Functional 20S Proteasomes in Retroviruses: Evidence in Favor

被引:0
作者
Morozov, Vladimir [1 ]
Morozov, Alexey [2 ]
Karpov, Vadim L. [2 ]
机构
[1] Robert Koch Inst, Dept Infect Dis, D-13353 Berlin, Germany
[2] Russian Acad Sci, Engelhardt Inst Mol Biol, Vavilov St 32, Moscow 119991, Russia
基金
俄罗斯科学基金会;
关键词
functional proteasomes; proteasome subunits; retroviruses; fractions; extracellular vesicles; viral cargo; PROTEOMIC ANALYSIS; CYCLOPHILIN-A; CELLULAR-PROTEINS; HIV-1; LOCALIZATION; DEGRADATION; PARTICLES; REGULATOR; REVEALS;
D O I
10.3390/ijms252111710
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Proteasomes are barrel-like cellular protein complexes responsible for the degradation of most intracellular proteins. Earlier, it has been shown that during assembly, hundreds of different cellular proteins are incorporated into retro-and herpes viruses. Among detected cellular proteins, there were different proteasome subunits (PS). Previous reports postulated the incorporation of 20S proteasome subunits and subunits of proteasome regulator complexes inside retroviruses. Here, we demonstrated the association of functional 20S proteasome with gammaretroviruses, betaretroviruses, and lentiviruses. Cleaved proteasome subunits beta 1, beta 2 and beta 5 were detected in tested viruses. Using fluorescent peptides and a cell-permeable proteasome activity probe, proteasome activity was detected in endogenous and exogenous retroviruses, including recombinant HIV-1. Taken together, our data favors the insertion of functional proteasomes into the retroviruses during assembly. The possible role of proteasomes in retroviruses is discussed.
引用
收藏
页数:18
相关论文
共 50 条
[21]   Amyloid-β Peptide Is a Substrate of the Human 20S Proteasome [J].
Zhao, Xiaobei ;
Yang, Jerry .
ACS CHEMICAL NEUROSCIENCE, 2010, 1 (10) :655-660
[22]   Purification and Identification of the 20S Proteasome Complex from Zebrafish [J].
Hasan, Ali Md ;
Jyoti, Md Maisum Sarwar ;
Rana, Md Rubel ;
Rezanujjaman, Md ;
Tokumoto, Toshinobu .
ZEBRAFISH, 2022, 19 (01) :18-23
[23]   Characterization of Fully Recombinant Human 20S and 20S-PA200 Proteasome Complexes [J].
Rego, Ana Toste ;
da Fonseca, Paula C. A. .
MOLECULAR CELL, 2019, 76 (01) :138-+
[24]   The 20S Proteasome as an Assembly Platform for the 19S Regulatory Complex [J].
Hendil, Klavs B. ;
Kriegenburg, Franziska ;
Tanaka, Keiji ;
Murata, Shigeo ;
Lauridsen, Anne-Marie B. ;
Johnsen, Anders H. ;
Hartmann-Petersen, Rasmus .
JOURNAL OF MOLECULAR BIOLOGY, 2009, 394 (02) :320-328
[25]   PA28αβ Reduces Size and Increases Hydrophilicity of 20S Immunoproteasome Peptide Products [J].
Raule, Mary ;
Cerruti, Fulvia ;
Benaroudj, Nadia ;
Migotti, Rebekka ;
Kikuchi, Julia ;
Bachi, Angela ;
Navon, Ami ;
Dittmar, Gunnar ;
Cascio, Paolo .
CHEMISTRY & BIOLOGY, 2014, 21 (04) :470-480
[26]   Resting complexes of the persistent yeast 20S RNA Narnavirus consist solely of the 20S RNA viral genome and its RNA polymerase p91 [J].
Vega, Lorena ;
Sevillano, Laura ;
Esteban, Rosa ;
Fujimura, Tsutomu .
MOLECULAR MICROBIOLOGY, 2014, 93 (06) :1119-1129
[27]   Naegleria fowleri and Naegleria gruberi 20S proteasome: identification and characterization [J].
Guzman-Tellez, Paula ;
Martinez-Valencia, Diana ;
Silva-Olivares, Angelica ;
del Angel, Rosa M. ;
Serrano-Luna, Jesus ;
Shibayama, Mineko .
EUROPEAN JOURNAL OF CELL BIOLOGY, 2020, 99 (05)
[28]   Quinone reductase acts as a redox switch of the 20S yeast proteasome [J].
Sollner, Sonja ;
Schober, Markus ;
Wagner, Andrea ;
Prem, Anna ;
Lorkova, Lucie ;
Palfey, Bruce A. ;
Groll, Michael ;
Macheroux, Peter .
EMBO REPORTS, 2009, 10 (01) :65-70
[29]   New Peptide-Based Pharmacophore Activates 20S Proteasome [J].
Osmulski, Pawel A. ;
Karpowicz, Przemyslaw ;
Jankowska, Elzbieta ;
Bohmann, Jonathan ;
Pickering, Andrew M. ;
Gaczynska, Maria .
MOLECULES, 2020, 25 (06)
[30]   Electrochemical assay for 20S proteasome activity and inhibition with anticancer drugs [J].
Henriques de Jesus, Catarina Sofia ;
Chiorcea-Paquim, Ana Maria ;
Barsan, Madalina Maria ;
Diculescu, Victor Constantin .
TALANTA, 2019, 199 :32-39