Degradation of Outer Membrane Protein A in Escherichia coli Killing by Neutrophil Elastase
Abstract
In determining the mechanism of neutrophil elastase (NE)-mediated killing of Escherichia coli, we found that NE degraded outer membrane protein A (OmpA), localized on the surface of Gram-negative bacteria. NE killed wild-type, but not OmpA-deficient, E. coli. Also, whereas NE-deficient mice had impaired survival in response to E. coli sepsis, as compared to wild-type mice, the presence or absence of NE had no influence on survival in response to sepsis that had been induced with OmpA-deficient E. coli. These findings define a mechanism of nonoxidative bacterial killing by NE and point to OmpA as a bacterial target in host defense.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Degradation of E. coli outer membrane protein A (OmpA) by HNE is lethal.
“Examples of HNE pathogen substrates include outer membrane protein A (OmpA) in E. coli, where its degradation is lethal [35]”
From Discrimination of Methionine Sulfoxide and Sulfone by Human Neutrophil Elastase (2021) · cites this paper as [35]
Cites
Mice lacking neutrophil elastase reveal impaired host defense against gram negative bacterial sepsis
Belaaouaj, A., McCarthy, R., Baumann, M. L., Gao, Z., Ley, T. J., Abraham, S. N., & Shapiro, S. D. (1998) · Nature Medicine · doi:10.1038/nm0598-615 · Cited by 691 · see citing works
Self-citationShapiro, S. D., Kobayashi, D. K., & Ley, T. J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80459-1 · Cited by 492 · see citing works
Self-citationPorin channels in Escherichia coli: studies with liposomes reconstituted from purified proteins
Nikaido, H., & Rosenberg, E. Y. (1983) · Journal of Bacteriology · doi:10.1128/jb.153.1.241-252.1983 · Cited by 448 · see citing works
Prasadarao, N. V., Wass, C. A., Weiser, J. N., Stins, M. F., Huang, S. H., & Kim, K. (1996) · Infection and Immunity · doi:10.1128/iai.64.1.146-153.1996 · Cited by 338 · see citing works
Self-citationWeiser, J. N., & Gotschlich, E. C. (1991) · Infection and Immunity · doi:10.1128/iai.59.7.2252-2258.1991 · Cited by 256 · see citing works
Zimmer, M., Medcalf, R. L., Fink, T. M., Mattmann, C., Lichter, P., & Jenne, D. E. (1992) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.89.17.8215 · Cited by 177 · see citing works
Neutrophil Emigration in the Lungs, Peritoneum, and Skin Does Not Require Gelatinase B
Betsuyaku, T., Shipley, J. M., Liu, Z., & Senior, R. M. (1999) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.20.6.3558 · Cited by 129 · see citing works
Normal Neutrophil Function in Cathepsin G-Deficient Mice
MacIvor, D. M., Shapiro, S. D., Pham, C. T. N., Belaaouaj, A., Abraham, S. N., & Ley, T. J. (1999) · Blood · doi:10.1182/blood.v94.12.4282 · Cited by 120 · see citing works
Self-citationSlot, J. W., Geuze, H. J., & Weerkamp, A. J. (1988) · Methods in microbiology · doi:10.1016/s0580-9517(08)70053-9 · Cited by 86 · see citing works
Klose, M., Schwarz, H., MacIntyre, S., Freudl, R., Eschbach, M.-L., & Henning, U. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)37703-2 · Cited by 74 · see citing works
Shafer, W. M., Hubálek, F., Huang, M. R., & Pohl, J. (1996) · Infection and Immunity · doi:10.1128/iai.64.11.4842-4845.1996 · Cited by 55 · see citing works
The Cloning and Characterization of a Murine Secretory Leukocyte Protease Inhibitor cDNA
Zitnik, R. J., Zhang, J., Kashem, M. A., Kohno, T., Lyons, D. E., Wright, C. D., Rosen, E. M., Goldberg, I. D., & Hayday, A. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6358 · Cited by 50 · see citing works
Immunocytochemical Labelling of Bacteroides nodosus Pili Using an Immunogold Technique
Beesley, J. E., Day, S., Betts, M. P., & Thorley, C. M. (1984) · Microbiology · doi:10.1099/00221287-130-6-1481 · Cited by 43 · see citing works
Oxygen‐Independent Microbicidal Mechanisms of Phagocytes
Ganz, T. (1999) · Proceedings of the Association of American Physicians · doi:10.1111/paa.1999.111.5.390 · Cited by 29 · see citing works
Degradation of gonococcal outer membrane proteins by human neutrophil lysosomal proteases
Rest, R. F., & Pretzer, E. (1981) · Infection and Immunity · doi:10.1128/iai.34.1.62-68.1981 · Cited by 22 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Myeloperoxidase: friend and foe
Klebanoff, S. J. (2005) · Journal of Leukocyte Biology · doi:10.1189/jlb.1204697 · Cited by 2,282 · see citing works
Neutrophil elastase and myeloperoxidase regulate the formation of neutrophil extracellular traps
Papayannopoulos, V., Metzler, K. D., Hakkim, A., & Zychlinsky, A. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201006052 · Cited by 2,103 · see citing works
Neutrophil serine proteases: specific regulators of inflammation
Pham, C. T. N. (2006) · Nature reviews. Immunology · doi:10.1038/nri1841 · Cited by 1,017 · see citing works
Neutrophil Elastase, Proteinase 3, and Cathepsin G as Therapeutic Targets in Human Diseases
Korkmaz, B., Horwitz, M. S., Jenne, D. E., & Gauthier, F. (2010) · Pharmacological Reviews · doi:10.1124/pr.110.002733 · Cited by 873 · see citing works
Myeloperoxidase: a front-line defender against phagocytosed microorganisms
Klebanoff, S. J., Kettle, A. J., Rosen, H., Winterbourn, C. C., & Nauseef, W. M. (2012) · Journal of Leukocyte Biology · doi:10.1189/jlb.0712349 · Cited by 679 · see citing works
NETs: a new strategy for using old weapons
Papayannopoulos, V., & Zychlinsky, A. (2009) · Trends in Immunology · doi:10.1016/j.it.2009.07.011 · Cited by 634 · see citing works
Severity of E. coli mastitis is mainly determined by cow factors
Burvenich, C., Merris, V. V., Mehrzad, J., Diez‐Fraile, A., & Duchateau, L. (2003) · Veterinary Research · doi:10.1051/vetres:2003023 · Cited by 598 · see citing works
Cabeen, M. T., & Jacobs, C. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1205 · Cited by 495 · see citing works
Gasdermin D Exerts Anti-inflammatory Effects by Promoting Neutrophil Death
Kambara, H., Liu, F., Zhang, X., Liu, P., Bajrami, B., Teng, Y., Zhao, L., Zhou, S., Yu, H., Zhou, W., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.02.067 · Cited by 418 · see citing works
Antimicrobial Peptides: Old Molecules with New Ideas
Nakatsuji, T., & Gallo, R. L. (2011) · Journal of Investigative Dermatology · doi:10.1038/jid.2011.387 · Cited by 397 · see citing works
A molecular Swiss army knife: OmpA structure, function and expression
Smith, S. G. J., Mahon, V., Lambert, M. A., & Fagan, R. P. (2007) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2007.00778.x · Cited by 392 · see citing works
Structure of outer membrane protein A transmembrane domain by NMR spectroscopy.
Arora, A., Abildgaard, F., Bushweller, J. H., & Tamm, L. K. (2001) · Nature Structural Biology · doi:10.1038/86214 · Cited by 389 · see citing works
Kessenbrock, K., Fröhlich, L. F., Sixt, M., Lämmermann, T., Pfister, H., Bateman, A., Belaaouaj, A., Ring, J., Ollert, M. W., Fässler, R., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci34694 · Cited by 363 · see citing works
Self-citationThe OmpA family of proteins: Roles in bacterial pathogenesis and immunity
Confer, A. W., & Ayalew, S. (2012) · Veterinary Microbiology · doi:10.1016/j.vetmic.2012.08.019 · Cited by 357 · see citing works
Yu, S., Li, G., Liu, R., Ma, D., & Xue, W. (2018) · Advanced Functional Materials · doi:10.1002/adfm.201707440 · Cited by 336 · see citing works
Neutrophil elastase targets virulence factors of enterobacteria
Weinrauch, Y., Drujan, D., Shapiro, S. D., Weiss, J. P., & Zychlinsky, A. (2002) · Nature · doi:10.1038/417091a · Cited by 334 · see citing works
Self-citationLee, W. L., & Downey, G. P. (2001) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm.164.5.2103040 · Cited by 325 · see citing works
Waki, H., Yamauchi, T., Kamon, J., Kita, S., Ito, Y., Hada, Y., Uchida, S., Tsuchida, A., Takekawa, S., & Kadowaki, T. (2005) · Endocrinology · doi:10.1210/en.2004-1096 · Cited by 319 · see citing works
The neutrophil: function and regulation in innate and humoral immunity.
Burg, N. D., & Pillinger, M. (2001) · Clinical Immunology · doi:10.1006/clim.2001.5007 · Cited by 286 · see citing works
Burgener, S. S., Leborgne, N. G. F., Snipas, S. J., Salvesen, G. S., Bird, P. I., & Benarafa, C. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.05.065 · Cited by 276 · see citing works
Neutrophils and Bacterial Immune Evasion
Kobayashi, S. D., Małachowa, N., & DeLeo, F. R. (2018) · Journal of Innate Immunity · doi:10.1159/000487756 · Cited by 255 · see citing works
Neutrophil serine proteases fine-tune the inflammatory response
Pham, C. T. N. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.11.008 · Cited by 252 · see citing works
Neutrophil elastase in cyclic and severe congenital neutropenia
Horwitz, M. S., Duan, Z., Korkmaz, B., Lee, H.-H., Mealiffe, M. E., & Salipante, S. J. (2006) · Blood · doi:10.1182/blood-2006-08-019166 · Cited by 246 · see citing works
The Function of OmpA in Escherichia coli
Wang, Y. (2002) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2002.6657 · Cited by 241 · see citing works
Rosenberger, C. M., Gallo, R. L., & Finlay, B. B. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0304455101 · Cited by 240 · see citing works
Neutrophil Elastase and Chronic Lung Disease
Voynow, J. A., & Shinbashi, M. Y. (2021) · Biomolecules · doi:10.3390/biom11081065 · Cited by 236 · see citing works
Modulating the outer membrane with small RNAsPreprint
Guillier, M., Gottesman, S., & Storz, G. (2006) · Genes & Development · doi:10.1101/gad.1457506 · Cited by 225 · see citing works
Rickettsia Phylogenomics: Unwinding the Intricacies of Obligate Intracellular Life
Gillespie, J. J., Williams, K. P., Shukla, M. P., Snyder, E. E., Nordberg, E. K., Ceraul, S. M., Dharmanolla, C., Rainey, D. Y., Soneja, J., Shallom, J. M., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002018 · Cited by 221 · see citing works
Neutrophil elastase promotes myofibroblast differentiation in lung fibrosis
Gregory, A. D., Kliment, C. R., Metz, H. E., Kim, K.-H., Kargl, J., Agostini, B. A., Crum, L. T., Oczypok, E. A., Oury, T. A., & Houghton, A. M. (2015) · Journal of Leukocyte Biology · doi:10.1189/jlb.3hi1014-493r · Cited by 216 · see citing works
Self-citationNeutrophil Extracellular Traps in Host DefensePreprint
Burgener, S. S., & Schroder, K. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a037028 · Cited by 193 · see citing works
Antimicrobial proteins and peptides: anti-infective molecules of mammalian leukocytes
Levy, O. (2004) · Journal of Leukocyte Biology · doi:10.1189/jlb.0604320 · Cited by 190 · see citing works
Lévesque, J.-P., Hendy, J., Winkler, I. G., Takamatsu, Y., & Simmons, P. J. (2003) · Experimental Hematology · doi:10.1016/s0301-472x(02)01028-7 · Cited by 187 · see citing works
Clancy, D. M., Sullivan, G. P., Moran, H. B. T., Henry, C. M., Reeves, E. P., McElvaney, N. G., Lavelle, E. C., & Martin, S. J. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.02.062 · Cited by 186 · see citing works
Wang, L., Huo, M., Chen, Y., & Shi, J. (2018) · Biomaterials · doi:10.1016/j.biomaterials.2018.02.018 · Cited by 182 · see citing works
Macrophage elastase kills bacteria within murine macrophages
Houghton, A. M., Hartzell, W. O., Robbins, C. S., Gomis‐Rüth, F. X., & Shapiro, S. D. (2009) · Nature · doi:10.1038/nature08181 · Cited by 180 · see citing works
Self-citationHuman Neutrophils Kill Streptococcus pneumoniae via Serine Proteases
Standish, A. J., & Weiser, J. N. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0900688 · Cited by 174 · see citing works
Roos, D., & Winterbourn, C. C. (2002) · Science · doi:10.1126/science.1071271 · Cited by 170 · see citing works
Young, K. D. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03607.x · Cited by 162 · see citing works
Neutrophil Extracellular Traps in Sepsis
Camicia, G., Pozner, R. G., & Larrañaga, G. F. D. (2014) · Shock · doi:10.1097/shk.0000000000000221 · Cited by 160 · see citing works
The emerging problems ofKlebsiella pneumoniaeinfections: carbapenem resistance and biofilm formation
Chung, P. Y. (2016) · FEMS Microbiology Letters · doi:10.1093/femsle/fnw219 · Cited by 156 · see citing works
Sutherland, R. E., Olsen, J. S., McKinstry, A., Villalta, S. A., & Wolters, P. J. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.181.8.5598 · Cited by 155 · see citing works
Park, C., Clark, S. G., Lichtensteiger, C. A., Jamison, R. D., & Johnson, A. J. W. (2009) · Acta Biomaterialia · doi:10.1016/j.actbio.2009.03.002 · Cited by 154 · see citing works
Serum Amyloid A Protein Binds to Outer Membrane Protein A of Gram-negative Bacteria
Hari-Dass, R., Shah, C., Meyer, D. J., & Raynes, J. G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500490200 · Cited by 152 · see citing works
Reta, N., Saint, C. P., Michelmore, A., Prieto‐Simón, B., & Voelcker, N. H. (2018) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.7b13943 · Cited by 150 · see citing works
Mast cell dipeptidyl peptidase I mediates survival from sepsis
Clair, J. M., Pham, C. T. N., Villalta, S. A., Caughey, G. H., & Wolters, P. J. (2004) · Journal of Clinical Investigation · doi:10.1172/jci19062 · Cited by 150 · see citing works
Cole, A. M., Shi, J., Ceccarelli, A., Kim, Y.-H., Park, A., & Ganz, T. (2001) · Blood · doi:10.1182/blood.v97.1.297 · Cited by 146 · see citing works
With Friends Like These: The Complex Role of Neutrophils in the Progression of Severe Pneumonia
Pechous, R. D. (2017) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2017.00160 · Cited by 145 · see citing works
Oral pathogenesis of Aggregatibacter actinomycetemcomitans
Gholizadeh, P., Pormohammad, A., Eslami, H., Shokouhi, B., Fakhrzadeh, V., & Kafil, H. S. (2017) · Microbial Pathogenesis · doi:10.1016/j.micpath.2017.11.001 · Cited by 144 · see citing works
Therapeutic targeting of cathepsin C: from pathophysiology to treatment
Korkmaz, B., Caughey, G. H., Chapple, I., Gauthier, F., Hirschfeld, J., Jenne, D. E., Kettritz, R., Lalmanach, G., Lamort, A., Lauritzen, C., et al. (2018) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2018.05.011 · Cited by 141 · see citing works
Staphylococcus aureus secretes a unique class of neutrophil serine protease inhibitors
Stapels, D. A. C., Ramyar, K. X., Bischoff, M., von Köckritz‐Blickwede, M., Milder, F. J., Ruyken, M., Eisenbeis, J., McWhorter, W. J., Herrmann, M., van Kessel, K. P. M., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1407616111 · Cited by 140 · see citing works
Helmig, B. R., Romero, R. J., Espinoza, J., Chaiworapongsa, T., Bujold, E., Gómez, R., OHLSSON, K., & Uldbjerg, N. (2002) · The Journal of Maternal-Fetal & Neonatal Medicine · doi:10.1080/jmf.12.4.237.246 · Cited by 138 · see citing works
Schreiber, A., Pham, C. T. N., Hu, Y., Schneider, W., Luft, F. C., & Kettritz, R. (2012) · Journal of the American Society of Nephrology · doi:10.1681/asn.2010080892 · Cited by 135 · see citing works
Zeiher, B. G., Matsuoka, S., Kawabata, K., & Repine, J. E. (2002) · Critical Care Medicine · doi:10.1097/00003246-200205001-00018 · Cited by 132 · see citing works
Morphology engineering of bacteria for bio-production
Jiang, X., & Chen, G. (2015) · Biotechnology Advances · doi:10.1016/j.biotechadv.2015.12.007 · Cited by 131 · see citing works
Neutrophil serine proteases: mediators of innate immune responses
Meyer‐Hoffert, U., & Wiedow, O. (2010) · Current Opinion in Hematology · doi:10.1097/moh.0b013e32834115d1 · Cited by 128 · see citing works
Hirche, T. O., Gaut, J. P., Heinecke, J. W., & Belaaouaj, A. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.3.1557 · Cited by 124 · see citing works
Self-citationLane, A. A., & Ley, T. J. (2003) · Cell · doi:10.1016/s0092-8674(03)00852-3 · Cited by 124 · see citing works
Antimicrobial peptides and proteins in mycobacterial therapy: Current status and future prospects
Padhi, A., Sengupta, M., Sengupta, S., Roehm, K. H., & Sonawane, A. (2014) · Tuberculosis · doi:10.1016/j.tube.2014.03.011 · Cited by 123 · see citing works
ELANE Mutations in Cyclic and Severe Congenital Neutropenia
Horwitz, M. S., Corey, S. J., Grimes, H. L., & Tidwell, T. J. (2012) · Hematology/Oncology Clinics of North America · doi:10.1016/j.hoc.2012.10.004 · Cited by 122 · see citing works
Neutrophil serine proteases in antibacterial defense
Stapels, D. A. C., Geisbrecht, B. V., & Rooijakkers, S. H. M. (2014) · Current Opinion in Microbiology · doi:10.1016/j.mib.2014.11.002 · Cited by 121 · see citing works
Progesterone Receptor Serves the Ovary as a Trigger of Ovulation and a Terminator of Inflammation
Park, C. J., Lin, P.-C. P., Zhou, S. Q., Barakat, R., Bashir, S. T., Choi, J. M., Cacioppo, J. A., Oakley, O. R., Duffy, D. M., Lydon, J. P., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.03.060 · Cited by 121 · see citing works
Mydel, P. M., Takahashi, Y., Yumoto, H., Sztukowska, M. N., Kubica, M., Gibson, F. C., Kurtz, D. M. J., Travis, J., Collins, L. V., Nguyen, K.-A. T., et al. (2006) · PLoS Pathogens · doi:10.1371/journal.ppat.0020076 · Cited by 119 · see citing works
NETosis and NADPH oxidase: at the intersection of host defense, inflammation, and injury
Almyroudis, N. G., Grimm, M. J., Davidson, B. A., Röhm, M., Urban, C. F., & Segal, B. H. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2013.00045 · Cited by 119 · see citing works
Current concepts on K1 translocation of the blood–brain barrier
XIE, Y., KIM, K., & KIM, K. (2004) · FEMS Immunology & Medical Microbiology · doi:10.1016/j.femsim.2004.09.001 · Cited by 117 · see citing works
Self-citationAcinetobacter lwoffii infection and gastritis
Rathinavelu, S., Zavros, Y. L., & Merchant, J. L. (2003) · Microbes and Infection · doi:10.1016/s1286-4579(03)00099-6 · Cited by 115 · see citing works
Benarafa, C., Priebe, G. P., & Remold‐O’Donnell, E. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20070494 · Cited by 114 · see citing works
Amézaga-Madrid, P., Silveyra-Morales, R., CORDOBAFIERRO, L., Nevárez‐Moorillón, G. V., Miki-Yoshida, M., Orrantia‐Borunda, E., & Solı&#x;s, F. J. (2003) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/s1011-1344(03)00054-x · Cited by 113 · see citing works
Quintero, P. A., Knolle, M. D., Cala, L. F., Zhuang, Y., & Owen, C. A. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0900290 · Cited by 110 · see citing works
Importance of lysosomal cysteine proteases in lung disease
Wolters, P. J., & Chapman, H. A. (2000) · Respiratory Research · doi:10.1186/rr29 · Cited by 110 · see citing works
Viability of Milk Neutrophils and Severity of Bovine Coliform Mastitis
Mehrzad, J., Duchateau, L., & Burvenich, C. (2004) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(04)73558-4 · Cited by 109 · see citing works
Host-Defense Mechanism of the Ocular Surfaces
Sack, R. A., Nunes, I., Beaton, A. R., & Morris, C. (2001) · Bioscience Reports · doi:10.1023/a:1017943826684 · Cited by 105 · see citing works
Shapiro, S. D. (2002) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.26.3.f233 · Cited by 105 · see citing works
Self-citationKhatua, B., Bhattacharya, K., & Mandal, C. (2012) · Journal of Leukocyte Biology · doi:10.1189/jlb.0511260 · Cited by 104 · see citing works
Sukumaran, S. K., Shimada, H., & Prasadarao, N. V. (2003) · Infection and Immunity · doi:10.1128/iai.71.10.5951-5961.2003 · Cited by 102 · see citing works
Kasperkiewicz, P., Altman, Y., D’Angelo, M. A., Salvesen, G. S., & Drąg, M. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b04394 · Cited by 101 · see citing works
Hahn, I., Klaus, A., Janze, A.-K., Steinwede, K., Ding, N., Bohling, J., Brumshagen, C., Serrano, H., Gauthier, F., Paton, J. C., et al. (2011) · Infection and Immunity · doi:10.1128/iai.05593-11 · Cited by 101 · see citing works
Hirche, T. O., Crouch, E. C., Espinola, M., Brokelman, T. J., Mecham, R. P., DeSilva, N., Cooley, J., Remold‐O’Donnell, E., & Belaaouaj, A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402936200 · Cited by 100 · see citing works
Self-citationFlavonoids as inhibitors of human neutrophil elastase
Jakimiuk, K., Gesek, J., Atanasov, A. G., & Tomczyk, M. (2021) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2021.1927006 · Cited by 99 · see citing works
Neutrophil Elastase Mediates Innate Host Protection against Pseudomonas aeruginosa
Hirche, T. O., Benabid, R., Deslée, G., Gangloff, S. C., Achilefu, S. A., Guenounou, M., Lebargy, F., Hancock, R. E. W., & Belaaouaj, A. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.181.7.4945 · Cited by 99 · see citing works
Self-citationKlebsiella pneumoniae OmpA Confers Resistance to Antimicrobial Peptides
Llobet, E., March, C., Giménez, P., & Bengoechea, J. A. (2008) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00657-08 · Cited by 98 · see citing works
Neutrophil elastase-mediated killing of bacteria: lessons from targeted mutagenesis
Belaaouaj, A. (2002) · Microbes and Infection · doi:10.1016/s1286-4579(02)01654-4 · Cited by 98 · see citing works
Self-citationCharacterization of Mutant Neutrophil Elastase in Severe Congenital Neutropenia
Li, F., & Horwitz, M. S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010279200 · Cited by 97 · see citing works
Campbell, E. J., & Owen, C. A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608346200 · Cited by 96 · see citing works
Cystic Fibrosis: Pathophysiology of Lung Disease
Bergeron, C., & Cantin, A. M. (2019) · Seminars in Respiratory and Critical Care Medicine · doi:10.1055/s-0039-1694021 · Cited by 94 · see citing works
Proteinases and oxidants as targets in the treatment of chronic obstructive pulmonary disease.
Owen, C. (2005) · Proceedings of the American Thoracic Society · doi:10.1513/pats.200504-029sr · Cited by 96 · see citing works
High-dose parenteral iron sucrose depresses neutrophil intracellular killing capacity
Deicher, R., Ziai, F., Cohen, G., Müllner, M., & Hörl, W. H. (2003) · Kidney International · doi:10.1046/j.1523-1755.2003.00125.x · Cited by 92 · see citing works
Lung injury following acute kidney injury: kidney–lung crosstalk
Doi, K., Ishizu, T., Fujita, T., & Noiri, E. (2011) · Clinical and Experimental Nephrology · doi:10.1007/s10157-011-0459-4 · Cited by 92 · see citing works
López-Boado, Y. S., Espinola, M., Bahr, S., & Belaaouaj, A. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.1.509 · Cited by 92 · see citing works
Self-citationThe periplasmic serine protease inhibitor ecotin protects bacteria against neutrophil elastase
Eggers, C. T., Murray, I. A., Delmar, V. A., Day, A. G., & Craik, C. S. (2004) · Biochemical Journal · doi:10.1042/bj20031790 · Cited by 91 · see citing works
March, C., Moranta, D., Regueiro, V., Llobet, E., Tomás, A., Garmendia, J., & Bengoechea, J. A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.181008 · Cited by 90 · see citing works
The Role of Neutrophils and Neutrophil Elastase in Pulmonary Arterial Hypertension
Taylor, S., Dirir, O., Zamanian, R. T., Rabinovitch, M., & Thompson, A. A. R. (2018) · Frontiers in Medicine · doi:10.3389/fmed.2018.00217 · Cited by 89 · see citing works
The Regulation and Modification of GSDMD Signaling in Diseases
Li, Z., Ji, S., Jiang, M., Xu, Y., & Zhang, C. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.893912 · Cited by 89 · see citing works
Park, J., Kim, J., Singha, K., Han, D. K., Park, H., & Kim, W. J. (2013) · Biomaterials · doi:10.1016/j.biomaterials.2013.07.064 · Cited by 89 · see citing works
Hemmat, N., Derakhshani, A., Baghi, H. B., Silvestris, N., Baradaran, B., & Summa, S. D. (2020) · Frontiers in Genetics · doi:10.3389/fgene.2020.00641 · Cited by 87 · see citing works
Shapiro, S. D. (2003) · European Respiratory Journal · doi:10.1183/09031936.03.00000903a · Cited by 86 · see citing works
Self-citationAdiponectin inhibits induction of TNF‐α/RANKL‐stimulated NFATc1 via the AMPK signaling
Yamaguchi, N., Kukita, T., Li, Y.-J., Kamio, N., Fukumoto, S., Nonaka, K., Ninomiya, Y., Hanazawa, S., & Yamashita, Y. (2008) · FEBS Letters · doi:10.1016/j.febslet.2007.12.037 · Cited by 83 · see citing works
Identification and agglutination properties of hemocyanin from the mud crab (Scylla serrata)
Fang, Y., Zhang, Y., Jiang, R., Zhong, M., Hu, Z., Du, H., Lun, J., Chen, J., & Li, Y. (2010) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2010.11.004 · Cited by 83 · see citing works
Neutrophil elastase cleaves epithelial cadherin in acutely injured lung epithelium
Boxio, R., Wartelle, J., Nawrocki‐Raby, B., Lagrange, B., Malleret, L., Hirche, T., Taggart, C. C., Pachéco, Y., Devouassoux, G., & Bentaher, A. (2016) · Respiratory Research · doi:10.1186/s12931-016-0449-x · Cited by 82 · see citing works
Neutrophil Elastase Contributes to Acute Lung Injury Induced by Bilateral Nephrectomy
Ishii, T., Doi, K., Okamoto, K., Imamura, M., Dohi, M., Yamamoto, K., Fujita, T., & Noiri, E. (2010) · American Journal Of Pathology · doi:10.2353/ajpath.2010.090793 · Cited by 81 · see citing works
An engineered innate immune defense protects grapevines from Pierce disease
Dandekar, A. M., Gouran, H., Ibáñez, A., Uratsu, S. L., Agüero, C. B., McFarland, S., Borhani, Y., Feldstein, P. A., Bruening, G. E., Nascimento, R., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1116027109 · Cited by 80 · see citing works
- Authors
- Belaaouaj, A. A., Kim, K. S., & Shapiro, S. D.
- Affiliations
- Washington University in St. Louis (US)
- Children's Hospital Los Angeles (US)
- Corresponding author
- Belaaouaj, Abderr azzaq
- Venue
- Science
- Published
- 2000-08-18
- Volume
- 289
- Issue
- 5482
- Pages
- 1185-1187
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2027297714
- Cited by
- 363
- References
- 15
- Citations by year
- 2026: 7 · 2025: 10 · 2024: 9 · 2023: 10 · 2022: 11 · 2021: 15 · 2020: 15 · 2019: 20 · 2018: 24 · 2017: 12 · 2016: 13 · 2015: 16 · 2014: 15 · 2013: 17 · 2012: 15
- FWCI
- 4.95
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Keywords
- neutrophil elastase, OmpA, Escherichia coli, neutrophil killing, Gram-negative bacteria, sepsis, host defense, bacterial surface proteins
- MeSH terms
- Animals, Bacterial Outer Membrane Proteins, Blood Bactericidal Activity, Cell Membrane, Escherichia coli, Escherichia coli Infections, Humans, Microscopy, Electron, Mutation, Neutrophils, Phagosomes, Proteins, Colony Count, Microbial, Serine Proteinase Inhibitors, Leukocyte Elastase, Mice, Proteinase Inhibitory Proteins, Secretory
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review