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Protection against Fatal Sindbis Virus Encephalitis by Beclin, a Novel Bcl-2-Interacting Protein
Open accessAbstract
bcl-2, the prototypic cellular antiapoptotic gene, decreases Sindbis virus replication and Sindbis virus-induced apoptosis in mouse brains, resulting in protection against lethal encephalitis. To investigate potential mechanisms by which Bcl-2 protects against central nervous system Sindbis virus infection, we performed a yeast two-hybrid screen to identify Bcl-2-interacting gene products in an adult mouse brain library. We identified a novel 60-kDa coiled-coil protein, Beclin, which we confirmed interacts with Bcl-2 in mammalian cells, using fluorescence resonance energy transfer microscopy. To examine the role of Beclin in Sindbis virus pathogenesis, we constructed recombinant Sindbis virus chimeras that express full-length human Beclin (SIN/beclin), Beclin lacking the putative Bcl-2-binding domain (SIN/beclin ΔBcl-2BD), or Beclin containing a premature stop codon near the 5′ terminus (SIN/beclin stop). The survival of mice infected with SIN/beclin was significantly higher (71%) than the survival of mice infected with SIN/beclin ΔBcl-2BD (9%) or SIN/beclin stop (7%) (P < 0.001). The brains of mice infected with SIN/beclin had fewer Sindbis virus RNA-positive cells, fewer apoptotic cells, and lower viral titers than the brains of mice infected with SIN/beclin ΔBcl-2BD or SIN/beclin stop. These findings demonstrate that Beclin is a novel Bcl-2-interacting cellular protein that may play a role in antiviral host defense.
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Cites
Basic local alignment search tool
Altschul, S. F., Gish, W., Miller, W., Myers, E. W., & Lipman, D. J. (1990) · Journal of Molecular Biology · doi:10.1006/jmbi.1990.9999 · Cited by 98,669
Predicting coiled coils from protein sequences.
Lupas, A., Van Dyke, M., & Stock, J. (1991) · Science · doi:10.1126/science.252.5009.1162 · Cited by 3,953
Cited by
Mitochondrial membrane permeabilization in cell death
Kroemer, G., Galluzzi, L., & Brenner, C. (2007) · Physiological Reviews · doi:10.1152/physrev.00013.2006 · Cited by 3,598
Induction of autophagy and inhibition of tumorigenesis by beclin 1
Liang, X. H., Jackson, S., Seaman, M., Brown, K., Kempkes, B., Hibshoosh, H., & Levine, B. (1999) · Nature · doi:10.1038/45257 · Cited by 3,347
Self-citationImmunogenic cell death in cancer and infectious disease
Galluzzi, L., Buqué, A., Kepp, O., Zitvogel, L., & Kroemer, G. (2017) · Nature Reviews Immunology · doi:10.1038/nri.2016.107 · Cited by 3,119
An Overview of Autophagy: Morphology, Mechanism, and Regulation
Parzych, K. R., & Klionsky, D. J. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5371 · Cited by 2,521
The Beclin 1 network regulates autophagy and apoptosis
Kang, R., Zeh, H. J., Lotze, M. T., & Tang, D. (2011) · Cell Death & Differentiation · doi:10.1038/cdd.2010.191 · Cited by 2,485
Promotion of tumorigenesis by heterozygous disruption of the beclin 1 autophagy gene
Qu, X., Yu, J., Bhagat, G., Furuya, N., Hibshoosh, H., Troxel, A., Rosen, J., Eskelinen, E.-L., Mizushima, N., Ohsumi, Y., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci20039 · Cited by 2,311
Self-citationYue, Z., Jin, S., Yang, C., Levine, A. J., & Heintz, N. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2436255100 · Cited by 2,116
The machinery of macroautophagy
Feng, Y., He, D., Yao, Z., & Klionsky, D. J. (2014) · Cell Research · doi:10.1038/cr.2013.168 · Cited by 2,083
Role of Bcl-2 family proteins in a non-apoptotic programmed cell death dependent on autophagy genes
Shimizu, S., Kanaseki, T., Mizushima, N., Mizuta, T., Arakawa-Kobayashi, S., Thompson, C. B., & Tsujimoto, Y. (2004) · Nature Cell Biology · doi:10.1038/ncb1192 · Cited by 1,358
Autophagy in healthy aging and disease
Aman, Y., Schmauck-Medina, T., Hansen, M., Morimoto, R. I., Simon, A. K., Bjedov, I., Palikaras, K., Simonsen, A., Johansen, T., Tavernarakis, N., et al. (2021) · Nature Aging · doi:10.1038/s43587-021-00098-4 · Cited by 1,313
Beclin 1 Forms Two Distinct Phosphatidylinositol 3-Kinase Complexes with Mammalian Atg14 and UVRAG
Itakura, E., Kishi, C., Inoue, K., & Mizushima, N. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-01-0080 · Cited by 1,176
Role of BNIP3 and NIX in cell death, autophagy, and mitophagy
Zhang, J., & Ney, P. A. (2009) · Cell Death & Differentiation · doi:10.1038/cdd.2009.16 · Cited by 1,021
Zhong, Y., Wang, Q. J., Li, X., Yan, Y., Backer, J. M., Chait, B. T., Heintz, N., & Yue, Z. (2009) · Nature Cell Biology · doi:10.1038/ncb1854 · Cited by 1,005
Kouroku, Y., Fujita, E., Tanida, I., Ueno, T., Isoai, A., Kumagai, H., Ogawa, S., Kaufman, R. J., Kominami, E., & Momoi, T. (2007) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401984 · Cited by 934
Autophagic and tumour suppressor activity of a novel Beclin1-binding protein UVRAG
Liang, C., Feng, P., Ku, B., Dotan, I., Canaani, D., Oh, B.-H., & Jung, J. U. (2006) · Nature Cell Biology · doi:10.1038/ncb1426 · Cited by 919
Autophagy during viral infection — a double-edged sword
Choi, Y., Bowman, J. W., & Jung, J. U. (2018) · Nature Reviews Microbiology · doi:10.1038/s41579-018-0003-6 · Cited by 838
HSV-1 ICP34.5 Confers Neurovirulence by Targeting the Beclin 1 Autophagy Protein
Orvedahl, A., Alexander, D., Tallóczy, Z., Sun, Q., Wei, Y., Zhang, W., Burns, D., Leib, D. A., & Levine, B. (2007) · Cell Host & Microbe · doi:10.1016/j.chom.2006.12.001 · Cited by 857
Self-citationPharmacological modulation of autophagy: therapeutic potential and persisting obstacles
Galluzzi, L., Bravo-San Pedro, J. M., Levine, B., Green, D. R., & Kroemer, G. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.22 · Cited by 842
Self-citationA critical role for the autophagy gene Atg5 in T cell survival and proliferation
Pua, H. H., Dzhagalov, I., Chuck, M., Mizushima, N., & He, Y.-W. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20061303 · Cited by 622
“Bcl-2 has been shown to inhibit autophagosome formation in nutrient-starved yeast and human cancer cell lines (25), yet Bcl-2 expression in Bax−/− Bak−/− mouse embryonic fi broblasts enhances autophagy after etoposide treatment (19).”
Spencer, B., Potkar, R., Trejo, M., Rockenstein, E., Patrick, C., Gindi, R., Adame, A., Wyss-Coray, T., & Masliah, E. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.4390-09.2009 · Cited by 595
Autophagy Protects against Sindbis Virus Infection of the Central Nervous System
Orvedahl, A., MacPherson, S., Sumpter, R., Tallóczy, Z., Zou, Z., & Levine, B. (2010) · Cell Host & Microbe · doi:10.1016/j.chom.2010.01.007 · Cited by 558
Self-citationEnhancing Macroautophagy Protects against Ischemia/Reperfusion Injury in Cardiac Myocytes
Hamacher-Brady, A., Brady, N. R., & Gottlieb, R. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603783200 · Cited by 555
The Role of Autophagy in the Heart
Sciarretta, S., Maejima, Y., Zablocki, D., & Sadoshima, J. (2018) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021317-121427 · Cited by 547
Dual role of autophagy in hallmarks of cancer
Singh, S. S., Vats, S., Chia, A. Y.-Q., Tan, T. Z., Deng, S., Ong, M. S., Arfuso, F., Yap, C. T., Goh, B. C., Sethi, G., et al. (2018) · Oncogene · doi:10.1038/s41388-017-0046-6 · Cited by 542
Physiological functions of Atg6/Beclin 1: a unique autophagy-related protein
Cao, Y., & Klionsky, D. J. (2007) · Cell Research · doi:10.1038/cr.2007.78 · Cited by 541
Matrix Protein 2 of Influenza A Virus Blocks Autophagosome Fusion with Lysosomes
Gannagé, M., Dormann, D., Albrecht, R., Dengjel, J., Torossi, T., Rämer, P. C., Lee, M., Strowig, T., Arrey, F., Conenello, G., et al. (2009) · Cell Host & Microbe · doi:10.1016/j.chom.2009.09.005 · Cited by 526
Mst1 inhibits autophagy by promoting the interaction between Beclin1 and Bcl-2
Maejima, Y., Kyoi, S., Zhai, P., Liu, T., Li, H., Ivessa, A., Sciarretta, S., Del Re, D. P., Zablocki, D. K., Hsu, C.-P., et al. (2013) · Nature Medicine · doi:10.1038/nm.3322 · Cited by 499
Biogenesis and Cargo Selectivity of Autophagosomes
Weidberg, H., Shvets, E., & Elazar, Z. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-052709-094552 · Cited by 466
Mitochondria and cell signalling
Tait, S. W. G., & Green, D. R. (2012) · Journal of Cell Science · doi:10.1242/jcs.099234 · Cited by 453
MAPK/JNK signalling: a potential autophagy regulation pathway
Zhou, Y.-Y., Li, Y., Jiang, W.-Q., & Zhou, L.-F. (2015) · Bioscience Reports · doi:10.1042/bsr20140141 · Cited by 444
Wohlgemuth, S. E., Seo, A. Y., Marzetti, E., Lees, H. A., & Leeuwenburgh, C. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2009.11.002 · Cited by 397
Autophagy in acute kidney injury
Kaushal, G. P., & Shah, S. V. (2016) · Kidney International · doi:10.1016/j.kint.2015.11.021 · Cited by 389
Tanaka, S., Hikita, H., Tatsumi, T., Sakamori, R., Nozaki, Y., Sakane, S., Shiode, Y., Nakabori, T., Saito, Y., Hiramatsu, N., et al. (2016) · Hepatology · doi:10.1002/hep.28820 · Cited by 376
Die another way – non-apoptotic mechanisms of cell death
Tait, S. W. G., Ichim, G., & Green, D. R. (2014) · Journal of Cell Science · doi:10.1242/jcs.093575 · Cited by 366
Neuronal cell death in neurodegenerative diseases: recurring themes around protein handling
Gorman, A. M. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00402.x · Cited by 362
PKR-Dependent Xenophagic Degradation of Herpes Simplex Virus Type 1
Tallóczy, Z., Virgin, IV, & Levine, B. (2006) · Autophagy · doi:10.4161/auto.2176 · Cited by 334
Self-citationA Novel Protein Complex Linking the δ2 Glutamate Receptor and Autophagy
Yue, Z., Horton, A., Bravin, M., DeJager, P. L., Selimi, F., & Heintz, N. (2002) · Neuron · doi:10.1016/s0896-6273(02)00861-9 · Cited by 306
Pickford, F., Masliah, E., Britschgi, M., Lucin, K., Narasimhan, R., Jaeger, P. A., Small, S., Spencer, B., Rockenstein, E., Levine, B., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci33585 · Cited by 268
Self-citationRegulation of autophagy by phosphatidylinositol 3‐phosphate
Burman, C., & Ktistakis, N. T. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.01.011 · Cited by 234
Nix directly binds to GABARAP: A possible crosstalk between apoptosis and autophagy
Schwarten, M., Mohrlüder, J., Ma, P., Stoldt, M., Thielmann, Y., Stangler, T., Hersch, N., Hoffmann, B., Merkel, R., & Willbold, D. (2009) · Autophagy · doi:10.4161/auto.5.5.8494 · Cited by 224
Physiological consequences of heat stress in pigs
Ross, J. W., Hale, B. J., Gabler, N. K., Rhoads, R. P., Keating, A. F., & Baumgard, L. H. (2015) · Animal Production Science · doi:10.1071/an15267 · Cited by 202
Autophagy Is a Component of Epithelial Cell Fate in Obstructive Uropathy
Li, L., Zepeda-Orozco, D., Black, R., & Lin, F. (2010) · The American Journal of Pathology · doi:10.2353/ajpath.2010.090345 · Cited by 195
Autophagy in the heart and liver during normal aging and calorie restriction
Wohlgemuth, S. E., Julian, D., Akin, D. E., Fried, J., Toscano, K., Leeuwenburgh, C., & Dunn, Jr. (2007) · Rejuvenation Research · doi:10.1089/rej.2006.0535 · Cited by 179
Salminen, A., Kaarniranta, K., & Kauppinen, A. (2013) · Ageing Research Reviews · doi:10.1016/j.arr.2012.11.004 · Cited by 173
Hepatitis C Virus Upregulates Beclin1 for Induction of Autophagy and Activates mTOR Signaling
Shrivastava, S., Bhanja Chowdhury, J., Steele, R., Ray, R., & Ray, R. B. (2012) · Journal of Virology · doi:10.1128/jvi.00616-12 · Cited by 163
Lu, J., He, L., Behrends, C., Araki, M., Araki, K., Jun Wang, Q., Catanzaro, J. M., Friedman, S. L., Zong, W.-X., Fiel, M. I., et al. (2014) · Nature Communications · doi:10.1038/ncomms4920 · Cited by 148
Brady, N. R., Hamacher‐Brady, A., Yuan, H., & Gottlieb, R. A. (2007) · The FEBS Journal · doi:10.1111/j.1742-4658.2007.05849.x · Cited by 137
Berberine as a potential autophagy modulator
Mohammadinejad, R., Ahmadi, Z., Tavakol, S., & Ashrafizadeh, M. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.28325 · Cited by 132
Association of increased autophagic inclusions labeled for β-galactosidase with fibroblastic aging
Gerland, L.-M., Peyrol, S., Lallemand, C., Branche, R., Magaud, J.-P., & Ffrench, M. (2003) · Experimental Gerontology · doi:10.1016/s0531-5565(03)00132-3 · Cited by 130
Physiological mechanisms through which heat stress compromises reproduction in pigs
Ross, J. W., Hale, B. J., Seibert, J. T., Romoser, M. R., Adur, M. K., Keating, A. F., & Baumgard, L. H. (2017) · Molecular Reproduction and Development · doi:10.1002/mrd.22859 · Cited by 128
Pathogenic role of BECN1/Beclin 1 in the development of amyotrophic lateral sclerosis
Nassif, M., Valenzuela, V., Rojas-Rivera, D., Vidal, R., Matus, S., Castillo, K., Fuentealba, Y., Kroemer, G., Levine, B., & Hetz, C. (2014) · Autophagy · doi:10.4161/auto.28784 · Cited by 100
Self-citationNascimento-Ferreira, I., Nóbrega, C., Vasconcelos-Ferreira, A., Onofre, I., Albuquerque, D., Aveleira, C., Hirai, H., Déglon, N., & Pereira de Almeida, L. (2013) · Brain · doi:10.1093/brain/awt144 · Cited by 96
mVps34 is activated following high‐resistance contractions
MacKenzie, M. G., Hamilton, D. L., Murray, J. T., Taylor, P. M., & Baar, K. (2009) · The Journal of Physiology · doi:10.1113/jphysiol.2008.159830 · Cited by 94
Crosstalk between apoptosis and autophagy signaling pathways
(2020) · International Review of Cell and Molecular Biology · doi:10.1016/bs.ircmb.2020.01.003 · Cited by 92
Autophagy in Pulmonary Diseases
Nakahira, K., Pabon Porras, M. A., & Choi, A. M. K. (2016) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201512-2468so · Cited by 78
Autophagy, and BiP level decrease are early key events in retrograde degeneration of motoneurons
Penas, C., Font-Nieves, M., Forés, J., Petegnief, V, Planas, A., Navarro, X., & Casas, C. (2011) · Cell Death & Differentiation · doi:10.1038/cdd.2011.24 · Cited by 58
Intracellular recognition of pathogens and autophagy as an innate immune host defence
Yano, T., & Kurata, S. (2011) · Journal of Biochemistry · doi:10.1093/jb/mvr083 · Cited by 54
Recent advances of tanshinone in regulating autophagy for medicinal research
Wu, S., Zhao, K., Wang, J., Liu, N., Nie, K., Qi, L., & Xia, L. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.1059360 · Cited by 32
Sigmond, T., Fehér, J., Baksa, A., Pásti, G., Pálfia, Z., Takács‐Vellai, K., Kovács, J., Vellai, T., & Kovács, A. L. (2008) · Methods in Enzymology · doi:10.1016/s0076-6879(08)03228-x · Cited by 25
Metadata
- Authors
- Liang, X. H., Kleeman, L. K., Jiang, H. H., Gordon, G., Goldman, J. E., Berry, G., Herman, B., & Levine, B.
- Venue
- Journal of Virology
- Publisher
- American Society for Microbiology
- Published
- 1998-11-01
- Volume
- 72
- Issue
- 11
- Pages
- 8586-8596
- ISSN
- 0022-538X (ISSN-L)
- 1098-5514
- OpenAlex
- W1780295430
- Cited by
- 1,132
- References
- 2
- FWCI
- 5.52
- Type
- journal article
- Language
- en
- Open access
- green
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