Quantitative proteomics analysis provides insight into the biological role of Hsp90 in BmNPV infection in Bombyx mori

Gomi, 1999, Sequence analysis of the genome of Bombyx mori nucleopolyhedrovirus, J. Gen. Virol., 80, 1323, 10.1099/0022-1317-80-5-1323 Jiang, 2014, The progress and future of enhancing antiviral capacity by transgenic technology in the silkworm Bombyx mori, Insect Biochem. Mol. Biol., 48, 1, 10.1016/j.ibmb.2014.02.003 Lee, 2000, Transcription of eukaryotic protein-coding genes, Annu. Rev. Genet., 34, 77, 10.1146/annurev.genet.34.1.77 Ulrich, 2002, Molecular chaperones in the cytosol: from nascent chain to folded protein, Science, 295, 1852, 10.1126/science.1068408 Gabriela, 2004, Hsp90: the vulnerable chaperone, Drug Discov. Today, 9, 881, 10.1016/S1359-6446(04)03245-3 Prodromou, 2012, The ‘active life’ of Hsp90 complexes, Biochim. Biophys. Acta Mol. Cell Res., 1823, 614, 10.1016/j.bbamcr.2011.07.020 Sullivan, 2001, ATP-dependent simian virus 40 T-antigen–Hsc70 complex formation, J. Virol., 75, 1601, 10.1128/JVI.75.4.1601-1610.2001 Kampmueller, 2005, The cellular chaperone heat shock protein 90 facilitates flock house virus RNA replication in Drosophila cells, J. Virol., 79, 6827, 10.1128/JVI.79.11.6827-6837.2005 Das, 2014, Heat shock protein 90 positively regulates Chikungunya virus replication by stabilizing viral non-structural protein nsP2 during infection, PLoS One, 9, 10.1371/journal.pone.0100531 Lyupina, 2011, New insights into the induction of the heat shock proteins in baculovirus infected insect cells, Virology, 421, 34, 10.1016/j.virol.2011.09.010 Linlin, 2013, HSP90 protects the human T-cell Leukemia virus type 1 (HTLV-1) tax oncoprotein from proteasomal degradation to support NF-κB activation and HTLV-1 replication, J. Virol., 87, 13640, 10.1128/JVI.02006-13 Xiaoping, 2013, Hsp90 inhibitor 17-DMAG decreases expression of conserved herpesvirus protein kinases and reduces virus production in Epstein-Barr virus-infected cells, J. Virol., 87, 10126, 10.1128/JVI.01671-13 Surender, 2015, Molecular chaperone Hsp90 is a therapeutic target for noroviruses, J. Virol., 89, 6352, 10.1128/JVI.00315-15 Marcu, 2000, The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone, J. Biol. Chem., 275, 37181, 10.1074/jbc.M003701200 Xu, 2002, Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu, Proc. Natl. Acad. Sci. U. S. A., 99, 12847, 10.1073/pnas.202365899 Ju, 2011, Synthesis and in vitro anti-HSV-1 activity of a novel Hsp90 inhibitor BJ-B11, Bioorg. Med. Chem. Lett., 21, 1675, 10.1016/j.bmcl.2011.01.098 Field, 2003, KSHV vFLIP binds to IKK-gamma to activate IKK, J. Cell Sci., 116, 3721, 10.1242/jcs.00691 Ron, 2013, Hsp90 inhibitors exhibit resistance-free antiviral activity against respiratory syncytial virus, PLoS One, 8 Shannon, 2003, Cytoscape: a software environment for integrated models of biomolecular interaction networks, Genome Res., 13, 2498, 10.1101/gr.1239303 André-Patrick, 2014, HspB1, HspB5 and HspB4 in human cancers: potent oncogenic role of some of their client proteins, Cancers, 6, 333, 10.3390/cancers6010333 Bukong, 2014, Exosomes from hepatitis C infected patients transmit HCV infection and contain replication competent viral RNA in complex with Ago2-miR122-HSP90, PLoS Pathog., 10, 10.1371/journal.ppat.1004424 Yu, 2017, iTRAQ-based quantitative proteomics analysis of molecular mechanisms associated with Bombyx mori (Lepidoptera) larval midgut response to BmNPV in susceptible and near-isogenic strains, J. Proteome, 165, 10.1016/j.jprot.2017.06.007 Mao, 2018, Quantitative proteomics of Bombyx mori after BmNPV challenge, J. Proteome, 181, 142, 10.1016/j.jprot.2018.04.010 Dong, 2017, iTRAQ proteomic analysis of the interactions between Bombyx mori nuclear polyhedrosis virus and silkworm, J. Proteome, 166, 138, 10.1016/j.jprot.2017.07.013 Dulaney, 2017, Poly(ADP-ribose) polymerase activity and inhibition in cancer, Semin. Cell Dev. Biol., 63, 144, 10.1016/j.semcdb.2017.01.007 Bai, 2015, Biology of poly(ADP-ribose) polymerases: the factotums of cell maintenance, Mol. Cell, 58, 947, 10.1016/j.molcel.2015.01.034 Lieber, 2010, The mechanism of double-strand DNA break repair by the nonhomologous DNA end-joining pathway, Annu. Rev. Biochem., 79, 181, 10.1146/annurev.biochem.052308.093131 Jen-Sheng, 2013, Association of X-ray repair cross-complementing-6 genotypes with childhood leukemia, Anticancer Res., 33, 5395 Xian, 2015, DNA repair gene ERCC1 C118T polymorphism predicts sensitivity of recurrent esophageal cancer to radiochemotherapy in a Chinese population, Thorac. Cancer, 6, 741, 10.1111/1759-7714.12251 Vilmos, 1998, Insect immunity: evolutionary roots of the mammalian innate immune system, Immunol. Lett., 62, 59, 10.1016/S0165-2478(98)00023-6 Arai, 2013, Immunohistochemical analysis of the role of Hemocytin in nodule formation in the larvae of the silkworm, Bombyx mori, J. Insect Sci., 13, 1, 10.1673/031.013.12501 Ratcliffe, 1977, Studies on the in vivo cellular reactions of insects: an ultrastructural analysis of nodule formation in galleria mellonella, Tissue Cell, 9, 73, 10.1016/0040-8166(77)90050-7 Koizumi, 1999, Lipopolysaccharide-binding protein of Bombyx mori participates in a hemocyte-mediated defense reaction against gram-negative bacteria, J. Insect Physiol., 45, 853, 10.1016/S0022-1910(99)00069-4 Yu, 2018, Molecular characterisation of Apolipophorin-III gene in Samia cynthia ricini and its roles in response to bacterial infection, J. Invertebr. Pathol., 159, 61, 10.1016/j.jip.2018.10.009 Taszlow, 2015, Changes in the hemolymph protein profiles in Galleria mellonella infected with Bacillus thuringiensis involve apolipophorin III. The effect of heat shock, Arch. Insect Biochem. Physiol., 88, 123, 10.1002/arch.21208 Wen, 2016, Involvement of a versatile pattern recognition receptor, apolipophorin-III in prophenoloxidase activation and antibacterial defense of the Chinese oak silkworm, Antheraea pernyi, Dev. Comp. Immunol., 65, 124, 10.1016/j.dci.2016.07.001 Ji, 2016, An insulin-binding protein from the venom of a solitary wasp Eumenes pomiformis binds to apolipophorin III in lepidopteran hemolymph, Toxicon, 111, 62, 10.1016/j.toxicon.2015.12.019 Mun, 2019, Cellular zinc finger protein 622 hinders human adenovirus lytic growth and limits binding of the viral pVII protein to virus DNA, J. Virol., 93, 21, 10.1128/JVI.01628-18 Li, 2016, Zinc finger E-box-binding homeobox 2 inhibits hepatitis B virus replication and expression, Zhonghua Gan Zang Bing Za Zhi, 24, 824 Takashi, 2013, Gene- and protein-delivered zinc finger-staphylococcal nuclease hybrid for inhibition of DNA replication of human papillomavirus, PLoS One, 8 Dores-Silva, 2013, Structural and stability studies of the human mtHsp70-escort protein 1: an essential mortalin co-chaperone, Int. J. Biol. Macromol., 56, 140, 10.1016/j.ijbiomac.2013.02.009 Lu, 1998, The conserved carboxyl terminus and zinc finger-like domain of the co-chaperone Ydj1 assist Hsp70 in protein folding, J. Biol. Chem., 273, 5970, 10.1074/jbc.273.10.5970 Martin, 2015, A first line of stress defense: small heat shock proteins and their function in protein homeostasis, J. Mol. Biol., 427, 1537, 10.1016/j.jmb.2015.02.002 Andrew, 2004, Phosphorylation of alphaB-crystallin alters chaperone function through loss of dimeric substructure, J. Biol. Chem., 279, 28675, 10.1074/jbc.M403348200 Den Englesman, 2005, Nuclear import of alpha B-crystallin is phosphorylation-dependent and hampered by hyperphosphorylation of the myopathy-related mutant R120G, J. Biol. Chem., 280, 37139, 10.1074/jbc.M504106200 Heath, 2007, Mimicking phosphorylation of alphaB-crystallin affects its chaperone activity, Biochem. J., 401, 129, 10.1042/BJ20060981 Vos, 2016, Specific protein homeostatic functions of small heat-shock proteins increase lifespan, Aging Cell, 15, 217, 10.1111/acel.12422 Arrigo, 2007, The cellular "networking" of mammalian Hsp27 and its functions in the control of protein folding, redox state and apoptosis, Adv. Exp. Med. Biol., 594, 14, 10.1007/978-0-387-39975-1_2 Balogi, 2008, A mutant small heat shock protein with increased thylakoid association provides an elevated resistance against UV-B damage in Synechocystis 6803, J. Biol. Chem., 283, 22983, 10.1074/jbc.M710400200 Ario, 2005, Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones, Cell Stress Chaperones, 10, 329, 10.1379/CSC-139R.1 De, 2016, Hsp70 chaperones use ATP to remodel native protein oligomers and stable aggregates by entropic pulling, Nat. Struct. Mol. Biol., 23, 766, 10.1038/nsmb.3283 Walker, 2003, Lifespan extension in C. elegans by a molecular chaperone dependent upon insulin-like signals, Aging Cell, 2, 131, 10.1046/j.1474-9728.2003.00045.x Geneviève, 2004, Overexpression of the small mitochondrial Hsp22 extends Drosophila life span and increases resistance to oxidative stress, FASEB J., 18, 598, 10.1096/fj.03-0860fje Jha, 2013, Heat shock protein 90 functions to stabilize and activate the testis-specific serine/threonine kinases, a family of kinases essential for male fertility, J. Biol. Chem., 288, 16308, 10.1074/jbc.M112.400978 Sato, 2000, Modulation of Akt kinase activity by binding to Hsp90, Proc. Natl. Acad. Sci. U. S. A., 97, 10832, 10.1073/pnas.170276797 Enomoto, 2013, The HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin modulates radiosensitivity by downregulating serine/threonine kinase 38 via Sp1 inhibition, Eur. J. Cancer, 49, 3547, 10.1016/j.ejca.2013.06.034 Sharma, 2012, Quantitative proteomics reveals that Hsp90 inhibition preferentially targets kinases and the DNA damage response, Mol. Cell Proteomics, 11, 10.1074/mcp.M111.014654 Zhixiang, 2012, Systematic identification of the HSP90 candidate regulated proteome, Mol. Cell Proteomics, 11 Fierro-Monti, 2013, Dynamic impacts of the inhibition of the molecular chaperone Hsp90 on T-cell proteome have implications for anti-cancer therapy, PLoS One, 8, 18, 10.1371/journal.pone.0080425 Sawarkar, 2012, Hsp90 globally targets paused RNA polymerase to regulate gene expression in response to environmental stimuli, Cell, 149, 807, 10.1016/j.cell.2012.02.061