Comprehensive SUMO Proteomic Analyses Identify HIV Latency-Associated Proteins in Microglia
SUMOylation, the post-translational modification of proteins by small ubiquitin-like modifiers, plays a critical role in regulating various cellular processes, including innate immunity. This modification is essential for modulating immune responses and influencing signaling pathways that govern the...
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| Format: | Article |
| Language: | English |
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MDPI AG
2025-02-01
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| Series: | Cells |
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| Online Access: | https://www.mdpi.com/2073-4409/14/3/235 |
| _version_ | 1826806280645246976 |
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| author | Fergan Imbert Dianne Langford |
| author_facet | Fergan Imbert Dianne Langford |
| author_sort | Fergan Imbert |
| collection | DOAJ |
| description | SUMOylation, the post-translational modification of proteins by small ubiquitin-like modifiers, plays a critical role in regulating various cellular processes, including innate immunity. This modification is essential for modulating immune responses and influencing signaling pathways that govern the activation and function of immune cells. Recent studies suggest that SUMOylation also contributes to the pathophysiology of central nervous system (CNS) viral infections, where it contributes to the host response and viral replication dynamics. Here, we explore the multifaceted role of SUMOylation in innate immune signaling and its implications for viral infections within the CNS. Notably, we present novel proteomic analyses aimed at elucidating the role of the small ubiquitin-related modifier (SUMO) in human immunodeficiency virus (HIV) latency in microglial cells. Our findings indicate that SUMOylation may regulate key proteins involved in maintaining viral latency, suggesting a potential mechanism by which HIV evades immune detection in the CNS. By integrating insights from proteomics with functional studies, we anticipate these findings to be the groundwork for future studies on HIV–host interactions and the mechanisms that underlie SUMOylation during latent and productive infection. |
| first_indexed | 2025-02-16T00:06:44Z |
| format | Article |
| id | doaj.art-fbc329b788de4eb1831809f1bee0bb3b |
| institution | Directory Open Access Journal |
| issn | 2073-4409 |
| language | English |
| last_indexed | 2025-02-16T00:06:44Z |
| publishDate | 2025-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Cells |
| spelling | doaj.art-fbc329b788de4eb1831809f1bee0bb3b2025-02-12T14:32:44ZengMDPI AGCells2073-44092025-02-0114323510.3390/cells14030235Comprehensive SUMO Proteomic Analyses Identify HIV Latency-Associated Proteins in MicrogliaFergan Imbert0Dianne Langford1Department of Neuroscience, Lewis Katz School of Medicine, Temple University, Philadelphia, PA 19140, USADepartment of Cell Biology and Neuroscience, Rowan-Virtua School of Translational Biomedical Engineering and Sciences, Stratford, NJ 08084, USASUMOylation, the post-translational modification of proteins by small ubiquitin-like modifiers, plays a critical role in regulating various cellular processes, including innate immunity. This modification is essential for modulating immune responses and influencing signaling pathways that govern the activation and function of immune cells. Recent studies suggest that SUMOylation also contributes to the pathophysiology of central nervous system (CNS) viral infections, where it contributes to the host response and viral replication dynamics. Here, we explore the multifaceted role of SUMOylation in innate immune signaling and its implications for viral infections within the CNS. Notably, we present novel proteomic analyses aimed at elucidating the role of the small ubiquitin-related modifier (SUMO) in human immunodeficiency virus (HIV) latency in microglial cells. Our findings indicate that SUMOylation may regulate key proteins involved in maintaining viral latency, suggesting a potential mechanism by which HIV evades immune detection in the CNS. By integrating insights from proteomics with functional studies, we anticipate these findings to be the groundwork for future studies on HIV–host interactions and the mechanisms that underlie SUMOylation during latent and productive infection.https://www.mdpi.com/2073-4409/14/3/235SUMOylationHIVmicrogliapost-translational modificationsCNS |
| spellingShingle | Fergan Imbert Dianne Langford Comprehensive SUMO Proteomic Analyses Identify HIV Latency-Associated Proteins in Microglia Cells SUMOylation HIV microglia post-translational modifications CNS |
| title | Comprehensive SUMO Proteomic Analyses Identify HIV Latency-Associated Proteins in Microglia |
| title_full | Comprehensive SUMO Proteomic Analyses Identify HIV Latency-Associated Proteins in Microglia |
| title_fullStr | Comprehensive SUMO Proteomic Analyses Identify HIV Latency-Associated Proteins in Microglia |
| title_full_unstemmed | Comprehensive SUMO Proteomic Analyses Identify HIV Latency-Associated Proteins in Microglia |
| title_short | Comprehensive SUMO Proteomic Analyses Identify HIV Latency-Associated Proteins in Microglia |
| title_sort | comprehensive sumo proteomic analyses identify hiv latency associated proteins in microglia |
| topic | SUMOylation HIV microglia post-translational modifications CNS |
| url | https://www.mdpi.com/2073-4409/14/3/235 |
| work_keys_str_mv | AT ferganimbert comprehensivesumoproteomicanalysesidentifyhivlatencyassociatedproteinsinmicroglia AT diannelangford comprehensivesumoproteomicanalysesidentifyhivlatencyassociatedproteinsinmicroglia |