Covalent conjugation of the equine infectious anemia virus Gag with SUMO.
Abstract: The conjugation of small ubiquitin-like modifier (SUMO) to the target protein, namely, SUMOylation, is involved in the regulation of many important biological events including host-pathogen interaction. Some viruses have evolved to exploit the host SUMOylation machinery to modify their own protein. Retroviral Gag protein plays critical roles in the viral life cycle. The HIV-1 p6 and the Moloney murine leukemia virus CA have been reported to be conjugated with SUMO. In this study, we report for the first time, to our knowledge, the covalent conjugation of equine infectious anemia virus (EIAV) Gag with SUMO. The C-terminal p9 domain of Gag is a main target for SUMOylation and SUMO is attached to multiple sites of p9, including K30 whose mutation abolished p9 SUMOylation completely. The SUMOylation of p9, but not the p9-K30 mutant, was also detected in equine fibroblastic cells ATCC CCL-57™. Ubc9 and its C93 residue are indispensable for the SUMOylation of p9. Using confocal microscopy, it is found that EIAV Gag localizes primarily, if not exclusively, in the cytoplasm of the cell and the co-localization of EIAV Gag with Ubc9 was observed. Our findings that EIAV Gag is SUMOylated at p9-K30, together with previous findings on the defects of p9-K30 mutant in viral DNA translocation from cytoplasm to the nucleus, suggests that SUMOylation of Gag may be involved in such functions.
Copyright © 2017 Elsevier Inc. All rights reserved.
Publication Date: 2017-03-22 PubMed ID: 28342872DOI: 10.1016/j.bbrc.2017.03.103Google Scholar: Lookup
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- Journal Article
Summary
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This research investigates how the equine infectious anemia virus (EIAV) modifies its own proteins using the host’s SUMOylation process, focusing on the Gag protein. The study discovered that SUMOylation of the Gag protein may play a crucial role in viral DNA movement from the cytoplasm to the nucleus.
Understanding SUMOylation and its Role in Viruses
- The conjugation of small ubiquitin-like modifier (SUMO) to a target protein, or SUMOylation, is involved in regulating numerous vital biological events. This includes host-pathogen interactions.
- Some viruses have evolved to exploit the host’s SUMOylation machinery to modify their own proteins.
- The retroviral Gag protein plays critical roles in the lifecycle of a virus. Prior studies have reported the conjugation of HIV-1 p6 and the Moloney murine leukemia virus CA with SUMO.
Focusing on the EIAV Gag Protein
- In this study, the researchers demonstrate that the Gag protein of EIAV can also be conjugated with SUMO. This is the first known instance of this happening.
- The conjugation primarily targets the C-terminal p9 domain of the Gag protein. The research discovered that SUMO is attached to multiple sites on p9, particularly K30. When K30 was mutated, SUMOylation was completely abolished.
- This SUMOylation process occurred in equine fibroblastic cells ATCC CCL-57™.
Role of Ubc9 in Gag SUMOylation
- The protein Ubc9 and its C93 residue are crucial for the SUMOylation of p9. Without this protein and its associated residue, SUMOylation cannot occur.
- This was made evident in the study by using confocal microscopy to study the cells. Researchers observed that EIAV Gag was primarily located in the cytoplasm of the cell and co-localized with Ubc9.
Implication of Gag SUMOylation
- The study’s key finding is that EIAV Gag is reliably SUMOylated at the p9-K30 region. This discovery, along with previous studies suggesting that the p9-K30 mutant is defective in regard to viral DNA transport from the cytoplasm to the nucleus, suggests that SUMOylation of Gag might be associated with such transport functions.
Cite This Article
APA
Wang J, Wen S, Zhao R, Qi J, Liu Z, Li W, An J, Wood C, Wang Y.
(2017).
Covalent conjugation of the equine infectious anemia virus Gag with SUMO.
Biochem Biophys Res Commun, 486(3), 712-719.
https://doi.org/10.1016/j.bbrc.2017.03.103 Publication
Researcher Affiliations
- TEDA Institute of Biological Sciences and Biotechnology, Nankai University, 23 Hongda Street, TEDA, Tianjin 300457, China; Key Laboratory of Molecular Microbiology and Technology, Ministry of Education, 23 Hongda Street, TEDA, Tianjin 300457, China; Tianjin Key Laboratory of Microbial Functional Genomics, 23 Hongda Street, TEDA, Tianjin 300457, China.
- TEDA Institute of Biological Sciences and Biotechnology, Nankai University, 23 Hongda Street, TEDA, Tianjin 300457, China.
- TEDA Institute of Biological Sciences and Biotechnology, Nankai University, 23 Hongda Street, TEDA, Tianjin 300457, China.
- TEDA Institute of Biological Sciences and Biotechnology, Nankai University, 23 Hongda Street, TEDA, Tianjin 300457, China.
- TEDA Institute of Biological Sciences and Biotechnology, Nankai University, 23 Hongda Street, TEDA, Tianjin 300457, China.
- TEDA Institute of Biological Sciences and Biotechnology, Nankai University, 23 Hongda Street, TEDA, Tianjin 300457, China.
- TEDA Institute of Biological Sciences and Biotechnology, Nankai University, 23 Hongda Street, TEDA, Tianjin 300457, China.
- Nebraska Center for Virology and School of Biological Sciences, University of Nebraska, Lincoln, NE 68583, USA. Electronic address: cwood1@unl.edu.
- TEDA Institute of Biological Sciences and Biotechnology, Nankai University, 23 Hongda Street, TEDA, Tianjin 300457, China; Key Laboratory of Molecular Microbiology and Technology, Ministry of Education, 23 Hongda Street, TEDA, Tianjin 300457, China; Tianjin Key Laboratory of Microbial Functional Genomics, 23 Hongda Street, TEDA, Tianjin 300457, China. Electronic address: yingwang@nankai.edu.cn.
MeSH Terms
- Amino Acid Sequence
- Animals
- Cell Line
- Escherichia coli / genetics
- Escherichia coli / metabolism
- Fibroblasts / metabolism
- Fibroblasts / virology
- Gene Expression Regulation
- Gene Products, gag / genetics
- Gene Products, gag / metabolism
- HEK293 Cells
- Horses
- Host-Pathogen Interactions
- Humans
- Infectious Anemia Virus, Equine / genetics
- Infectious Anemia Virus, Equine / metabolism
- Lysine / metabolism
- Mutation
- Protein Domains
- SUMO-1 Protein / genetics
- SUMO-1 Protein / metabolism
- Signal Transduction
- Sumoylation
- Ubiquitin-Conjugating Enzymes / genetics
- Ubiquitin-Conjugating Enzymes / metabolism
Citations
This article has been cited 1 times.- Bussienne C, Marquet R, Paillart JC, Bernacchi S. Post-Translational Modifications of Retroviral HIV-1 Gag Precursors: An Overview of Their Biological Role. Int J Mol Sci 2021 Mar 11;22(6).
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