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Academic literature on the topic 'Hsp90 gene'

Author: Grafiati

Published: 6 September 2023

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Journal articles on the topic "Hsp90 gene"

1

Rehman, Saif ur, Asif Nadeem, Maryam Javed, Faiz-ul Hassan, Xier Luo, Ruqayya Bint Khalid, and Qingyou Liu. "Genomic Identification, Evolution and Sequence Analysis of the Heat-Shock Protein Gene Family in Buffalo." Genes 11, no. 11 (November 23, 2020): 1388. http://dx.doi.org/10.3390/genes11111388.

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Heat-shock proteins (HSP) are conserved chaperones crucial for protein degradation, maturation, and refolding. These adenosine triphosphate dependent chaperones were classified based on their molecular mass that ranges between 10–100 kDA, including; HSP10, HSP40, HSP70, HSP90, HSPB1, HSPD, and HSPH1 family. HSPs are essential for cellular responses and imperative for protein homeostasis and survival under stress conditions. This study performed a computational analysis of the HSP protein family to better understand these proteins at the molecular level. Physiochemical properties, multiple sequence alignment, and phylogenetic analysis were performed for 64 HSP genes in the Bubalus bubalis genome. Four genes were identified as belonging to the HSP90 family, 10 to HSP70, 39 to HSP40, 8 to HSPB, one for each HSPD, HSPH1, and HSP10, respectively. The aliphatic index was higher for HSP90 and HSP70 as compared to the HSP40 family, indicating their greater thermostability. Grand Average of hydropathicity Index values indicated the hydrophilic nature of HSP90, HSP70, and HSP40. Multiple sequence alignment indicated the presence of highly conserved consensus sequences that are plausibly significant for the preservation of structural integrity of proteins. In addition, this study has expanded our current knowledge concerning the genetic diversity and phylogenetic relatedness of HSPs of buffalo with other mammalian species. The phylogenetic tree revealed that buffalo is more closely related to Capra hircus and distantly associated with Danio rerio. Our findings provide an understanding of HSPs in buffalo at the molecular level for the first time. This study highlights functionally important HSPs and indicates the need for further investigations to better understand the role and mechanism of HSPs.

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Ajayi, Oyeyemi O., Sunday O. Peters, Marcos De Donato, Sunday O. Sowande, Fidalis D. N. Mujibi, Olanrewaju B. Morenikeji, Bolaji N. Thomas, Matthew A. Adeleke, and Ikhide G. Imumorin. "Computational genome-wide identification of heat shock protein genes in the bovine genome." F1000Research 7 (September 20, 2018): 1504. http://dx.doi.org/10.12688/f1000research.16058.1.

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Background: Heat shock proteins (HSPs) are molecular chaperones known to bind and sequester client proteins under stress. Methods: To identify and better understand some of these proteins, we carried out a computational genome-wide survey of the bovine genome. For this, HSP sequences from each subfamily (sHSP, HSP40, HSP70 and HSP90) were used to search the Pfam (Protein family) database, for identifying exact HSP domain sequences based on the hidden Markov model. ProtParam tool was used to compute potential physico-chemical parameters detectable from a protein sequence. Evolutionary trace (ET) method was used to extract evolutionarily functional residues of a homologous protein family. Results: We computationally identified 67 genes made up of 10, 43, 10 and 4 genes belonging to small HSP, HSP40, HSP70 and HSP90 families respectively. These genes were widely dispersed across the bovine genome, except in chromosomes 24, 26 and 27, which lack bovine HSP genes. We found an uncharacterized outer dense fiber (ODF1) gene in cattle with an intact alpha crystallin domain, like other small HSPs. Physico-chemical characteristic of aliphatic index was higher in HSP70 and HSP90 gene families, compared to small HSP and HSP40. Grand average hydropathy showed that small HSP (sHSP), HSP40, HSP70 and HSP90 genes had negative values except for DNAJC22, a member of HSP40 gene family. The uniqueness of DNAJA3 and DNAJB13 among HSP40 members, based on multiple sequence alignment, evolutionary trace analysis and sequence identity dendrograms, suggests evolutionary distinct structural and functional features, with unique roles in substrate recognition and chaperone functions. The monophyletic pattern of the sequence identity dendrograms of cattle, human and mouse HSP sequences suggests functional similarities. Conclusions: Our computational results demonstrate the first-pass in-silico identification of heat shock proteins and calls for further investigation to better understand their functional roles and mechanisms in Bovidae.

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Matsuoka, Erina, Naoki Kato, and Masakazu Hara. "Induction of the heat shock response in Arabidopsis by heat shock protein 70 inhibitor VER-155008." Functional Plant Biology 46, no. 10 (2019): 925. http://dx.doi.org/10.1071/fp18259.

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The heat shock protein 90 (HSP90) inhibitor, geldanamycin, is a chemical inducer of the heat shock response (HSR) in Arabidopsis. Geldanamycin is thought to activate the heat shock signal by dissociating the HSP90-heat shock factor (HSF) complex. Recent studies have indicated that plant HSP70 is also associated with HSF, suggesting that inhibition of HSP70 may induce the HSR. However, no studies have been conducted to test this hypothesis. Here, we found that a specific HSP70 inhibitor VER-155008 activated the promoter of a small HSP gene (At1 g53540, HSP17.6C-CI) of Arabidopsis, which was shown to be activated by geldanamycin and other HSP90 inhibitors. The production of HSP17.6C-CI, HSP70 and HSP90.1 proteins in Arabidopsis was enhanced by the addition of VER-155008. The reduction of chlorophyll contents by heat shock was ameliorated by VER-155008. Chaperone analyses indicated that VER-155008 inhibited the chaperone activities of wheat germ extract and human HSP70/HSP40, respectively. These results suggest that the inhibition of HSP70 by VER-155008 enhanced the heat tolerance of Arabidopsis by inducing the HSR in the plant.

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Ali, Adnan, and John J. Heikkila. "Enhanced accumulation of constitutive heat shock protein mRNA is an initial response of eye tissue to mild hyperthermia in vivo in adult Xenopus laevis." Canadian Journal of Physiology and Pharmacology 80, no. 11 (November 1, 2002): 1119–23. http://dx.doi.org/10.1139/y02-133.

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We have examined the effect of mild hyperthermia in vivo on heat shock transcription factor (HSF) binding activity and heat shock protein (hsp) gene expression in eye tissue of adult Xenopus laevis. A specific interaction between HSF and a synthetic oligonucleotide corresponding to the proximal heat shock element of the Xenopus hsp70B gene was greatly enhanced in eyes from hyperthermic animals compared with controls. Given these results, we examined the effect of hyperthermia in vivo on the expression of five hsp genes (hsp70, hsc70, BiP, hsp90, and hsp30) in eye tissue. Interestingly, at 28°C constitutively expressed hsp genes hsc70, BiP, and hsp90 were strongly enhanced, with further accumulation at 30°C. However, hsp70 and hsp30 mRNA accumulation were not detectable at 28°C but were strongly induced at 30°C. No enhancement of the relative levels of cytoskeletal actin mRNA was observed in the eye tissue of hyperthermic animals. These results suggest that one of the primary responses of eye tissue to hyperthermia in vivo is in the elevation of mRNAs encoding a set of constitutively expressed molecular chaperones.Key words: Xenopus, mRNA, eye, heat shock, heat shock factor.

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STEPHANOU, A., V. AMIN, D. A. ISENBERG, S. AKIRA, T. KISHIMOTO, and David S. LATCHMAN. "Interleukin 6 activates heat-shock protein 90β gene expression." Biochemical Journal 321, no. 1 (January 1, 1997): 103–6. http://dx.doi.org/10.1042/bj3210103.

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The levels of the cytokine interleukin-6 (IL-6) and the heat-shock protein hsp90 have both been reported to be elevated in patients with active systemic lupus erythematosus (SLE). We show that hsp90 protein accumulates to increased levels in both HuH7 hepatoma cells and peripheral blood mononuclear cells (PBMCs) treated with IL-6. In PBMCs this effect occurs without induction of the other hsps, paralleling the specific elevation of hsp90 in SLE. IL-6 is able to activate the hsp90 gene promoter directly; this activation can also be achieved by overexpressing either of the transcription factors NF-IL-6 or NF-IL-6β whose synthesis is induced by IL-6 treatment. Hence the induction of hsp90 protein accumulation by IL-6 is likely to be dependent on the enhanced activity of the hsp90β gene promoter produced by increased levels of NF-IL-6 and/or NF-IL-6β. These effects are discussed in terms of the role of hsp90 in the normal immune system and the mechanism of its activation in patients with SLE.

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Birbo, Bereket, Elechi E. Madu, Chikezie O. Madu, Aayush Jain, and Yi Lu. "Role of HSP90 in Cancer." International Journal of Molecular Sciences 22, no. 19 (September 25, 2021): 10317. http://dx.doi.org/10.3390/ijms221910317.

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HSP90 is a vital chaperone protein conserved across all organisms. As a chaperone protein, it correctly folds client proteins. Structurally, this protein is a dimer with monomer subunits that consist of three main conserved domains known as the N-terminal domain, middle domain, and the C-terminal domain. Multiple isoforms of HSP90 exist, and these isoforms share high homology. These isoforms are present both within the cell and outside the cell. Isoforms HSP90α and HSP90β are present in the cytoplasm; TRAP1 is present in the mitochondria; and GRP94 is present in the endoplasmic reticulum and is likely secreted due to post-translational modifications (PTM). HSP90 is also secreted into an extracellular environment via an exosome pathway that differs from the classic secretion pathway. Various co-chaperones are necessary for HSP90 to function. Elevated levels of HSP90 have been observed in patients with cancer. Despite this observation, the possible role of HSP90 in cancer was overlooked because the chaperone was also present in extreme amounts in normal cells and was vital to normal cell function, as observed when the drastic adverse effects resulting from gene knockout inhibited the production of this protein. Differences between normal HSP90 and HSP90 of the tumor phenotype have been better understood and have aided in making the chaperone protein a target for cancer drugs. One difference is in the conformation: HSP90 of the tumor phenotype is more susceptible to inhibitors. Since overexpression of HSP90 is a factor in tumorigenesis, HSP90 inhibitors have been studied to combat the adverse effects of HSP90 overexpression. Monotherapies using HSP90 inhibitors have shown some success; however, combination therapies have shown better results and are thus being studied for a more effective cancer treatment.

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Le Thi, Man, Na Nguyen Quoc, Huyen Tran Thi Thanh, Hong La Viet, and Bang Cao Phi. "Identification and analysis of HSP90 genes in papaya (Carica papaya L.) by using bioinformatics method." Journal of Science Natural Science 66, no. 4F (November 2021): 196–204. http://dx.doi.org/10.18173/2354-1059.2021-0083.

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The HSP90 gene family has been shown to play an important role in the tolerance and development of plants. Papaya, which is a fruit crop with high nutritional value, is native to the tropics but now is widely cultivated in many subtropical regions of the world. Therefore, papaya plants have to face many environmental factors during their life. This study aims to identify and analyze the HSP90 gene family in papaya by bioinformatics method. A total of seven HSP90 genes have been identified in the genome of papaya (Carica papaya L.) by using the bioinformatic methods. The full-length genomic sequence of papaya HSP90 genes were ranging from 2650 to 8136 nucleotides, non continuous coding, with number of intro ranging from two to 19. The predicted protein sequences included from 348 to 796 amino acids, according to the molecular weight ranged from 39.92 to 90.61 kDa. Among seven CpHSP90, the two CpHSP90-1 and CpHSP90-4 were considered pseudogenes due to their small size. These proteins were acidic with a pI value ranging from 4.69 to 5.42, except CpHSP90-1 (pI 7.03). Based on the protein structure, subcellular localization and the phylogenic analysis, the papaya HSP90 were divided into two groups, I (cytoplasmic HSP90, four members) and II (organelle HSP90, three members). Analysis of transcriptomes showed that the papaya HSP90s were differentially expressed in different tissues at different development stages. In which, most of the papaya HSP90 is highly expressed in flower buds or in fruits at stage 2 or stage 3. CpHSP90-2 had the highest level of expression, followed by CpHSP90-5. In contrast, CpHSP90-1 was not expressed or very weakly expressed in these studied tissues. All of seven HSP90 genes of papaya were induced by freeze-thaw awakening treatment (in comparison with control treatment), among them, CpHSP90-1 was strongest induced by stress (12.13-folds), however, it was a pseudogene and had a very low level of basal expression. CpHSP90-2 had a high induction level (2.81- folds), and also had a high basal expression level compared to other HSP90 genes of papaya. The results of this work have an important significance and will serve as a base for the further research on gene cloning, functional analysis of HSP90 genes and breeding of papaya in response to environmental abiotic stresses and the development of this fruit crop.

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Gupta, Payal, Amit K. Mittal, Dennis D. Weisenburger, Philip Bierman, and Shantaram S. Joshi. "Heat-Shock Protein Signature Is Associated with Refractory Chronic Lymphocytic Leukemia Cells From Different In Vivo Microenvironments,." Blood 118, no. 21 (November 18, 2011): 3866. http://dx.doi.org/10.1182/blood.v118.21.3866.3866.

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Abstract Abstract 3866 Chronic Lymphocytic Leukemia (CLL) is a monoclonal B-cell disorder with accumulation of leukemic cells in peripheral blood, bone marrow and lymphoid organs. It presents with a heterogeneous clinical course. Many patients survive long periods of time without any need for treatment, whereas other patients show resistance to treatment or relapse soon after administration of therapy. Although some prognostic markers such as mutational status of immunoglobulin variable heavy chain, chromosomal abnormalities, CD38 levels, or ZAP-70 expression may help predict at initial diagnosis which patients will have more aggressive disease, the exact factors that can determine chances of remission in CLL are still not clear, making treatment challenging. Furthermore, CLL remains an incurable disease, necessitating a way for controlling its progression. Identifying novel molecular signatures associated with refractory CLL disease may help devise targeted treatment strategies and thus may prolong survival times and prevent the progression of CLL in relapsed patients. Considering this, we performed gene expression profiling (GEP) on peripheral blood (PB), bone marrow (BM) and lymph node (LN) samples collected at the time of diagnosis. We divided CLL samples into 3 groups based on their response to treatment; i) Stable CLL group: asymptomatic patients requiring no treatment, ii) Treated but stable CLL group: patients required treatment but had stable disease for at least one year after the end of the treatment cycle, and iii) Relapsed CLL: patients who relapsed within a year of end of the treatment cycle. Significance analysis of microarray (SAM) revealed that the heat-shock protein (HSP) signature (HSJ2, HSP70, HSP90, HSP60, HSP10, HSP 105, HSP40, HSP27, HSPA2, HSJ1, HSF4, HSPCA), BCR signaling pathway (JUN, NFATC4, NFKBIE, PPP3CB, TRAF3, CD81, CCT4), activation markers (CD81, CD83) and MMPs (MMP3, MMP9) were overexpressed in relapsed PB-CLL (n=3) compared to stable PB-CLL (n=6) and treated but stable PB-CLL (n=10). Overexpression of heat-shock protein signature genes were further observed in additional relapsed PB-CLL (n=6) group compared to other two PB-CLL (n=22) group. Interestingly, the HSP signature was consistently overexpressed in relapsed BM-CLL (n=6) and LN-CLL (n=12) compared to stable and treated but stable BM-CLL (n=11) and LN-CLL (n=3) groups. HSPs are considered chaperones of tumorigenesis and known to enhance survival, migration, and proliferation of tumor cells which may contribute to relapse in patients. Furthermore, the HSPs genes (HSP90 and HSP70) were significantly overexpressed in LN-CLL as compared to PB-CLL which implies important role of the microenviroment in rendering CLL refractory. To investigate the link between the expression of the individual genes with the aggressiveness of the disease, Kaplan-Meier log-rank tests were performed. We found that the higher expression of HSP90A, HSP90B, HSJ, and MMP9 were significantly (p<0.05) associated with shorter time to treatment. In summary, our study suggests that HSP genes are overexpressed in refractory CLL patients and thus are promising targets to improve clinical outcome. Disclosures: No relevant conflicts of interest to declare.

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Fu, Ssu-Ju, Meng-Chun Hu, Cheng-Tsung Hsiao, An-Ting Cheng, Tsung-Yu Chen, Chung-Jiuan Jeng, and Chih-Yung Tang. "Regulation of ClC-2 Chloride Channel Proteostasis by Molecular Chaperones: Correction of Leukodystrophy-Associated Defect." International Journal of Molecular Sciences 22, no. 11 (May 30, 2021): 5859. http://dx.doi.org/10.3390/ijms22115859.

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The ClC-2 channel plays a critical role in maintaining ion homeostasis in the brain and the testis. Loss-of-function mutations in the ClC-2-encoding human CLCN2 gene are linked to the white matter disease leukodystrophy. Clcn2-deficient mice display neuronal myelin vacuolation and testicular degeneration. Leukodystrophy-causing ClC-2 mutant channels are associated with anomalous proteostasis manifesting enhanced endoplasmic reticulum (ER)-associated degradation. The molecular nature of the ER quality control system for ClC-2 protein remains elusive. In mouse testicular tissues and Leydig cells, we demonstrated that endogenous ClC-2 co-existed in the same protein complex with the molecular chaperones heat shock protein 90β (Hsp90β) and heat shock cognate protein (Hsc70), as well as the associated co-chaperones Hsp70/Hsp90 organizing protein (HOP), activator of Hsp90 ATPase homolog 1 (Aha1), and FK506-binding protein 8 (FKBP8). Further biochemical analyses revealed that the Hsp90β-Hsc70 chaperone/co-chaperone system promoted mouse and human ClC-2 protein biogenesis. FKBP8 additionally facilitated membrane trafficking of ClC-2 channels. Interestingly, treatment with the Hsp90-targeting small molecule 17-allylamino-17-demethoxygeldanamycin (17-AAG) substantially boosted ClC-2 protein expression. Also, 17-AAG effectively increased both total and cell surface protein levels of leukodystrophy-causing loss-of-function ClC-2 mutant channels. Our findings highlight the therapeutic potential of 17-AAG in correcting anomalous ClC-2 proteostasis associated with leukodystrophy.

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Shyamala, G., Y. Gauthier, S. K. Moore, M. G. Catelli, and S. J. Ullrich. "Estrogenic regulation of murine uterine 90-kilodalton heat shock protein gene expression." Molecular and Cellular Biology 9, no. 8 (August 1989): 3567–70. http://dx.doi.org/10.1128/mcb.9.8.3567-3570.1989.

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Murine uterine steady-state protein levels of the 90-kilodalton heat shock protein (HSP90) have been demonstrated recently to be increased by estrogen in a target tissue- and steroid-specific manner (C. Ramachandran, M.G. Catelli, W. Schneider, and G. Shyamala, Endocrinology 123:956-961, 1988). We now report that this regulation occurred with both the HSP86 and HSP84 forms of HSP90 as well as with the 94-kilodalton glucose-regulated protein. At the mRNA level, this response was greatest for HSP86 (15-fold). In contrast, estradiol had no significant effect on HSP70.

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Dissertations / Theses on the topic "Hsp90 gene"

1

Smith, David. "Hsp90 and hsp70 genes of Theileria annulata : structure, regulation and molecular phylogeny." Thesis, University of York, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.298437.

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Weeks, Stacey. "Characterisation of the HSP70-HSP90 organising protein gene and its link to cancer." Thesis, Rhodes University, 2015. http://hdl.handle.net/10962/56006.

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HOP (Heat shock protein 70/ Heat shock protein 90 organising protein) is a co-chaperone essential for client protein transfer from HSP70 to HSP90 within the HSP90 chaperone machine and has been found to be up-regulated in various cancers. However, minimal in vitro information can be found on the regulation of HOP expression. The aim of this study was to analyse the HOP gene structure across known orthologues, identify and characterise the HOP promoter, and identify the regulatory mechanisms influencing the expression of HOP in cancer. We hypothesized that the expression of HOP in cancer cells is likely regulated by oncogenic signalling pathways linked to cis-elements within the HOP promoter. An initial study of the evolution of the HOP gene speciation was performed across identified orthologues using Mega5.2. The evolutionary pathway of the HOP gene was traced from the unicellular organisms to fish, to amphibian and then to land mammal. The synteny across the orthologues was identified and the co-expression profile of HOP analysed. We identified the putative promoter region for HOP in silico and in vitro. Luciferase reporter assays were utilized to demonstrate promoter activity of the upstream region in vitro. Bioinformatic analysis of the active promoter region identified a large CpG island and a range of putative cis-elements. Many of the cis-elements interact with transcription factors which are activated by oncogenic pathways. We therefore tested the regulation of HOP levels by rat sarcoma viral oncogene homologue (RAS). Cancer cell lines were transfected with mutated RAS to observe the effect of constitutively active RAS expression on the production of HOP using qRT-PCR and Western Blot analyses. Additionally, inhibitors of the RAS signalling pathway were utilised to confirm the regulatory effect of mutated RAS on HOP expression. In cancer cell lines containing mutated RAS (Hs578T), HOP was up-regulated via a mechanism involving the MAPK signalling pathway and the ETS-1 and C/EBPβ cis-elements within the HOP promoter. These findings suggest for the first time that Hop expression in cancer may be regulated by RAS activation of the HOP promoter. Additionally, this study allowed us to determine the murine system to be the most suited genetic model organism with which to study the function of human HOP.

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Silva, Luciana Pugliese da. "Estudo da expressão dos genes de choque térmico hsp90, hsp60 e hsp10 do fungo aquático Blastocladiella emersonii." Universidade de São Paulo, 2003. http://www.teses.usp.br/teses/disponiveis/46/46131/tde-14052018-120842/.

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A proteína de choque térmico Hsp90 é uma chaperone molecular encontrada no citosol. O cDNA incompleto desta proteína foi isolado de uma biblioteca construída a partir de mRNA de células de esporulação de B. emersonii submetidas a choque térmico. Um clone genômico contendo a seqüência completa do gene hsp90 também foi isolado, seqüenciado e caracterizado. A região codificadora do gene hsp90 é interrompida por um único íntron de 184 nucleotídeos. A seqüência de aminoácidos deduzida indicou uma proteína de 71 O resíduos, com massa molecular calculada de 80.792 Da e um pl médio de 4,85. Experimentos de extensão de oligonucleotídeo e RACE-PCR demonstraram um sítio único de início de transcrição localizado a -65 e -70 nucleotídeos do ATG da metionina iniciadora, respectivamente. Motivos similares ao consenso do elemento de choque térmico eucariótico (HSE) e do elemento responsivo a estresse (STRE) foram encontrados na região promotora do gene a -395 e -98 nucleotídeos do ATG, respectivamente. Experimentos de \"Northern blot\" revelaram que o mRNA para a Hsp90 apresenta níveis máximos aos 90 minutos da fase de esporulação do fungo. Análise por \"western blot\" mostrou que a proteína Hsp90 está presente durante todo o ciclo de vida do fungo e os níveis máximos de acúmulo foram observados aos 90 minutos da esporulação, indicando um controle transcricional do gene. Tanto a proteína quanto o mRNA são altamente induzidos quando as células são submetidas a choque térmico e a cádmio. As proteínas Hsp60 e Hsp10 são chaperones moleculares mitocondriais (chaperoninas). Os cDNAs completos destas proteínas foram isolados e totalmente seqüenciados. A seqüência de aminoácidos deduzida da Hsp60 corresponde a uma proteína de 559 resíduos, com massa molecular calculada em 58.741 Da e um pl médio de 8, 7. Experimentos de \"Northern blot\" revelaram que o mRNA para Hsp60 tem níveis máximos de expressão aos 90 minutos da esporulação. Análise por \"western blot\" mostrou que a Hsp60 está presente durante todo o ciclo de vida do fungo, com níveis máximos da proteína 90 minutos após a indução da esporulação. Tanto a proteína quanto o mRNA são bastante induzidos quando as células são submetidas ao choque térmico. A seqüência de aminoácidos deduzida da Hsp10 corresponde um polipeptídeo de 101 resíduos com massa molecular calculada em 10.688 Da e um pl médio de 6,25. Experimentos de \"Northern blot\" revelaram que o mRNA para Hsp10 tem níveis máximos de expressão aos 120 minutos da germinação e é bastante induzido quando as células são submetidas ao choque térmico.
The heat shock protein 90 (Hsp90) is a cytosolic molecular chaperone. The incomplete cDNA of this protein was isolated by immunoblot screening of a heat shock cDNA expression library. The complete genomic clone was also isolated and completely sequenced and characterized. The coding sequence is interrupted by a single intron with 184 nucleotides. The deduced amino acid sequence corresponds to a 710-residue polypeptide with a calculated molecular mass of 80,792 Da and an average pl of 4.85. Primer extension and RACE-PCR experiments demonstrated a single transcription start site localized -65 and -70 nucleotides from de ATG of the initiator methionine, respectively. Sequence motifs resembling the standard eukaryotic heat shock element (HSE) and the stress responsive element (STRE) were evident in the regulatory region -395 and -98 nucleotides from de ATG, respectively. Northern blot analysis revealed that the Hsp90 mRNA presents maximum levels by 90 minutes of the sporulation stage. Immunoblot analysis indicated that the Hsp90 is present during the entire life cycle of the fungus and maximum levels were observed 90 minutes after the induction of sporulation, indicating a transcriptional control. During heat shock both the mRNA and the Hsp90 protein are highly induced. Proteins Hsp60 and Hsp10, are mitochondrial molecular chaperones (chaperonines). The complete cDNAs encoding these proteins were and completely sequenced. The deduced amino acid sequence for Hsp60 corresponds to a 559-residue polypeptide with a calculated molecular mass of 58,741 Da and an average pl of 8.7. Immunoblot analysis showed that Hsp60 is present during the entire life cycle of the fungus and presents maximum levels by 90 minutes of the sporulation. Northern blot analysis indicated maximum levels of the Hsp60 mRNA by 90 minutes of sporulation too. Both mRNA and the protein are highly induced during heat shock. The deduced amino acid sequence for Hsp10 corresponds to a 101-residue polypeptide with a calculated molecular mass of 10,688 Da and an average pl of 6.25. Northern blot analysis indicated maximum mRNA levels by 120 minutes of germination and high levels of expression when the cells are exposed to heat shock.

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Mattison, Stacey. "Analysis of the human HSP70-HSP90 organising protein (HOP) gene - characterisation of the promoter and identification of a novel isoform." Thesis, Rhodes University, 2018. http://hdl.handle.net/10962/62821.

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Hu, Bin. "Functional analysis of the middle domain of Hsp90, and characterisation of QR12/NSE4, an essential cell cycle gene that is found in an Hsp90 complex." Thesis, King's College London (University of London), 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.424460.

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Sass, Jennifer Beth. "Heat-inducible and constitutive expression of the 90 kD heat shock protein gene, Hsp90, during zebrafish embryogenesis." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1998. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp02/NQ32798.pdf.

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Marsee, Derek K. "Exploration of novel therapies for thyroid cancer adenoviral gene therapy and 17-allylamino-17-demethoxygeldanamycin /." Connect to this title online, 2004. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1087497053.

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Thesis (Ph. D.)--Ohio State University, 2004.
Title from first page of PDF file. Document formatted into pages; contains xv, 118 p.; also includes graphics (some col.) Includes bibliographical references (p. 106-118). Available online via OhioLINK's ETD Center

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Jacob, Tiago Rinaldi. "Expressão, regulação e funcionalidade de genes HSPs no dermatófito Trichophyton rubrum." Universidade de São Paulo, 2014. http://www.teses.usp.br/teses/disponiveis/17/17135/tde-15052014-105536/.

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O dermatófito Trichophyton rubrum é um fungo filamentoso, queratinofílico e antropofílico, sendo o principal agente etiológico de micoses cutâneas em humanos. Sua distribuição cosmopolita e seu acometimento grave em pacientes imunocomprometidos fazem dele um dos desafios a ser enfrentado pelos serviços de saúde pública mundial. As interações patógeno-hospedeiro envolvem diferentes processos relacionados com a degradação de queratina e com modificações metabólicas que permitem sua adesão e posterior penetração nos tecidos infectados. Essas alterações são importantes para o sucesso do processo infeccioso e envolvem mecanismos que modulam a expressão gênica, a secreção de proteínas específicas, a adaptação metabólica e as alterações no pH cutâneo, fundamentais para o estabelecimento da infecção. Dentre as proteínas que participam do processo de interação patógeno-hospedeiro estão as proteínas de choque térmico HSPs (Heat Shock Proteins), relacionadas aos mais diversificados processos celulares. Nesse sentido, a hipótese desse trabalho foi avaliar se os genes hsps de T. rubrum, bem como seu principal fator de transcrição (Hsf1), estão envolvidos nos processos de resposta a situações adversas e na interação com o microambiente hospedeiro, e se estes genes são modulados pelo fator de transcrição pacC, um regulador envolvido na sinalização do pH ambiente. Para tanto, a expressão dos genes hsps foi analisada em resposta ao cultivo de T. rubrum em diferentes meios de cultura, durante a exposição a antifúngicos, estresse térmico e interação com fragmentos de unha e pele humanas. O envolvimento da Hsp90 na modulação da expressão gênica, na suscetibilidade a antifúngicos e na interação de T. rubrum com fragmentos de unha humana foi avaliado utilizando-se um inibidor químico específico para esta proteína. Os resultados indicam uma expressão variável dentre os genes hsps e até mesmo dentro de cada família HSP, em resposta a cada condição ambiental ou interação a que o fungo foi exposto. Além disto, temos indício de que a expressão dos genes hsps seja modulada pelo fator de transcrição PacC, através da modulação do fator de transcrição Hsf1. Constatamos ainda, a influência de Hsp90 na susceptibilidade de T. rubrum às drogas Itraconazol e Micafungina, e no desenvolvimento de T. rubrum em fragmentos de unha humana. Esses resultados revelam a participação das proteínas HSPs em diversos aspectos do metabolismo de T. rubrum, e sugerem a participação de Hsp90 na patogenicicade e na suscetibilidade a drogas deste dermatófito
The dermatophyte Trichophyton rubrum is a filamentous, keratinophilic, and anthrophophilic fungi, being the major etiologic agent of cutaneous mycoses in humans. Its cosmopolitan distribution and the severe infection in immunocompromised patients make it one of the challenges to be faced by public health agencies worldwide. Hostpathogen interactions involve different processes related to keratin degradation and metabolic changes that allow adhesion and subsequent penetration of the infected tissue. These changes are important to the success of the infectious process and involve mechanisms that modulate gene expression, secretion of specific proteins, and metabolic adaptation, and cutaneous pH changes, essential to the establishment of the infection. Among the proteins that participate in the host-pathogen interaction are the heat shoch proteins (HSPs), related to diverse cellular processes. Thus, the hypothesis of this work was to evaluate whether T. rubrum hsp genes, as well as their major transcription factor (Hsf1), are involved in the response to adverse situations and in the interaction with the host microenvironment, and if these genes are regulated by the transcription fator PacC, a regulator of the pH signaling pathway. The expression of the hsp genes was evaluated in response to the cultivation of T. rubrum in different culture medium, during exposure to antifungal drugs, heat stress, and interaction with human nail and skin. The involvement of T. rubrum Hsp90 in the modulation of gene expression, susceptibility to antifungal drugs, and interaction with human nails was evaluated by using a chemical inhibitor, specific to this protein. Our results indicate a variable expression of the hsp genes, even among members of the same HSP family, in response to each environmental condition or interaction, to which the fungus was exposed. Furthermore, we have evidence that the hsp gene expression is modulated by the PacC transcription factor, by modulating the expression of the Hsf1 coding gene. We also found that Hsp90 is involved in T. rubrum susceptibility to the drugs Itraconazole and Micafungin, and in the development of this dermatophyte in human nails. These results reveal the involvement of HSPs in several aspects of T. rubrum metabolism, suggesting a role for Hsp90 in the pathogenicity and drug susceptibility in this dermatophyte

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Coumailleau, Pascal. "I - clonage et expression d'un gene de la famille hsp90 au cours du developpement chez l'amphibien urodele pleurodeles waltlIi - signification de l'interaction entre la proteine hsp90 et deux facteurs de transcription a motif helice-boucle-helice(hlh)." Paris 5, 1996. http://www.theses.fr/1996PA05S029.

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Cette these a porte sur l'etude du role de certains membres de la famille des proteines de stress de 90kda (hsc90 ou hsp90) exprimes dans les conditions physiologiques. Cette analyse a ete realisee dans un premier temps in vivo par le clonage et l'etude de l'expression d'un gene hsc90 (strictement constitutif) au cours de l'ovogenese et de l'embryogenese chez l'amphibien pleurodeles waltl. Ces resultats nous ont permis d'analyser la distribution du messager hsc90 au cours de ces deux etapes-cles du developpement. La fabrication d'un anticorps dirige specifiquement contre hsc90 nous a permis de determiner la localisation cellulaire et tissulaire de cette proteine. Le role de cette proteine a ete ensuite envisagee au cours de l'ovogenese en inhibant la fonction de la proteine par microinjection d'anticorps. Une deuxieme approche, cette fois in vitro, nous a permis d'aborder le role de la proteine hsp90 exprimee dans un systeme acellulaire lors de son interaction avec des facteurs de transcription de la famille hlh (helix-loop-helix), facteurs pour la plupart impliques dans les processus de l'embryogenese. Le premier facteur etudie est le recepteur de la dioxine (dr) appele ainsi en raison de sa forte affinite notamment pour la dioxine, une substance xenobiotique et hautement cancerigene. Les resultats permettent de delimiter clairement un domaine sur le recepteur responsable a la fois de l'affinite pour la dioxine et de la proteine hsp90. Nos resultats suggerent fortement des proprietes de chaperon pour hsp90. La proteine sim (single minded protein) est un autre facteur de transcription a motif bhlh dont les etudes recentes suggerent des fonctions importantes dans la neurogenese. Nos resultats permettent de mettre en evidence que sim est une autre proteine cible d'hsp90 et que cette derniere pourrait reguler la fonction du facteur sim.

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MENG, XIA. "Clonage et regulation du gene hsp90 beta de poulet mutagenese de l'hsp90 : dimerisation, localisation subcellulaire et interaction in vivo avec le recepteur des oestrogenes." Paris 6, 1995. http://www.theses.fr/1995PA066666.

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Le clonage du gene hsp90 beta confirme que la duplication de l'hsp90 alpha et beta se situe, au cours de la phylogenese, a l'epoque de l'apparition des vertebres. De plus, le messager hsp90 beta aviaire n'est pas inductible par le stress thermique contrairement aux messagers hsp90 alpha et beta de mammiferes. Les stimuli mitogenes comme le serum et l'insuline, qui induisent le messager hsp90 alpha, n'augmentent pas le taux du messager hsp90 beta. Cette regulation differencielle des hsp90 alpha et beta de poulet, pourrait etre expliquee par les divergences majeures existant au niveau du promoteur. Dans le promoteur hsp90 beta une seule boite caat et un seul element de choc thermique (hsf) sont presents 3 et 2 kb en amont de la boite tata, respectivement. La mutagenese de l'hsp90 a ete realisee pour etudier son homodimerisation, sa localisation subcellulaire, et enfin son interaction in vivo avec le recepteur nucleaire des oestrogenes (re). L'analyse des cytosols des cellules cos7 apres transfection de l'hsp90 sauvage ou mutee a demontre que la deletion de 30 acides amines en c-terminal est suffisante pour empecher la formation de dimere, que la region c-terminale de 282 acides amines est suffisante pour l'homo-dimerisation et que les deletions de plusieurs sous-regions dans cette partie empechent egalement la dimerisation de l'hsp90. L'analyse de la localisation subcellulaire des mutants exprimes dans les cellules cos7 a montre une localisation nucleaire de la region n-terminale de 285 acides amines, contenant des signaux de localisation nucleaire potentiels. Cette fonction est masquee dans les mutants moins deletes en c-terminal et dans la proteine sauvage. L'interaction in vivo entre l'hsp90 sauvage cytoplasmique et le re nucleaire est observee apres co-expression des deux proteines et re-localisation specifique d'une partie de l'hsp90 dans le noyau, a cause de son interaction avec le re. Plusieurs mutants cytoplasmiques ont ete testes pour leur capacite a migrer du cytoplasme vers le noyau via l'interaction avec le re. Nous avons montre que l'abolition de la dimerisation de l'hsp90 ne bloquait pas necessairement son interaction in vivo avec le re, ceci suggere que la dimerisation de l'hsp90 et son interaction avec le re sont deux fonctions distinctes

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Books on the topic "Hsp90 gene"

1

Nicholson, Richard Charles. The HSP70 multi-gene family in saccharomyces cerevisiae. 1987.

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Lowe, David George. Characterization of the mouse major heat shock protein (HSP70) gene family. 1985.

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(Editor), R. J. Mayer, I. R. Brown (Editor), and Peter Jenner (Series Editor), eds. Heat Shock Proteins in the Nervous System (Neuroscience Perspectives). Academic Press, 1994.

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(Editor), R. J. Mayer, I. R. Brown (Editor), and Peter Jenner (Series Editor), eds. Heat Shock Proteins in the Nervous System (Neuroscience Perspectives). Academic Press, 1994.

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Book chapters on the topic "Hsp90 gene"

1

Adhikari, Susanta Sekhar, Sujan Kumar Mondal, and Rajkumar Banerjee. "Gene Therapy Against HSP90: Glucocorticoid Receptor-Assisted Cancer Treatment." In Heat Shock Proteins, 219–56. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-17211-8_12.

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Hartl, Franz Ulrich. "The Role of Molecular Chaperones Hsp70 And Hsp60 in Protein Folding." In Post-transcriptional Control of Gene Expression, 193–206. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-642-60929-9_17.

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Baulieu, Etienne-Emile. "Is the hsp90 Connection Between Steroid Receptors and Immunosuppressant Binding Immunophilins Involved in the Control of Gene Transcription and Cell Growth?" In Hormonal Carcinogenesis II, 150–55. New York, NY: Springer New York, 1996. http://dx.doi.org/10.1007/978-1-4612-2332-0_17.

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Howarth, Joanna, Do-Young Lee, and James B. Uney. "Use of Viral Gene Delivery Systems to Investigate the Neuroprotective Roles of Hsp70 and Hsp40 Proteins." In Heat Shock Proteins and the Brain: Implications for Neurodegenerative Diseases and Neuroprotection, 223–37. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-8231-3_11.

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Petersen, Robert B., and Susan Lindquist. "Differential mRNA Stability: A Regulatory Strategy for Hsp70 Synthesis." In Post-Transcriptional Control of Gene Expression, 83–91. Berlin, Heidelberg: Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-75139-4_9.

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Shapira, Michal, Juan G. McEwen, and Charles L. Jaffe. "In Vitro and in Vivo Differentiation of L.Mexicana-Hsp70 Gene Expression." In Leishmaniasis, 575–79. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4613-1575-9_70.

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Li, G. C., L. Li, R. Liu, J. Y. Mak, and W. Lee. "Stable Expression of Human HSP70 Gene in Rodent Cells Confers Thermal Resistance." In Heat Shock, 257–67. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-76679-4_28.

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Brown, Ian R. "Expression of Heat Shock Genes (hsp70) in the Mammalian Nervous System." In Results and Problems in Cell Differentiation, 217–29. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-540-46712-0_15.

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Takenaka, Ivone M., Seth Sadis, and Lawrence E. Hightower. "Transforming Growth Factor-ß Regulates Basal Expression of the hsp70 Gene Family in Cultured Chicken Embryo Cells." In Results and Problems in Cell Differentiation, 188–209. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-540-46712-0_13.

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Singh, N. K., Preethi Rao, and Alexzander Asea. "Silencing of Metastasis-associated Gene 1 (Mta1) Stimulates Hsp70 Cellular Release and Neurite extension in Neuroblastoma Cells." In Heat Shock Proteins and the Brain: Implications for Neurodegenerative Diseases and Neuroprotection, 273–82. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-8231-3_14.

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Conference papers on the topic "Hsp90 gene"

1

Wang, Gang. "Drosophila Hsp90 Gene Can be Upregulated by Ecdysone." In 2015 International Conference on Education, Management, Information and Medicine. Paris, France: Atlantis Press, 2015. http://dx.doi.org/10.2991/emim-15.2015.158.

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Li, Tao, Farideh Mehraein-Ghomi, Sanjeev V. Namjoshi, Lynette M. Phillips, Elizabeth A. Ballard, Mary E. Forbes, ping-Chieh Chou, Xuejun Yang, and Wei Zhang. "Abstract 1736: Targeting Hsp90-Cdc37 complex overcomes drug resistance in glioma cells harboring FGFR3-TACC3 fusion gene." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-1736.

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Puteri, S. A., S. B. Aritonang, H. T. Nussa, A. F. Rahmani, A. Bowolaksono, and R. Lestari. "The profile of HSP90 gene expression of Bali cattle to heat stress in West Sumbawa, West Nusa Tenggara." In PROCEEDINGS OF THE 3RD INTERNATIONAL SYMPOSIUM ON CURRENT PROGRESS IN MATHEMATICS AND SCIENCES 2017 (ISCPMS2017). Author(s), 2018. http://dx.doi.org/10.1063/1.5064135.

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Venkatesan, Thiagarajan, Ali Alaseem, Khalid Alhazzani, Priya Dondapati, Saad Alobid, and Appu Rathinavelu. "Abstract 1839: Analysis of cell cycle-related gene expressions in MDM2-transfected LNCaP-MST cells after inhibition of HSP90." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-1839.

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Venkatesan, Thiagarajan, Ali Alaseem, Khalid Alhazzani, and Appu Rathinavelu. "Abstract 81: Effect of HSP90 inhibition on the gene expression profile of MDM2 transfected LNCaP-MST prostate cancer cells." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-81.

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Shee, K., MH Ung, C. Cheng, and TW Miller. "Abstract P1-07-04: Unique overlapping subtypes of triple-negative breast and ovarian cancers and sensitivity of “mesenchymal-like” cancers to HSP90 inhibition is revealed by integrated gene expression and drug sensitivity profiling." In Abstracts: 2016 San Antonio Breast Cancer Symposium; December 6-10, 2016; San Antonio, Texas. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.sabcs16-p1-07-04.

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Beckham, Josh T., J. A. Baran, A. D. Izzo, and E. Duco Jansen. "Optical imaging of Hsp70 gene expression following thermal laser injury." In BiOS 2001 The International Symposium on Biomedical Optics, edited by Donald D. Duncan, Steven L. Jacques, and Peter C. Johnson. SPIE, 2001. http://dx.doi.org/10.1117/12.434723.

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Albuquerque Filho, José Marcos Vieira de, Natália Merten Athayde, Alzira Alves de Siqueira Carvalho, Igor Braga Farias, Roberta Ismael Lacerda Machado, and Marco Antônio Troccoli Chieia. "Familial ALS Type 25 – A Brazillian Case Serie." In XIII Congresso Paulista de Neurologia. Zeppelini Editorial e Comunicação, 2021. http://dx.doi.org/10.5327/1516-3180.186.

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Introduction: Familial Amyotrophic Lateral Sclerosis (fALS) represent 5-10% of ALS patients. Different mutations in the N-terminal motor or coiled-coil domains of the kinesin family member 5A (KIF5A) cause Hereditary Spastic Paraplegia Type 10 (HSP10), Charcot-Marie-Tooth 2 (CMT2), Neonatal Intractable Myoclonus and more recently described fALS Type 25. Previous described phenotypes are very similar to the sporadic type, except from the long course of disease. Methods: We describe four Brazillian patients, under clinical follow-up on two Neuromuscular services with genetic diagnosis of fALS25. Results: Four diferent fALS25 are described. Two brothers and two unrelated patients, with distinct features, three males and one female, age range from 72 to 24; age of onset ranged from 62 to 22. The genetic mutations were the following: simple heterozygous pathogenic variant c.1651C>G (p. Leu551Val), simple heterozygous pathogenic variant c.2953G>A (p. Gly985Ser) and pathogenic variant c.484C>T (p.Arg162Trp); all of KIF5A gene (fALS25). Only one patient presented with similar phenoptype and age of onset as sporadic ALS (sALS), the two brothers presented the symptoms at the ages of 28 and 30, the female patient at 22. All patients still walk without assistence after the diagnosis. All patients showed classic superior and inferior motor neuron involvement signs, but one brother had a mild limb ataxia. The three younger patients had MRI with no specific findings, except from subtle cortical atrophy in one brother, and mild vermis and corpus callosum atrophy on the other brother. Only the female patient had negative familiar history. Conclusions: fALS25 should be suspected in patient with fALS and longer course disease. Mutations KIF5A gene must be remembered either in juvenile form of ALS.

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Mbofung, Rina M., Jodi A. McKenzie, Shruti Malu, Chengwen Liu, Weiyi Peng, Isere Kuiatse, Leila Williams, et al. "Abstract B105: HSP90 inhibitor, ganetespib, enhances responses to cancer immunotherapy through increased expression of interferon response genes." In Abstracts: Second CRI-CIMT-EATI-AACR International Cancer Immunotherapy Conference: Translating Science into Survival; September 25-28, 2016; New York, NY. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/2326-6066.imm2016-b105.

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Mbofung, Rina M., Jodi A. McKenzie, Shruti Malu, Chengwen Liu, Leila Williams, Weiyi Peng, Zhe Wang, et al. "Abstract 4360: Inhibition of HSP90 enhances T cell-mediated antitumor immune responses through expression of interferon-alpha response Genes." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-4360.

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Reports on the topic "Hsp90 gene"

1

Ghanim, Murad, Joe Cicero, Judith K. Brown, and Henryk Czosnek. Dissection of Whitefly-geminivirus Interactions at the Transcriptomic, Proteomic and Cellular Levels. United States Department of Agriculture, February 2010. http://dx.doi.org/10.32747/2010.7592654.bard.

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Our project focuses on gene expression and proteomics of the whitefly Bemisia tabaci (Gennadius) species complex in relation to the internal anatomy and localization of expressed genes and virions in the whitefly vector, which poses a major constraint to vegetable and fiber production in Israel and the USA. While many biological parameters are known for begomovirus transmission, nothing is known about vector proteins involved in the specific interactions between begomoviruses and their whitefly vectors. Identifying such proteins is expected to lead to the design of novel control methods that interfere with whitefly-mediated begomovirus transmission. The project objectives were to: 1) Perform gene expression analyses using microarrays to study the response of whiteflies (B, Q and A biotypes) to the acquisition of begomoviruses (Tomato yellow leaf curl (TYLCV) and Squash leaf curl (SLCV). 2) Construct a whitefly proteome from whole whiteflies and dissected organs after begomovirus acquisition. 3) Validate gene expression by q-RTPCR and sub-cellular localization of candidate ESTs identified in microarray and proteomic analyses. 4) Verify functionality of candidate ESTs using an RNAi approach, and to link these datasets to overall functional whitefly anatomical studies. During the first and second years biological experiments with TYLCV and SLCV acquisition and transmission were completed to verify the suitable parameters for sample collection for microarray experiments. The parameters were generally found to be similar to previously published results by our groups and others. Samples from whole whiteflies and midguts of the B, A and Q biotypes that acquired TYLCV and SLCV were collected in both the US and Israel and hybridized to B. tabaci microarray. The data we analyzed, candidate genes that respond to both viruses in the three tested biotypes were identified and their expression that included quantitative real-time PCR and co-localization was verified for HSP70 by the Israeli group. In addition, experiments were undertaken to employ in situ hybridization to localize several candidate genes (in progress) using an oligonucleotide probe to the primary endosymbiont as a positive control. A proteome and corresponding transcriptome to enable more effective protein identification of adult whiteflies was constructed by the US group. Further validation of the transmission route of begomoviruses, mainly SLCV and the involvement of the digestive and salivary systems was investigated (Cicero and Brown). Due to time and budget constraints the RNAi-mediated silencing objective to verify gene function was not accomplished as anticipated. HSP70, a strong candidate protein that showed over-expression after TYLCV and SLCV acquisition and retention by B. tabaci, and co-localization with TYLCV in the midgut, was further studies. Besides this protein, our joint research resulted in the identification of many intriguing candidate genes and proteins that will be followed up by additional experiments during our future research. To identify these proteins it was necessary to increase the number and breadth of whitefly ESTs substantially and so whitefly cDNAs from various libraries made during the project were sequenced (Sanger, 454). As a result, the proteome annotation (ID) was far more successful than in the initial attempt to identify proteins using Uniprot or translated insect ESTs from public databases. The extent of homology shared by insects in different orders was surprisingly low, underscoring the imperative need for genome and transcriptome sequencing of homopteran insects. Having increased the number of EST from the original usable 5500 generated several years ago to >600,000 (this project+NCBI data mining), we have identified about one fifth of the whitefly proteome using these new resources. Also we have created a database that links all identified whitefly proteins to the PAVEdb-ESTs in the database, resulting in a useful dataset to which additional ESTS will be added. We are optimistic about the prospect of linking the proteome ID results to the transcriptome database to enable our own and other labs the opportunity to functionally annotate not only genes and proteins involved in our area of interest (whitefly mediated transmission) but for the plethora of other functionalities that will emerge from mining and functionally annotating other key genes and gene families in whitefly metabolism, development, among others. This joint grant has resulted in the identification of numerous candidate proteins involved in begomovirus transmission by B. tabaci. A next major step will be to capitalize on validated genes/proteins to develop approaches to interfere with the virus transmission.

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Dolja, Valerian V., Amit Gal-On, and Victor Gaba. Suppression of Potyvirus Infection by a Closterovirus Protein. United States Department of Agriculture, March 2002. http://dx.doi.org/10.32747/2002.7580682.bard.

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The plant virus family Polyviridae is the largest and most destructive of all plant viruses. Despite the continuous effort to develop resistant plant varieties, there is a desperate need for novel approaches conferring wide-range potyvirus resistance. Based on experiments with the tobacco etch potyvirus (TEV)-derived gene expression vector, we suggested approach for screening of the candidate resistance genes. This approach relies on insertion of the genes into a virus vector and evaluation of the phenotypes of the resulting recombinant viruses. The genes which suppress infection by the recombinant virus are selected as candidates for engineering transgenic resistance. Our analysis of the TEV variants expressing proteins of the beet yellows closterovirus (BYV) revealed that one of those, the leader proteinase (L-Pro), strongly and specifically interfered with the hybrid TEV infection. Since closterovirus L-Pro is evolutionary related to potyviral helper component-proteinase (HC-Pro), we suggested that the L-Pro interfered with HC-Pro function via a trans-dominant inhibitory effect. Based on these findings, we proposed to test two major hypotheses. First, we suggested that L-Pro-mediated suppression of potyvirus infection is a general phenomenon effective against a range of potyviruses. The second hypothesis stated that the suppression effect can be reproduced in transgenic plants expressing L-Pro, and can be utilized for generation of resistance to potyviruses. In accord with these hypotheses, we developed two original objectives of our proposal: A) to determine the range of the closterovirus-derived suppression of potyviral infection, and B) to try and utilize the L-Pro-mediated suppression for the development of transgenic resistance to potyviruses. In the first phase of the project, we have developed all major tools and technologies required for successful completion of the proposed research. These included TEV and ZYMV vectors engineered to express several closteroviral L-Pro variants, and generation of the large collection of transgenic plants. To our satisfaction, characterization of the infection phenotypes exhibited by chimeric TEV and ZYMV variants confirmed our first hypothesis. For instance, similar to TEV-L- Pro(BYV) chimera, ZYMV-L-Pro(LIYV) chimera was debilitated in its systemic spread. In contrast, ZYMV-GUS chimera (positive control) was competent in establishing vigorous systemic infection. These and other results with chimeric viruses indicated that several closteroviral proteinases inhibit long-distance movement of the potyviruses upon co-expression in infected plants. In order to complete the second objective, we have generated ~90 tobacco lines transformed with closteroviral L-Pro variants, as well as ~100 lines transformed with BYV Hsp70-homolog (Hsp70h; a negative control). The presence and expression of the trans gene in each line was initially confirmed using RT-PCR and RNA preparations isolated from plants. However, since detection of the trans gene-specific RNA can not guarantee production of the corresponding protein, we have also generated L-Pro- and Hsp70h-specific antisera using corresponding synthetic peptides. These antisera allowed us to confirm that the transgenic plant lines produced detectable, although highly variable levels of the closterovirus antigens. In a final phase of the project, we tested susceptibility of the transgenic lines to TEV infection. To this end, we determined that the minimal dilution of the TEV inoculum that is still capable of infecting 100% of nontransgenic plants was 1:20, and used 10 plants per line (in total, ~2,000 plants). Unfortunately, none of the lines exhibited statistically significant reduction in susceptibility. Although discouraging, this outcome prompted us to expand our experimental plan and conduct additional experiments. Our aim was to test if closteroviral proteinases are capable of functioning in trans. We have developed agroinfection protocol for BYV, and tested if co- expression of the L-Pro is capable of rescuing corresponding null-mutant. The clear-cut, negative results of these experiments demonstrated that L-Pro acts only in cis, thus explaining the lack of resistance in our transgenic plants. We have also characterized a collection of the L-Pro alanine- scanning mutants and found direct genetic evidence of the requirement for L-Pro in virus systemic spread. To conclude, our research supported by BARD confirmed one but not another of our original hypotheses. Moreover, it provided an important insight into functional specialization of the viral proteinases and generated set of tools and data with which we will be able to address the molecular mechanisms by which these proteins provide a variety of critical functions during virus life cycle.

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