Helicobacter pylori HtrA is a new secreted virulence factor that cleaves E‐cadherin to disrupt intercellular adhesion
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Mammalian and prokaryotic high-temperature requirement A (HtrA) proteins are chaperones and serine proteases with important roles in protein quality control. Here, we describe an entirely new function of HtrA and identify it as a new secreted virulence factor from Helicobacter pylori, which cleaves the ectodomain of the cell-adhesion protein E-cadherin. E-cadherin shedding disrupts epithelial barrier functions allowing H. pylori designed to access the intercellular space. We then designed a small-molecule inhibitor that efficiently blocks HtrA activity, E-cadherin cleavage and intercellular entry of H. pylori.
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The zinc-protease PqqE and the serine-protease HtrA disrupt gastric mucosal integrity and thereby facilitate bacterial invasion.
“the zinc-protease PqqE and the serine-protease HtrA disrupt gastric mucosal integrity61–63 and thereby facilitate bacterial invasion.”
From The emerging roles of bacterial proteases in intestinal diseases (2023) · cites this paper as [63]
Tight junctions are targets of infectious agents such as Pseudomonas aeruginosa (through LasB), H. pylori (PqqE and HtrA), C. jejuni (HtrA), V. cholerae (vibrolysin), Shigella, Salmonella or pathogenic Escherichia coli (SepA).
“Tight junctions are also targets of infectious agents such as Pseudomonas aeruginosa (through LasB),132 H. pylori (PqqE and HtrA),61–63 C. jejuni (HtrA), 79,80 V. cholerae (vibrolysin),10,83 Shigella, Salmonella or pathogenic Escherichia coli (SepA).72,133”
From The emerging roles of bacterial proteases in intestinal diseases (2023) · cites this paper as [63]
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 · see citing works
Helicobacter pylori and gastrointestinal tract adenocarcinomas
Peek, R. M., & Blaser, M. J. (2002) · Nature reviews. Cancer · doi:10.1038/nrc703 · Cited by 1,807 · see citing works
Disruption of the Epithelial Apical-Junctional Complex by Helicobacter pylori CagA
Amieva, M. R., Vogelmann, R., Covacci, A., Tompkins, L. S., Nelson, W. J., & Falkow, S. (2003) · Science · doi:10.1126/science.1081919 · Cited by 739 · see citing works
Release of an invasion promoter E-cadherin fragment by matrilysin and stromelysin-1
Noë, V., Fingleton, B., Jacobs, K., Crawford, H. C., Vermeulen, S. J. T., Steelant, W. F. A., Bruyneel, E. A., Matrisian, L. M., & Mareel, M. M. K. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.1.111 · Cited by 697 · see citing works
Maretzky, T., Reiß, K., Ludwig, A., Buchholz, J., Scholz, F., Proksch, E., Strooper, B. D., Hartmann, D., & Säftig, P. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500918102 · Cited by 663 · see citing works
Helicobacter pylori VacA, a paradigm for toxin multifunctionality
Cover, T. L., & Blanke, S. R. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1095 · Cited by 569 · see citing works
Murata-Kamiya, N., Kurashima, Y., Teishikata, Y., Yamahashi, Y., Saito, Y., Higashi, H., Aburatani, H., Akiyama, T., Peek, R. M., Azuma, T., et al. (2007) · Oncogene · doi:10.1038/sj.onc.1210251 · Cited by 468 · see citing works
Structural basis for the regulated protease and chaperone function of DegP
Krojer, T. J., Sawa-Makarska, J. Z., Schäfer, E., Saibil, H. R., Ehrmann, M., & Clausen, T. (2008) · Nature · doi:10.1038/nature07004 · Cited by 368 · see citing works
Global Transposon Mutagenesis and Essential Gene Analysis of Helicobacter pylori
Salama, N. R., Shepherd, B., & Falkow, S. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.23.7926-7935.2004 · Cited by 309 · see citing works
The Role of Human HtrA1 in Arthritic Disease
Grau, S., Richards, P. J., Kerr, B. C., Hughes, C., Caterson, B., Williams, A. S., JUNKER, U., Jones, S. A., Clausen, T., & Ehrmann, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500361200 · Cited by 290 · see citing works
Papini, E., Satin, B., Norais, N., de Bernard, M., Telford, J. L., Rappuoli, R., & Montecucco, C. (1998) · Journal of Clinical Investigation · doi:10.1172/jci2764 · Cited by 248 · see citing works
Necchi, V., Candusso, M. E., Tava, F., Luinetti, O., Ventura, U., Fiocca, R., Ricci, V., & Solcia, E. (2007) · Gastroenterology · doi:10.1053/j.gastro.2007.01.049 · Cited by 243 · see citing works
Primary structure of a putative serine protease specific for IGF‐binding proteins
Zumbrunn, J., & Trüeb, B. (1996) · FEBS Letters · doi:10.1016/s0014-5793(96)01229-x · Cited by 212 · see citing works
Wroblewski, L. E., Shen, L., Ogden, S., Romero–Gallo, J., Lapierre, L. A., Israel, D. A., Turner, J. R., & Peek, R. M. (2009) · Gastroenterology · doi:10.1053/j.gastro.2008.10.011 · Cited by 193 · see citing works
Proteases in bacterial pathogenesis
Ingmer, H., & Brøndsted, L. (2009) · Research in Microbiology · doi:10.1016/j.resmic.2009.08.017 · Cited by 172 · see citing works
Jiang, J., Zhang, X., Chen, Y., Wu, Y., Zhou, Z. H., Chang, Z., & Sui, S. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805464105 · Cited by 160 · see citing works
Chan, A. O. O. (2006) · World Journal of Gastroenterology · doi:10.3748/wjg.v12.i2.199 · Cited by 118 · see citing works
Molecular mechanisms of epithelial-barrier disruption by Helicobacter pylori
Weßler, S., & Backert, S. (2008) · Trends in Microbiology · doi:10.1016/j.tim.2008.05.005 · Cited by 113 · see citing works
Self-citationLöwer, M., Weydig, C., Metzler, D., Reuter, A., Starzinski‐Powitz, A., Weßler, S., & Schneider, G. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003510 · Cited by 84 · see citing works
Self-citationMeltzer, M., Hasenbein, S., Mamant, N., Merdanovic, M., Poepsel, S., Hauske, P., Kaiser, M., Huber, R., Krojer, T. J., Clausen, T., et al. (2009) · Research in Microbiology · doi:10.1016/j.resmic.2009.07.012 · Cited by 77 · see citing works
p120 and Kaiso RegulateHelicobacter pylori-induced Expression of Matrix Metalloproteinase-7
Ogden, S. R., Wroblewski, L. E., Weydig, C., Romero–Gallo, J., O’Brien, D., Israel, D. A., Krishna, U. S., Fingleton, B., Reynolds, A. B., Weßler, S., et al. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-03-0283 · Cited by 72 · see citing works
Self-citationWeydig, C., Starzinski‐Powitz, A., Carra, G., Löwer, J., & Weßler, S. (2007) · Experimental Cell Research · doi:10.1016/j.yexcr.2007.07.015 · Cited by 69 · see citing works
Self-citationEctodomain shedding of E-cadherin and c-Met is induced by Helicobacter pylori infection
Schirrmeister, W., Gnad, T., Wex, T., Higashiyama, S., Wolke, C., Naumann, M., & Lendeckel, U. (2009) · Experimental Cell Research · doi:10.1016/j.yexcr.2009.07.029 · Cited by 59 · see citing works
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Clausen, T., Kaiser, M., Huber, R., & Ehrmann, M. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3065 · Cited by 479 · see citing works
Baj, J., Forma, A., Sitarz, M., Portincasa, P., Garruti, G., Krasowska, D., & Maciejewski, R. (2020) · Cells · doi:10.3390/cells10010027 · Cited by 389 · see citing works
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Tegtmeyer, N., Weßler, S., & Backert, S. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08035.x · Cited by 250 · see citing works
Self-citationHelicobacter pylori: an up-to-date overview on the virulence and pathogenesis mechanisms
Sharndama, H. C., & Mba, I. E. (2022) · Brazilian Journal of Microbiology · doi:10.1007/s42770-021-00675-0 · Cited by 266 · see citing works
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Paredes, J., Figueiredo, J., Albergaria, A., Oliveira, P., Carvalho, J., Ribeiro, A. S., Caldeira, J., Costa, Â. M., Simões‐Correia, J., Oliveira, M. J., et al. (2012) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2012.05.002 · Cited by 230 · see citing works
The impacts of H. pylori virulence factors on the development of gastroduodenal diseases
Chang, W.-L., Yeh, Y.-C., & Sheu, B. (2018) · Journal of Biomedical Science · doi:10.1186/s12929-018-0466-9 · Cited by 221 · see citing works
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Agbowuro, A. A., Huston, W. M., Gamble, A. B., & Tyndall, J. D. A. (2017) · Medicinal Research Reviews · doi:10.1002/med.21475 · Cited by 188 · see citing works
Posselt, G., Backert, S., & Weßler, S. (2013) · Cell Communication and Signaling · doi:10.1186/1478-811x-11-77 · Cited by 179 · see citing works
Self-citationProtein Quality Control in the Bacterial Periplasm
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Chhibber‐Goel, J., Singhal, V., Bhowmik, D., Vivek, R., Parakh, N., Bhargava, B., & Sharma, A. (2016) · npj Biofilms and Microbiomes · doi:10.1038/s41522-016-0009-7 · Cited by 179 · see citing works
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Self-citationElmi, A., Nasher, F., Jagatia, H., Gundogdu, O., Bajaj‐Elliott, M., Wren, B. W., & Dorrell, N. (2015) · Cellular Microbiology · doi:10.1111/cmi.12534 · Cited by 146 · see citing works
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Wroblewski, L. E., & Peek, R. M. (2013) · Gastroenterology Clinics of North America · doi:10.1016/j.gtc.2013.01.006 · Cited by 126 · see citing works
Hansen, G., & Hilgenfeld, R. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1076-4 · Cited by 123 · see citing works
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Steck, N., Mueller, K., Schemann, M., & Haller, D. (2011) · Gut · doi:10.1136/gutjnl-2011-300775 · Cited by 119 · see citing works
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Vaca, D. J., Thibau, A., Schütz, M. S., Kraiczy, P., Happonen, L., Malmström, J. A., & Kempf, V. A. J. (2019) · Medical Microbiology and Immunology · doi:10.1007/s00430-019-00644-3 · Cited by 117 · see citing works
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Self-citationRamírez-Larrota, J. S., & Eckhard, U. (2022) · Biomolecules · doi:10.3390/biom12020306 · Cited by 108 · see citing works
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Arnold, I. C., Zigova, Z., Holden, M. T. G., Lawley, T. D., Rad, R., Dougan, G., Falkow, S., Bentley, S. D., & Mueller, A. (2011) · Genome Biology and Evolution · doi:10.1093/gbe/evr022 · Cited by 94 · see citing works
Wiedemann, T., Hofbaur, S., Tegtmeyer, N., Huber, S., Sewald, N., Weßler, S., Backert, S., & Rieder, G. (2012) · Gut · doi:10.1136/gutjnl-2011-300525 · Cited by 102 · see citing works
Self-citationBackert, S., & Tegtmeyer, N. (2017) · Toxins · doi:10.3390/toxins9040115 · Cited by 95 · see citing works
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Self-citationDiffuse Gastric Cancer: A Summary of Analogous Contributing Factors for Its Molecular Pathogenicity
Ansari, S., Gantuya, B., Tuan, V. P., & Yamaoka, Y. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19082424 · Cited by 90 · see citing works
A single-nucleotide polymorphism in Helicobacter pylori promotes gastric cancer development
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Self-citationCarneiro, P., Fernandes, M. S., Figueiredo, J., Caldeira, J., Carvalho, J., Pinheiro, H. C., Leite, M., Melo, S., Oliveira, P., Simões‐Correia, J., et al. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.07.045 · Cited by 89 · see citing works
Schmidt, T. P., Perna, A. M., Fugmann, T., Böhm, M., Hiss, J. A., Haller, S., Goetz, C., Tegtmeyer, N., Hoy, B., Rau, T. T., et al. (2016) · Scientific Reports · doi:10.1038/srep23264 · Cited by 89 · see citing works
Self-citationHelicobacter pylori CagA: From Pathogenic Mechanisms to Its Use as an Anti-Cancer Vaccine
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Cassone, M., Gagne, A. L., Spruce, L. A., Seeholzer, S. H., & Sebert, M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.391482 · Cited by 86 · see citing works
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Self-citationAnalysis of Surface-Exposed Outer Membrane Proteins in Helicobacter pylori
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Sankaran, S., Ammanath, A. V., Biswas, R., Anita, B., Sukumaran, S., & Venkidasamy, B. (2022) · Microbial Pathogenesis · doi:10.1016/j.micpath.2022.105594 · Cited by 56 · see citing works
Löwer, M., Geppert, T., Schneider, P., Hoy, B., Weßler, S., & Schneider, G. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017986 · Cited by 55 · see citing works
Self-citationZarzecka, U., Modrak‐Wójcik, A., Figaj, D., Apanowicz, M., Lesner, A., Bzowska, A., Lipińska, B., Zawilak-Pawlik, A. M., Backert, S., & Skórko‐Glonek, J. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.00961 · Cited by 56 · see citing works
Self-citationColeman, J. L., Crowley, J. T., Toledo, A. M., & Benach, J. L. (2013) · Molecular Microbiology · doi:10.1111/mmi.12213 · Cited by 54 · see citing works
HtrA is a major virulence determinant of Bacillus anthracis
Chitlaru, T., Zaide, G., Ehrlich, S., Inbar, I., Cohen, O., & Avigdor Shafferman, C. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07790.x · Cited by 54 · see citing works
Simister, P. C., & Feller, S. M. (2011) · Molecular BioSystems · doi:10.1039/c1mb05272a · Cited by 54 · see citing works
Russell, T. M., Delorey, M. J., & Johnson, B. J. B. (2013) · Molecular Microbiology · doi:10.1111/mmi.12377 · Cited by 53 · see citing works
Impact ofHelicobacter pylorion the healing process of the gastric barrier
Mnich, E., Kowalewicz‐Kulbat, M., Sicińska, P., Hinc, K., Obuchowski, M., Gajewski, A., Moran, A. P., & Chmiela, M. (2016) · World Journal of Gastroenterology · doi:10.3748/wjg.v22.i33.7536 · Cited by 52 · see citing works
Postinfection Irritable Bowel Syndrome
Downs, I. A., Aroniadis, O. C., Kelly, L., & Brandt, L. J. (2017) · Journal of Clinical Gastroenterology · doi:10.1097/mcg.0000000000000924 · Cited by 52 · see citing works
L yme disease spirochaetes possess an aggrecan‐binding protease with aggrecanase activity
Russell, T. M., & Johnson, B. J. B. (2013) · Molecular Microbiology · doi:10.1111/mmi.12276 · Cited by 50 · see citing works
Bacterial serine protease HtrA as a promising new target for antimicrobial therapy?
Weßler, S., Schneider, G., & Backert, S. (2017) · Cell Communication and Signaling · doi:10.1186/s12964-017-0162-5 · Cited by 50 · see citing works
Self-citationHarrer, A., Boehm, M., Backert, S., & Tegtmeyer, N. (2017) · Gut Pathogens · doi:10.1186/s13099-017-0189-6 · Cited by 50 · see citing works
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Perna, A. M., Rodrigues, T., Schmidt, T. P., Böhm, M., Stutz, K., Reker, D., Pfeiffer, B., Altmann, K., Backert, S., Weßler, S., et al. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201504035 · Cited by 49 · see citing works
Self-citationTegtmeyer, N., & Backert, S. (2011) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2010.11.006 · Cited by 48 · see citing works
Self-citationAbfalter, C. M., Schubert, M., Goetz, C., Schmidt, T. P., Posselt, G., & Weßler, S. (2016) · Cell Communication and Signaling · doi:10.1186/s12964-016-0153-y · Cited by 48 · see citing works
Implications of the Human Gut–Brain and Gut–Cancer Axes for Future Nanomedicine
Javed, I., Cui, X., Wang, X., Mortimer, M., Andrikopoulos, N. K., Li, Y., Davis, T. P., Zhao, Y., Ke, P. C., & Chen, C. (2020) · ACS Nano · doi:10.1021/acsnano.0c07258 · Cited by 47 · see citing works
Hou, Y., Lin, H., Zhu, L., Liu, Z., Hu, F., Shi, J., Yang, T., Shi, X., Zhu, M., Godley, B. F., et al. (2013) · Arthritis & Rheumatism · doi:10.1002/art.38124 · Cited by 47 · see citing works
HtrA Is Important for Stress Resistance and Virulence in Haemophilus parasuis
Zhang, L., Li, Y., Wen, Y., Lau, G. W., Huang, X., Wu, R. J., Yan, Q., Huang, Y., Zhao, Q., Ma, X., et al. (2016) · Infection and Immunity · doi:10.1128/iai.00147-16 · Cited by 47 · see citing works
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SUTTON, P. R. N., & Chionh, Y. T. (2013) · Expert Review of Vaccines · doi:10.1586/erv.13.20 · Cited by 47 · see citing works
Bacterial extracellular vesicles – brain invaders? A systematic review
Kaisanlahti, A., Salmi, S., Kumpula, S., Amatya, S. B., Turunen, J., Tejesvi, M. V., Byts, N., Tapiainen, T., & Reunanen, J. (2023) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2023.1227655 · Cited by 46 · see citing works
Adherens junctions as targets of microorganisms: A focus on Helicobacter pylori
Costa, Â. M., Leite, M., Seruca, R., & Figueiredo, C. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.12.008 · Cited by 46 · see citing works
Wang, Y., Sun, Y., Wang, Y., Ju, Y., & Meng, D. (2019) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2019.102924 · Cited by 46 · see citing works
Thermosensing to Adjust Bacterial Virulence in a Fluctuating Environment
Steinmann, R., & Dersch, P. (2012) · Future Microbiology · doi:10.2217/fmb.12.129 · Cited by 44 · see citing works
Activities of muscadine grape skin and polyphenolic constituents againstHelicobacter pylori
Brown, J., & Jiang, X. (2013) · Journal of Applied Microbiology · doi:10.1111/jam.12129 · Cited by 43 · see citing works
Dalmasso, G., Cougnoux, A., Faïs, T., Bonnin, V., Mottet-Auselo, B., Nguyen, H. T. T., Sauvanet, P., Barnich, N., Jary, M., Pezet, D., et al. (2024) · Gut Microbes · doi:10.1080/19490976.2024.2310215 · Cited by 43 · see citing works
Schott, T., Kondadi, P. K., Hänninen, M., & Rossi, M. (2011) · BMC Genomics · doi:10.1186/1471-2164-12-534 · Cited by 42 · see citing works
- Authors
- Hoy, B., Löwer, M., Weydig, C., Carra, G., Tegtmeyer, N., Geppert, T., Schröder, P., Sewald, N., Backert, S., Schneider, G., & Wessler, S.
- Affiliations
- Paul Ehrlich Institut (DE)
- Goethe University Frankfurt (DE)
- University College Dublin (IE)
- ETH Zurich (CH)
- Bielefeld University (DE)
- Venue
- The EMBO Reports
- Published
- 2010-09-03
- Volume
- 11
- Issue
- 10
- Pages
- 798-804
- ISSN
- 1469-221X (ISSN-L)
- 1469-3178
- PMC
- PMC2948180
- OpenAlex
- W2097301400
- Cited by
- 295
- References
- 23
- Citations by year
- 2026: 9 · 2025: 11 · 2024: 20 · 2023: 19 · 2022: 13 · 2021: 24 · 2020: 19 · 2019: 28 · 2018: 16 · 2017: 18 · 2016: 16 · 2015: 19 · 2014: 20 · 2013: 26 · 2012: 15
- FWCI
- 21.25
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- EMBO Reports (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- PUB – Publications at Bielefeld University (Bielefeld University) (submittedVersion)
- Publikationen an der Universität Bielefeld (Universität Bielefeld) (submittedVersion)
- Topics
- Health Sciences › Medicine › Surgery › Helicobacter pylori-related gastroenterology studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- Helicobacter pylori, HtrA, secreted virulence factors, E-cadherin cleavage, cell-cell adhesion, epithelial barrier function, serine protease, molecular chaperones, small molecule inhibitors, bacterial cell entry
- MeSH terms
- Bacterial Adhesion, Bacterial Outer Membrane Proteins, Epithelial Cells, Humans, Blotting, Western, Cell Adhesion Molecules, Cadherins, Helicobacter pylori, Helicobacter Infections, Virulence Factors, Cell Line, Tumor
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