications</title><addtitle>Proteomics Clin Appl</addtitle><description>ABSTRACT
Background: Human macrophages generate antimicrobial reactive nitrogen species in response to infection by Mycobacterium tuberculosis (Mtb). Exposure to these redox‐reactive compounds induces stress response in Mtb, which can affect posttranslational modifications (PTM). Methods: Here, we present the global analysis of the PTM acylation of Mtb proteins in response to a sublethal dose of nitrosative stress in the form of nitric oxide (NO) using label free quantification. Results: A total of 6437 acylation events were identified on 1496 Mtb proteins, and O‐acylation accounted for 92.2% of the events identified, while 7.8% were N‐acylation events. About 22% of the sites identified were found to be acylated by more than one acyl‐group. Furthermore, the abundance of each acyl‐group decreased as their molecular weight increased. Quantitative PTM analysis revealed differential abundance of acylation in proteins involved in stress response, iron ion homeostasis, growth, energy metabolism, and antimicrobial resistance (AMR) induced by nitrosative stress over time. Conclusions: The results reveal a potential role of Mtb protein acylation in the bacterial stress responses and AMR. To our knowledge, this is the first report on global O‐acylation profile of Mtb in response to NO. This will significantly improve our understanding of the changes in Mtb acylation under nitrosative stress, highly relevant for global health.</description><subject>Acylation</subject><subject>Antimicrobial agents</subject><subject>Antimicrobial resistance</subject><subject>Bacterial Proteins - metabolism</subject><subject>Cellular stress response</subject><subject>Energy metabolism</subject><subject>Homeostasis</subject><subject>Humans</subject><subject>Macrophages</subject><subject>mass spectrometry</subject><subject>Molecular weight</subject><subject>Mycobacterium tuberculosis</subject><subject>Mycobacterium tuberculosis - drug effects</subject><subject>Mycobacterium tuberculosis - metabolism</subject><subject>Nitric oxide</subject><subject>Nitric Oxide - metabolism</subject><subject>nitrosative stress</subject><subject>Nitrosative Stress - drug effects</subject><subject>posttranslational modifications</subject><subject>protein acylation</subject><subject>Protein Processing, Post-Translational</subject><subject>Protein turnover</subject><subject>Proteins</subject><subject>Public health</subject><subject>Reactive nitrogen species</subject><subject>Sublethal dosage</subject><subject>Tuberculosis</subject><issn>1862-8346</issn><issn>1862-8354</issn><issn>1862-8354</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><sourceid>24P</sourceid><sourceid>WIN</sourceid><sourceid>EIF</sourceid><sourceid>3HK</sourceid><recordid>eNqFkb1vFDEQxS1EREKgpUSWaGju4o_dtV2eLgkghSQCUltee1ZytGcf_gDuv4_DJVfQUM086TfvafQQekfJkhLCzrbJmiUjjDdB2Qt0QuXAFpL33cvD3g3H6HXO94T0HRPkFTrmikjWq-EEhXM_TZAgFG9mvBprcCZYwHHCtykW8AGv7G42xceAm_i6s3E0tkDydYNLHSHZOsfsM74LDhK--LONuSbAJeJrX1LM7fYX4O8lQc5v0NFk5gxvn-Ypuru8-LH-vLi6-fRlvbpaWE5lv3CyI1QAUEGMNcx1fBLGcTo6N0zKKq5G4STjXT8YSUcuBYxWKisks1IKzk8R3vva5HPxQYeYjKZE9kxT2tO_yMc9sk3xZ4Vc9MZnC_NsAsSaNSdy4JIrSRr64R_0PtYU2gOaUyYZVWJQjVo-Z8acE0x6m_zGpF3L1Y9l6cey9KGsdvD-ybaOG3AH_LmdBnR74LefYfcfO337bb1qe88fAIwfnys</recordid><startdate>202411</startdate><enddate>202411</enddate><creator>Birhanu, Alemayehu Godana</creator><creator>Riaz, Tahira</creator><creator>Støen, Mari</creator><creator>Tønjum, Tone</creator><general>Wiley Subscription Services, Inc</general><general>Wiley-Interscience Publishers</general><scope>24P</scope><scope>WIN</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>3HK</scope><orcidid>https://orcid.org/0000-0001-5302-0919</orcidid><orcidid>https://orcid.org/0000-0002-9759-5316</orcidid><orcidid>https://orcid.org/0000-0002-1709-6921</orcidid></search><sort><creationdate>202411</creationdate><title>Differential Abundance of Protein Acylation in Mycobacterium tuberculosis Under Exposure to Nitrosative Stress</title><author>Birhanu, Alemayehu Godana ; Riaz, Tahira ; Støen, Mari ; Tønjum, Tone</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3185-d84017ee170aca2d43f7ad31bdd6f9c939b7d823456a81b387ebc89c782c88733</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>Acylation</topic><topic>Antimicrobial agents</topic><topic>Antimicrobial resistance</topic><topic>Bacterial Proteins - metabolism</topic><topic>Cellular stress response</topic><topic>Energy metabolism</topic><topic>Homeostasis</topic><topic>Humans</topic><topic>Macrophages</topic><topic>mass spectrometry</topic><topic>Molecular weight</topic><topic>Mycobacterium tuberculosis</topic><topic>Mycobacterium tuberculosis - drug effects</topic><topic>Mycobacterium tuberculosis - metabolism</topic><topic>Nitric oxide</topic><topic>Nitric Oxide - metabolism</topic><topic>nitrosative stress</topic><topic>Nitrosative Stress - drug effects</topic><topic>posttranslational modifications</topic><topic>protein acylation</topic><topic>Protein Processing, Post-Translational</topic><topic>Protein turnover</topic><topic>Proteins</topic><topic>Public health</topic><topic>Reactive nitrogen species</topic><topic>Sublethal dosage</topic><topic>Tuberculosis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Birhanu, Alemayehu Godana</creatorcontrib><creatorcontrib>Riaz, Tahira</creatorcontrib><creatorcontrib>Støen, Mari</creatorcontrib><creatorcontrib>Tønjum, Tone</creatorcontrib><collection>Wiley Online Library Open Access</collection><collection>Wiley Free Content</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>NORA - Norwegian Open Research Archives</collection><jtitle>Proteomics. Clinical applications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Birhanu, Alemayehu Godana</au><au>Riaz, Tahira</au><au>Støen, Mari</au><au>Tønjum, Tone</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Differential Abundance of Protein Acylation in Mycobacterium tuberculosis Under Exposure to Nitrosative Stress</atitle><jtitle>Proteomics. Clinical applications</jtitle><addtitle>Proteomics Clin Appl</addtitle><date>2024-11</date><risdate>2024</risdate><volume>18</volume><issue>6</issue><spage>e202300212</spage><epage>n/a</epage><pages>e202300212-n/a</pages><issn>1862-8346</issn><issn>1862-8354</issn><eissn>1862-8354</eissn><abstract>ABSTRACT
Background: Human macrophages generate antimicrobial reactive nitrogen species in response to infection by Mycobacterium tuberculosis (Mtb). Exposure to these redox‐reactive compounds induces stress response in Mtb, which can affect posttranslational modifications (PTM). Methods: Here, we present the global analysis of the PTM acylation of Mtb proteins in response to a sublethal dose of nitrosative stress in the form of nitric oxide (NO) using label free quantification. Results: A total of 6437 acylation events were identified on 1496 Mtb proteins, and O‐acylation accounted for 92.2% of the events identified, while 7.8% were N‐acylation events. About 22% of the sites identified were found to be acylated by more than one acyl‐group. Furthermore, the abundance of each acyl‐group decreased as their molecular weight increased. Quantitative PTM analysis revealed differential abundance of acylation in proteins involved in stress response, iron ion homeostasis, growth, energy metabolism, and antimicrobial resistance (AMR) induced by nitrosative stress over time. Conclusions: The results reveal a potential role of Mtb protein acylation in the bacterial stress responses and AMR. To our knowledge, this is the first report on global O‐acylation profile of Mtb in response to NO. This will significantly improve our understanding of the changes in Mtb acylation under nitrosative stress, highly relevant for global health.</abstract><cop>Germany</cop><pub>Wiley Subscription Services, Inc</pub><pmid>39082596</pmid><doi>10.1002/prca.202300212</doi><tpages>15</tpages><orcidid>https://orcid.org/0000-0001-5302-0919</orcidid><orcidid>https://orcid.org/0000-0002-9759-5316</orcidid><orcidid>https://orcid.org/0000-0002-1709-6921</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Acylation Antimicrobial agents Antimicrobial resistance Bacterial Proteins - metabolism Cellular stress response Energy metabolism Homeostasis Humans Macrophages mass spectrometry Molecular weight Mycobacterium tuberculosis Mycobacterium tuberculosis - drug effects Mycobacterium tuberculosis - metabolism Nitric oxide Nitric Oxide - metabolism nitrosative stress Nitrosative Stress - drug effects posttranslational modifications protein acylation Protein Processing, Post-Translational Protein turnover Proteins Public health Reactive nitrogen species Sublethal dosage Tuberculosis |
| title | Differential Abundance of Protein Acylation in Mycobacterium tuberculosis Under Exposure to Nitrosative Stress |
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