Pseudomonas aeruginosa pili and flagella mediate distinct binding and signaling events at the apical and basolateral surface of airway epithelium.
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Pseudomonas aeruginosa, an important opportunistic pathogen of man, exploits numerous factors for initial attachment to the host, an event required to establish bacterial infection. In this paper, we rigorously explore the role of two major bacterial adhesins, type IV pili (Tfp) and flagella, in bacterial adherence to distinct host receptors at the apical (AP) and basolateral (BL) surfaces of polarized lung epithelial cells and induction of subsequent host signaling and pathogenic events. Using an isogenic mutant of P. aeruginosa that lacks flagella or utilizing beads coated with purified Tfp, we establish that Tfp are necessary and sufficient for maximal binding to host N-glycans at the AP surface of polarized epithelium. In contrast, experiments utilizing a P. aeruginosa isogenic mutant that lacks Tfp or using beads coated with purified flagella demonstrate that flagella are necessary and sufficient for maximal binding to heparan sulfate (HS) chains of heparan sulfate proteoglycans (HSPGs) at the BL surface of polarized epithelium. Using two different cell-free systems, we demonstrate that Tfp-coated beads show highest binding affinity to complex N-glycan chains coated onto plastic plates and preferentially aggregate with beads coated with N-glycans, but not with single sugars or HS. In contrast, flagella-coated beads bind to or aggregate preferentially with HS or HSPGs, but demonstrate little binding to N-glycans. We further show that Tfp-mediated binding to host N-glycans results in activation of phosphatidylinositol 3-kinase (PI3K)/Akt pathway and bacterial entry at the AP surface. At the BL surface, flagella-mediated binding to HS activates the epidermal growth factor receptor (EGFR), adaptor protein Shc, and PI3K/Akt, and induces bacterial entry. Remarkably, flagella-coated beads alone can activate EGFR and Shc. Together, this work provides new insights into the intricate interactions between P. aeruginosa and lung epithelium that may be potentially useful in the development of novel treatments for P. aeruginosa infections.
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Exposure of apical receptors like integrins permits adhesion of bacteria such as S. aureus and P. aeruginosa.
“For example the exposure of apical receptors like integrins permit the adhesion of bacteria such as S. aureus and P. aeruginosa (Sanford et al., 1978; Davison and Sanford, 1981; Bucior et al., 2012; Smith and McCullers, 2014).”
From Secondary bacterial infections associated with influenza pandemics (2017) · cites this paper as Bucior et al., 2012
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Cites
Principles and Practice of Infectious Diseases.
(1991) · Annals of Internal Medicine · doi:10.7326/0003-4819-114-9-818_5 · Cited by 12,045 · see citing works
Mandell, Douglas, and Bennett's Principles and Practice of Infectious Diseases
Castagnola, E., Viscoli, C., & Mikulska, M. (2015) · Elsevier eBooks · doi:10.1016/c2012-1-00075-6 · Cited by 2,587 · see citing works
Genetic adaptation by <i>Pseudomonas aeruginosa</i> to the airways of cystic fibrosis patients
Smith, E. E., Buckley, D. G., Wu, Z., Saenphimmachak, C., Hoffman, L. R., D’Argenio, D. A., Miller, S. I., Ramsey, B. W., Speert, D. P., Moskowitz, S. M., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602138103 · Cited by 1,319 · see citing works
Type IV Pili and Twitching Motility
Mattick, J. S. (2002) · Annual Review of Microbiology · doi:10.1146/annurev.micro.56.012302.160938 · Cited by 1,257 · see citing works
Innate immune recognition of bacterial ligands by NAIPs determines inflammasome specificity
Kofoed, E. M., & Vance, R. E. (2011) · Nature · doi:10.1038/nature10394 · Cited by 894 · see citing works
Role of Flagella in Pathogenesis ofPseudomonas aeruginosaPulmonary Infection
Feldman, M. F., Bryan, R. A., Rajan, S., Scheffler, L., Brunnert, S. R., Tang, H. B., & Prince, A. S. (1998) · Infection and Immunity · doi:10.1128/iai.66.1.43-51.1998 · Cited by 489 · see citing works
Lightfield, K. L., Persson, J., Brubaker, S. W., Witte, C. E., von Moltke, J., Dunipace, E. A., Henry, T., Sun, Y., Cado, D., Dietrich, W. F., et al. (2008) · Nature Immunology · doi:10.1038/ni.1646 · Cited by 487 · see citing works
Dasgupta, N., Wolfgang, M. C., Goodman, A. L., Arora, S. K., Jyot, J., Lory, S. J., & Ramphal, R. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03740.x · Cited by 451 · see citing works
Vallet-Gély, I., Olson, J. W., Lory, S. J., Lazdunski, A. M., & Filloux, A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.111551898 · Cited by 355 · see citing works
Saiman, L. M., & Prince, A. S. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116779 · Cited by 347 · see citing works
Involvement of Toll-like receptor 5 in the recognition of flagellated bacteria
Feuillet, V., Medjane, S., Mondor, I., Demaria, O., Pagni, P. P., Galán, J. E., Flavell, R. A., & Alexopoulou, L. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605200103 · Cited by 337 · see citing works
Role of Pseudomonas aeruginosa type III effectors in disease
Engel, J. N., & Balachandran, P. (2009) · Current Opinion in Microbiology · doi:10.1016/j.mib.2008.12.007 · Cited by 330 · see citing works
Chemani, C., Imberty, A., de Bentzmann, S., Pierre, M., Wimmerová, M., Guery, B. P., & Faure, K. (2009) · Infection and Immunity · doi:10.1128/iai.01204-08 · Cited by 329 · see citing works
Toll-Like Receptors in Normal and Cystic Fibrosis Airway Epithelial Cells
Muir, A. B., Soong, G., Sokol, S., Reddy, B. D., Gómez, M. I., van Heeckeren, A. M., & Prince, A. S. (2003) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2003-0329oc · Cited by 259 · see citing works
Liu, P. V. (1966) · The Journal of Infectious Diseases · doi:10.1093/infdis/116.4.481 · Cited by 226 · see citing works
Koff, J. L., Shao, M. X. G., Ueki, I. F., & Nadel, J. A. (2008) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00025.2008 · Cited by 226 · see citing works
Type IV pili of pathogenic Neisseriae elicit cortical plaque formation in epithelial cells
Merz, A. J., Enns, C. A., & So, M. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01459.x · Cited by 210 · see citing works
Keates, S. E., Sougioultzis, S., Keates, A. C., Zhao, D., Peek, R. M., Shaw, L. M., & Kelly, C. P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m107630200 · Cited by 194 · see citing works
Interaction of Pseudomonas aeruginosa with A549 pneumocyte cells
Chi, E. Y., Mehl, T., Nunn, D., & Lory, S. J. (1991) · Infection and Immunity · doi:10.1128/iai.59.3.822-828.1991 · Cited by 179 · see citing works
Epithelial cell polarity affects susceptibility to Pseudomonas aeruginosa invasion and cytotoxicity
Fleiszig, S. M. J., Evans, D. J., Do, N., Vallas, V., Shin, S., & Mostov, K. E. (1997) · Infection and Immunity · doi:10.1128/iai.65.7.2861-2867.1997 · Cited by 168 · see citing works
Bertrand, J. J., West, J. T., & Engel, J. N. (2009) · Journal of Bacteriology · doi:10.1128/jb.01390-09 · Cited by 148 · see citing works
A genomic island in Pseudomonas aeruginosa carries the determinants of flagellin glycosylation
Arora, S. K., Bangera, M. G., Lory, S. J., & Ramphal, R. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.161249198 · Cited by 148 · see citing works
Bucior, I., Simon Scheuring, A., Engel, A. H., & Burger, M. M. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200309005 · Cited by 146 · see citing works
Pier, G. B. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.16.8822 · Cited by 145 · see citing works
Comolli, J. C., Waite, L. L., Mostov, K. E., & Engel, J. N. (1999) · Infection and Immunity · doi:10.1128/iai.67.7.3207-3214.1999 · Cited by 134 · see citing works
Kierbel, A., Gassama‐Diagne, A., Mostov, K. E., & Engel, J. N. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-08-0717 · Cited by 131 · see citing works
Gotoh, N., Tojo, A., Muroya, K., Hashimoto, Y., Hattori, S., Nakamura, S., Takenawa, T., Yazaki, Y., & Shibuya, M. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.1.167 · Cited by 123 · see citing works
Identification of Pseudomonas aeruginosa genes required for epithelial cell injury
Kang, P. J., Hauser, A. R., Apodaca, G., Fleiszig, S. M. J., Wiener-Kronish, J. P., Mostov, K. E., & Engel, J. N. (1997) · Molecular Microbiology · doi:10.1046/j.1365-2958.1997.4311793.x · Cited by 121 · see citing works
Nagy, T. A., Frey, M. R., Yan, F., Israel, D. A., Polk, D. B., & Peek, R. M. (2009) · The Journal of Infectious Diseases · doi:10.1086/596660 · Cited by 120 · see citing works
Yan, F., Cao, H., Chaturvedi, R., Krishna, U. S., Hobbs, S. S., Dempsey, P. J., Peek, R. M., Cover, T. L., Washington, M. K., Wilson, K. T., et al. (2009) · Gastroenterology · doi:10.1053/j.gastro.2008.12.059 · Cited by 111 · see citing works
Koff, J. L., Shao, M. X. G., Kim, S., Ueki, I. F., & Nadel, J. A. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.12.8693 · Cited by 111 · see citing works
Evans, D. J., Frank, D. W., Finck‐Barbançon, V., Wu, C. C., & Fleiszig, S. M. J. (1998) · Infection and Immunity · doi:10.1128/iai.66.4.1453-1459.1998 · Cited by 103 · see citing works
Scharfman, A., Arora, S. K., Delmotte, P. F., Brussel, E. V., Mazurier, J., Ramphal, R., & Roussel, P. (2001) · Infection and Immunity · doi:10.1128/iai.69.9.5243-5248.2001 · Cited by 101 · see citing works
Almagro, P., Salvadó, M., García‐Vidal, C., Rodríguez‐Carballeira, M., Cuchí, E., de-Torres, J. P., & Heredia, J. L. (2011) · Respiration · doi:10.1159/000331224 · Cited by 94 · see citing works
Roger, P., Puchelle, É., Bajolet-Laudinat, O., Tournier, J.-M., Debordeaux, C., Plotkowski, M.-C., Cohen, J. H. M., Sheppard, D., & de Bentzmann, S. (1999) · European Respiratory Journal · doi:10.1034/j.1399-3003.1999.13f14.x · Cited by 92 · see citing works
Seo, B., Choy, E. W., Maudsley, S. R., Miller, W. E., Wilson, B. A., & Luttrell, L. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.3.2239 · Cited by 87 · see citing works
Li, H., Schmid‐Bindert, G., Wang, D., Zhao, Y. F., Yang, X., Su, B., & Zhou, C. (2011) · Advances in Medical Sciences · doi:10.2478/v10039-011-0043-x · Cited by 85 · see citing works
The Role of Flagellin versus Motility in Acute Lung Disease Caused byPseudomonas aeruginosa
Balloy, V., Verma, A., Kuravi, S., Si‐Tahar, M., Chignard, M., & Ramphal, R. (2007) · The Journal of Infectious Diseases · doi:10.1086/518610 · Cited by 84 · see citing works
Esen, M., Grassmé, H., Riethmüller, J., Riehle, A., Fassbender, K. C., & Gulbins, E. (2001) · Infection and Immunity · doi:10.1128/iai.69.1.281-287.2001 · Cited by 81 · see citing works
Hybiske, K., Ichikawa, J. K., Huang, V., Lory, S. J., & Machen, T. E. (2003) · Cellular Microbiology · doi:10.1046/j.1462-5822.2003.00342.x · Cited by 79 · see citing works
Pielage, J. F., Powell, K. R., Kalman, D., & Engel, J. N. (2008) · PLoS Pathogens · doi:10.1371/journal.ppat.1000031 · Cited by 76 · see citing works
Bucior, I., Mostov, K. E., & Engel, J. N. (2009) · Infection and Immunity · doi:10.1128/iai.01215-09 · Cited by 75 · see citing works
Franzetti, F., Grassini, A., Piazza, M., Degl’Innocenti, M., Bandera, A., Gazzola, L., Marchetti, G. C., & Gori, A. (2006) · Infection · doi:10.1007/s15010-006-5007-x · Cited by 65 · see citing works
Rush, J. S., Panneerselvam, K., Waechter, C. J., & Freeze, H. H. (2000) · Glycobiology · doi:10.1093/glycob/10.8.829 · Cited by 63 · see citing works
Molecular Pathogenesis of Acute Pseudomonas Aeruginosa Infections
Engel, J. N. (2003) · Perspectives on critical care infectious diseases · doi:10.1007/978-1-4615-0433-7_13 · Cited by 60 · see citing works
Wong, W. Y., McInnes, C., Sykes, B. D., PARANCHYCH, W., Irvin, R. T., & Hodges, R. S. (1995) · Biochemistry · doi:10.1021/bi00040a006 · Cited by 56 · see citing works
Mikami, F., He, G., Jono, H., Andalibi, A., Kai, H., & Li, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503941200 · Cited by 56 · see citing works
Lack of Adherence of Clinical Isolates of Pseudomonas aeruginosa to Asialo-GM 1 on Epithelial Cells
Schroeder, T. H., Zaidi, T., & Pier, G. B. (2001) · Infection and Immunity · doi:10.1128/iai.69.2.719-729.2001 · Cited by 56 · see citing works
Tseng, J., Jiun, L., Widdicombe, J. H., & Machen, T. E. (2005) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00166.2005 · Cited by 55 · see citing works
Toll-like receptor 5 forms asymmetric dimers in the absence of flagellin
Zhou, K., Kanai, R., Lee, P., Wang, H., & Modis, Y. (2011) · Journal of Structural Biology · doi:10.1016/j.jsb.2011.12.002 · Cited by 54 · see citing works
Zhang, J., Li, H., Wang, J., Dong, Z., Mian, S. I., & Yu, F. X. (2004) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.03-1323 · Cited by 54 · see citing works
Tramper‐Stranders, G. A., van der Ent, C. K., Molin, S., Yang, L., Hansen, S. K., Rau, M. H., Ciofu, O., Johansen, H. K., & Wolfs, T. F. W. (2011) · Clinical Microbiology and Infection · doi:10.1111/j.1469-0691.2011.03627.x · Cited by 47 · see citing works
Epithelial Cell Polarity Alters Rho-GTPase Responses toPseudomonas aeruginosa
Kazmierczak, B. I., Mostov, K. E., & Engel, J. N. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-08-0559 · Cited by 45 · see citing works
Lepanto, P., Bryant, D. M., Rossello, J., Datta, A., Mostov, K. E., & Kierbel, A. (2011) · Cellular Microbiology · doi:10.1111/j.1462-5822.2011.01611.x · Cited by 42 · see citing works
Gao, N., Kumar, A., Jyot, J., & Yu, F.-S. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009351 · Cited by 40 · see citing works
Neisseria gonorrhoeae-induced transactivation of EGFR enhances gonococcal invasion
Swanson, K. V., Griffiss, J. M., Edwards, V. L., Stein, D. C., & Song, W. (2011) · Cellular Microbiology · doi:10.1111/j.1462-5822.2011.01603.x · Cited by 38 · see citing works
Bacterial Penetration of the Mucosal Barrier by Targeting Lipid Rafts
Abraham, S. N., Duncan, M. J., Li, G., & Zaas, D. (2005) · Journal of Investigative Medicine · doi:10.2310/6650.2005.53609 · Cited by 29 · see citing works
Evans, D. J., Kuo, T. C., Kwong, M. S. F., Van, R., & Fleiszig, S. M. J. (2002) · Microbial Pathogenesis · doi:10.1006/mpat.2002.0521 · Cited by 28 · see citing works
Gerçeker, A. A., Zaidi, T., Marks, P. W., Golan, D. E., & Pier, G. B. (2000) · Infection and Immunity · doi:10.1128/iai.68.2.861-870.2000 · Cited by 24 · see citing works
Emam, A., Yu, A., Park, H.-J., Mahfoud, R., Kus, J. V., Burrows, L. L., & Lingwood, C. A. (2006) · Microbiology · doi:10.1099/mic.0.28863-0 · Cited by 23 · see citing works
Bacterial pneumonia in the AIDS patients
Salami, A., Oluboyo, P., Akambi, A., & Fawibe, A. E. (2007) · West African Journal of Medicine · doi:10.4314/wajm.v25i1.28236 · Cited by 18 · see citing works
Song, J. S., Hyun, S. W., Lillihoj, E., & Kim, B. T. (2001) · The Korean Journal of Internal Medicine · doi:10.3904/kjim.2001.16.3.167 · Cited by 14 · see citing works
Superinfections in Pseudomonas aeruginosa ventilator-associated pneumonia.
Giantsou, E., & Manolas, K. I. (2011) · PubMed · Cited by 8 · see citing works
Pseudomonas aeruginosa Internalization by Non-Phagocytic Cells
Engel, J. N. (2007) · Springer eBooks · doi:10.1007/978-1-4020-6097-7_12 · Cited by 7 · see citing works
Keates, S. E., Keates, A. C., Sougioultzis, S., Peek, R. M., & Kelly, C. P. (2003) · Gastroenterology · doi:10.1016/s0016-5085(03)80213-5 · Cited by 1 · see citing works
HIV/AIDS Case Histories: Diagnostic Problems
Godwin, T. A. (1998) · AIDS Patient Care and STDs · doi:10.1089/apc.1998.12.573 · Cited by 1 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
The Epidemiology and Pathogenesis and Treatment of Pseudomonas aeruginosa Infections: An Update
Reynolds, D., & Kollef, M. H. (2021) · Drugs · doi:10.1007/s40265-021-01635-6 · Cited by 729 · see citing works
“aeruginosa infection, the main adhesins are the single flagellum, which is necessary for motility, adhesion to cells and formation of a biofilm, and the type IV pili, which are appendages composed of pilin polymers, which allow the bacteria to move over surfaces in addition to serving relevant roles in biofilm formati…”
BackgroundPseudomonas aeruginosa: An Audacious Pathogen with an Adaptable Arsenal of Virulence Factors
Jurado‐Martín, I., Sainz-Mejías, M., & McClean, S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22063128 · Cited by 722 · see citing works
“Aside from motility, FliC protein is responsible for binding to (i) the membrane glycolipid asialo-GM1 on the apical surface of the lung epithelial cells [79], (ii) heparan sulphate proteoglycans localised on the basolateral surface [84], and (iii) SP-A surfactant [85], whereas FliD mediates adhesion to human”
BackgroundThe Role of the Bacterial Flagellum in Adhesion and Virulence
Haiko, J., & Westerlund-Wikström, B. (2013) · Biology · doi:10.3390/biology2041242 · Cited by 589 · see citing works
“Flagellum Adhesion Calu-3 basolateral surface HSPGs (b) [39]”
BackgroundSecondary bacterial infections associated with influenza pandemics
Morris, D. E., Cleary, D. W., & Clarke, S. C. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.01041 · Cited by 576 · see citing works
“For example the exposure of apical receptors like integrins permit the adhesion of bacteria such as S. aureus and P. aeruginosa (Sanford et al., 1978; Davison and Sanford, 1981; Bucior et al., 2012; Smith and McCullers, 2014).”
BackgroundPasteurella multocida: from Zoonosis to Cellular Microbiology
Wilson, B. A., & Ho, M. (2013) · Clinical Microbiology Reviews · doi:10.1128/cmr.00024-13 · Cited by 548 · see citing works
“On the other hand, an analogous type IV pilin protein, Tfp, of Pseudomonas aeruginosa has been shown to bind lung epithelial cells, leading to pathogenic effects in the host (452).”
BackgroundHelicobacter pylori infection: An overview of bacterial virulence factors and pathogenesis
Kao, C., Sheu, B., & Wu, J.-J. (2016) · Biomedical Journal · doi:10.1016/j.bj.2015.06.002 · Cited by 527 · see citing works
“In animal cell models, Pseudomonas aeruginosa flagella can recognize lung epithelial cells through heparan sulfate, a highly sulfated proteoglycan [28].”
BackgroundType IV pili mechanochemically regulate virulence factors in Pseudomonas aeruginosa
Persat, A., Inclán, Y. F., Engel, J. N., Stone, H. A., & Gitai, Z. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1502025112 · Cited by 426 · see citing works
“However, in natural environments such as the mucosal epithelia of their hosts, bacteria would freely transition from swimming (planktonic) to surface-attached states (16).”
BackgroundHuman Coronavirus NL63 Utilizes Heparan Sulfate Proteoglycans for Attachment to Target Cells
Milewska, A., Zarębski, M., Nowak, P., Stożek, K., Potempa, J., & Pyrć, K. (2014) · Journal of Virology · doi:10.1128/jvi.02078-14 · Cited by 289 · see citing works
“Heparan sulfate inhibits virus attachment and entry 366 As HS proteoglycans are important for entry of several pathogens (36-50), a soluble HS 367 was used to assess whether attachment of HCoV-NL63 is mediated by these molecules.”
Bacterial Flagella: Twist and Stick, or Dodge across the Kingdoms
Rossez, Y., Wolfson, E. B., Holmes, A., Gally, D. L., & Holden, N. J. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1004483 · Cited by 214 · see citing works
“aeruginosa flagella can recognise the basolateral surface of polarized lung epithelial cells through heparan sulphate, a highly sulphated proteoglycan [46].”
BackgroundPseudomonas aeruginosa in Chronic Lung Infections: How to Adapt Within the Host?
Faure, E., Kwong, K., & Nguyen, D. M. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02416 · Cited by 212 · see citing works
“Beyond its ability to activate host cell signaling pathways, the flagellum also promotes adherence and colonization of host surfaces, and various specific targets have been identified including MUC1 mucin (18), heparin sulfate (19), surfactant protein A (20), and asialoGM1 (21).”
BackgroundSurvival of Helicobacter pylori in gastric acidic territory
Ansari, S., & Yamaoka, Y. (2017) · Helicobacter · doi:10.1111/hel.12386 · Cited by 216 · see citing works
Chagnot, C., Zorgani, M. A., Astruc, T., & Desvaux, M. (2013) · Frontiers in Microbiology · doi:10.3389/fmicb.2013.00303 · Cited by 208 · see citing works
“…303 | 9 to plasticware, human mucus and mucin, epithelial cells, enterocytes, vegetables (Grant et al., 1993; Ramphal et al., 1996; Lillehoj et al., 2002; Kirov et al., 2004; Berger et al., 2009b; Mahajan et al., 2009; Shaw et al., 2011; Tran et al., 2011; Bucior et al., 2012; Troge et al., 2012).”
Mechanisms and Targeted Therapies for Pseudomonas aeruginosa Lung Infection
Curran, C. S., Bolig, T. C., & Torabi‐Parizi, P. (2017) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201705-1043so · Cited by 182 · see citing works
Mechanisms of phagocytosis and host clearance of Pseudomonas aeruginosa
Lovewell, R. R., Patankar, Y. R., & Berwin, B. L. (2014) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00335.2013 · Cited by 166 · see citing works
Dancing to Another Tune—Adhesive Moonlighting Proteins in Bacteria
Kainulainen, V., & Korhonen, T. (2014) · Biology · doi:10.3390/biology3010178 · Cited by 154 · see citing works
“epithelium [133] and to human Le x and sialyl Le x determinants in human respiratory mucins [134].”
BackgroundPseudomonas aeruginosa defends against phages through type IV pilus glycosylation
Harvey, H., Bondy‐Denomy, J., Marquis, H., Sztanko, K. M., Davidson, A. R., & Burrows, L. L. (2017) · Nature Microbiology · doi:10.1038/s41564-017-0061-y · Cited by 154 · see citing works
Human Immunodeficiency Virus and Heparan Sulfate: From Attachment to Entry Inhibition
Connell, B. J., & Lortat‐Jacob, H. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2013.00385 · Cited by 143 · see citing works
“These include parasites, for example Plasmodium falciparum (27) bacteria, such as Pseudomonas aeruginosa (28), Borrelia burdorferi (29), or Mycobacterium tuberculosis (30), and many viruses, amongst which are found B (31), C (32), delta (33), and E (34) hepatitis viruses, Human Papillomavirus (35), Herpes viruses (36)…”
BackgroundContact lens-related corneal infection: Intrinsic resistance and its compromise
Fleiszig, S. M. J., Kroken, A. R., Nieto, V., Grosser, M. R., Wan, S. J., Metruccio, M. M. E., & Evans, D. J. (2019) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2019.100804 · Cited by 140 · see citing works
“, 2010), with pili or flagella acting as their respective ligands (Bucior et al., 2012).”
BackgroundGlycosaminoglycans and infection
Park, P. W. (2016) · Frontiers in bioscience · doi:10.2741/4455 · Cited by 139 · see citing works
Skariyachan, S., Sridhar, V. S., Packirisamy, S., Kumargowda, S. T., & Challapilli, S. B. (2018) · Folia Microbiologica · doi:10.1007/s12223-018-0585-4 · Cited by 137 · see citing works
McKee, R. W., Mangalea, M. R., Purcell, E. B., Borchardt, E. K., & Tamayo, R. (2013) · Journal of Bacteriology · doi:10.1128/jb.00501-13 · Cited by 125 · see citing works
Manna, S., Baindara, P., & Mandal, S. M. (2020) · Journal of Infection and Public Health · doi:10.1016/j.jiph.2020.07.003 · Cited by 118 · see citing works
Rossi, E., Paroni, M., & Landini, P. (2018) · Journal of Applied Microbiology · doi:10.1111/jam.14089 · Cited by 116 · see citing works
“At low c-di-GMP concentrations, FleQ is an activator of flagella biosynthesis and a repressor of pel operon.”
BackgroundInfluentialWu, W., Jin, Y., Bai, F., & Jin, S. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-397169-2.00041-x · Cited by 115 · see citing works
Type IV Pili: dynamic bacterial nanomachines
Ellison, C. K., Whitfield, G. B., & Brun, Y. V. (2021) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuab053 · Cited by 114 · see citing works
Wang, F., Coureuil, M., Osinski, T., Orlova, A., Altindal, T., Gesbert, G., Nassif, X., Egelman, E. H., & Craig, L. (2017) · Structure · doi:10.1016/j.str.2017.07.016 · Cited by 111 · see citing works
“PaK pili function in adhesion to glycans on the surfaces of epithelial cells (Bucior et al., 2012; Irvin et al., 1989; Saiman and Prince, 1993).”
BackgroundVirulence factors of uropathogens and their role in host pathogen interactions
Govindarajan, D. K., & Kandaswamy, K. (2022) · The Cell Surface · doi:10.1016/j.tcsw.2022.100075 · Cited by 107 · see citing works
Physical stress and bacterial colonization
Otto, M. J. (2014) · FEMS Microbiology Reviews · doi:10.1111/1574-6976.12088 · Cited by 100 · see citing works
Anyan, M. E., Amiri, A., Harvey, C. W., Tierra, G., Morales-Soto, N., Driscoll, C. M., Alber, M., & Shrout, J. D. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1414661111 · Cited by 91 · see citing works
“aeruginosa biofilm formation (24) and mediate attachment to different surfaces, including eukaryotic epithelial cells (25).”
BackgroundAn Organ System-Based Synopsis of Pseudomonas aeruginosa Virulence
Morin, C. D., Déziel, É., Gauthier, J., Lévesque, R. C., & Lau, G. W. (2021) · Virulence · doi:10.1080/21505594.2021.1926408 · Cited by 90 · see citing works
“bind N-glycans at the apical surface of polarized cells while the flagellum will bind to heparan sulfate present at the basolateral side of the cells [129].”
BackgroundCrabbé, A., Liu, Y., Matthijs, N., Rigole, P., de la Fuente‐Núñez, C., Davis, R. R., Ledesma, M. A., Sarker, S. F., Houdt, R. V., Hancock, R. E. W., et al. (2017) · Scientific Reports · doi:10.1038/srep43321 · Cited by 86 · see citing works
Fila, G., Kawiak, A., & Grinholc, M. (2016) · Virulence · doi:10.1080/21505594.2016.1250995 · Cited by 83 · see citing works
Deshpande, R., & Zou, C. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155356 · Cited by 80 · see citing works
“The flagella and Type IV pili (TFP) play the role of adhesins for host cells [9].”
BackgroundPI3-kinase activation is critical for host barrier permissiveness to Listeria monocytogenes
Gessain, G., Tsai, Y.-H., Travier, L., Bonazzi, M., Grayo, S., Cossart, P., Charlier, C., Disson, O., & Lecuit, M. (2015) · The Journal of Experimental Medicine · doi:10.1084/jem.20141406 · Cited by 80 · see citing works
Bruzaud, J., Tarrade, J., Coudreuse, A., Canette, A., Herry, J., de Givenchy, E. T., Darmanin, T., Guittard, F., Guilbaud, M., & Bellon‐Fontaine, M. (2015) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2015.04.036 · Cited by 73 · see citing works
Plasma membrane reorganization: A glycolipid gateway for microbes.
Aigal, S., Claudinon, J., & Römer, W. (2015) · Biochimica et Biophysica Acta · doi:10.1016/j.bbamcr.2014.11.014 · Cited by 59 · see citing works
Latino, L., Midoux, C., Hauck, Y., Vergnaud, G., & Pourcel, C. (2016) · Microbiology · doi:10.1099/mic.0.000263 · Cited by 68 · see citing works
“aeruginosa cells to the host epithelium and also play a role in biofilm formation (Bucior et al., 2012; Klausen et al., 2003; O’Toole & Kolter, 1998).”
Gu, M., & Pang, Z. (2025) · Phytomedicine · doi:10.1016/j.phymed.2025.156663 · Cited by 65 · see citing works
Innate Immune Signaling Activated by MDR Bacteria in the Airway
Parker, D., Ahn, D. S., Cohen, T. S., & Prince, A. S. (2015) · Physiological Reviews · doi:10.1152/physrev.00009.2015 · Cited by 67 · see citing works
Singh, A. K., Pluvinage, B., Higgins, M. A., Dalia, A. B., Woodiga, S. A., Flynn, M., Lloyd, A. R., Weiser, J. N., Stubbs, K. A., Boraston, A. B., et al. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1004364 · Cited by 62 · see citing works
“potential myriad of proteins from single, dedicated surface proteins to components of complex flagellar structures [43–46].”
BackgroundRole of Glycosaminoglycans in Infectious Disease
Jinno, A., & Park, P. W. (2014) · Methods in molecular biology · doi:10.1007/978-1-4939-1714-3_45 · Cited by 61 · see citing works
“Because many studies have examined the role of GAGs as attachment sites for viruses [68–70], bacteria [24, 71, 72], and parasites [73, 74], and microbial binding and attachment assays are established, these will not be discussed in this review.”
BackgroundSialic Acids as Receptors for Pathogens
Burzyńska, P., Sobala, Ł. F., Mikołajczyk, K., Jodłowska, M., & Jaśkiewicz, E. (2021) · Biomolecules · doi:10.3390/biom11060831 · Cited by 50 · see citing works
Klebsiella pneumoniae and Pseudomonas aeruginosa
Wu, M., & Li, X. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-397169-2.00087-1 · Cited by 60 · see citing works
Assessing Travel Conditions: Environmental and Host Influences on Bacterial Surface Motility
Mattingly, A. E., Weaver, A. A., Dimkovikj, A., & Shrout, J. D. (2018) · Journal of Bacteriology · doi:10.1128/jb.00014-18 · Cited by 56 · see citing works
Sendra, E., Fernández-Muñoz, A., Zamorano, L., Oliver, A., Horcajada, J. P., Juan, C., & Gómez-Zorrilla, S. (2024) · Infection · doi:10.1007/s15010-024-02313-x · Cited by 59 · see citing works
Wiesmann, C. L., Wang, N. R., Zhang, Y., Liu, Z., & Haney, C. H. (2022) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuac048 · Cited by 53 · see citing works
A guide to polarized airway epithelial models for studies of host–pathogen interactions
Hasan, S., Šebo, P., & Osička, R. (2018) · FEBS Journal · doi:10.1111/febs.14582 · Cited by 52 · see citing works
Peñaranda, C., Chumbler, N. M., & Hung, D. T. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009534 · Cited by 52 · see citing works
“Because the type IV pilus is required for maximal adherence to and invasion of host cells [36], we examined the impact of decreased invasion of ΔalgR on the ability of bacteria to survive intracellularly.”
BackgroundCurrent concepts on Pseudomonas aeruginosa interaction with human airway epithelium
Muggeo, A., Coraux, C., & Guillard, T. (2023) · PLoS Pathogens · doi:10.1371/journal.ppat.1011221 · Cited by 51 · see citing works
Host Cell Polarity Proteins Participate in Innate Immunity to Pseudomonas aeruginosa Infection
Tran, C. S., Eran, Y., Ruch, T. R., Bryant, D. M., Datta, A., Brakeman, P., Kierbel, A., Wittmann, T., Metzger, R. J., Mostov, K. E., et al. (2014) · Cell Host & Microbe · doi:10.1016/j.chom.2014.04.007 · Cited by 51 · see citing works
“The mutant PAKΔfliC, which fails to produce flagellin, shows ~50% reduction in binding to the apical surface of polarized MDCK cells (Bucior et al., 2012).”
BackgroundMethodTran, C. S., Rangel, S. M., Almblad, H., Kierbel, A., Givskov, M., Tolker‐Nielsen, T., Hauser, A. R., & Engel, J. N. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1004479 · Cited by 51 · see citing works
“aeruginosa infection of polarized epithelial cells to model host-pathogen interactions at the mucosal barrier [12,13].”
BackgroundPathogenic Mannheimia haemolytica Invades Differentiated Bovine Airway Epithelial Cells
Cozens, D., Sutherland, E., Lauder, M., Taylor, G., Berry, C. C., & Davies, R. L. (2019) · Infection and Immunity · doi:10.1128/iai.00078-19 · Cited by 54 · see citing works
“interactions of various bacterial and viral pathogens with different host species (39-57).”
BackgroundAnti-Pseudomonas aeruginosa Vaccines and Therapies: An Assessment of Clinical Trials
Elmassry, M. M., Colmer‐Hamood, J. A., Kopel, J. J., Francisco, M. J. S., & Hamood, A. N. (2023) · Microorganisms · doi:10.3390/microorganisms11040916 · Cited by 49 · see citing works
“aeruginosa in cell motility, adhesion, and colonization [103,104].”
Rossy, T., Distler, T., Meirelles, L. A., Pezoldt, J., Kim, J., Talà, L., Bouklas, N., Deplancke, B., & Persat, A. (2023) · PLoS Biology · doi:10.1371/journal.pbio.3002209 · Cited by 56 · see citing works
Crabbé, A., Ledesma, M. A., & Nickerson, C. A. (2014) · Pathogens and Disease · doi:10.1111/2049-632x.12180 · Cited by 49 · see citing works
“…planktonic cells and aggregates) can enhance the expression of basolateral receptors at the apical surface to facilitate its uptake through activation of host signaling pathways (Kierbel et al., 2005; Gassama-Diagne et al., 2006; Kierbel et al., 2007; Lepanto et al., 2011; Bucior et al., 2012).”
Bucior, I., Abbott, J. A., Song, Y., Matthay, M. A., & Engel, J. N. (2013) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00387.2012 · Cited by 47 · see citing works
“aeruginosa binds to N-glycan chains on the apical (AP) surface of the host epithelium, whereas flagella mediate binding to heparan sulfate chains of heparan sulfate proteoglycans (HSPGs) on the basolateral (BL) surface (7, 8).”
BackgroundCollagen and hyaluronan at wound sites influence early polymicrobial biofilm adhesive events
Birkenhauer, E., Neethirajan, S. R., & Weese, J. S. (2014) · BMC Microbiology · doi:10.1186/1471-2180-14-191 · Cited by 47 · see citing works
“aureus relies mainly on surface proteinprotein interactions for attachment [23,24,41,44-46].”
BackgroundGuillard, T., Pons, S., Roux, D., Pier, G. B., & Skurnik, D. (2016) · BioEssays · doi:10.1002/bies.201500180 · Cited by 47 · see citing works
Targeting the Mucosal Barrier: How Pathogens Modulate the Cellular Polarity NetworkPreprint
Ruch, T. R., & Engel, J. N. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a027953 · Cited by 47 · see citing works
“Cite this article as Cold Spring Harb Perspect Biol doi: 10.1101/cshperspect.a027953 5 lows more efficient colonization at the apical surface (Bucior et al. 2010, 2012).”
BackgroundInfluentialGolovkine, G. R., Faudry, É., Bouillot, S., Elsen, S., Attrée, I., & Huber, P. (2016) · PLoS Pathogens · doi:10.1371/journal.ppat.1005377 · Cited by 45 · see citing works
“Pili have also been shown to preferentially interact with the cells’ basolateral domain [6, 18, 19].”
BackgroundJackson, L. M. D., & Waters, V. J. (2020) · Journal of Cystic Fibrosis · doi:10.1016/j.jcf.2020.10.008 · Cited by 44 · see citing works
Banerjee, P., Sahoo, P. K., Sheenu, Adhikary, A., Ruhal, R., & Jain, D. (2021) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2021.101001 · Cited by 44 · see citing works
Ginseng alleviates microbial infections of the respiratory tract: a review
Iqbal, H., & Rhee, D. (2019) · Journal of Ginseng Research · doi:10.1016/j.jgr.2019.12.001 · Cited by 41 · see citing works
“aeruginosa disrupts airway homeostasis in the lung by damaging the epithelium and evading innate and adaptive immune responses [84,85].”
BackgroundDavid, A., Tahrioui, A., Tareau, A.-S., Forge, A., Gonzalez, M., Bouffartigues, E., Lesouhaitier, O., & Chevalier, S. (2024) · Antibiotics · doi:10.3390/antibiotics13080688 · Cited by 40 · see citing works
“Flagella crosslink the bacterial pole vertically to the surface [25,26], and the surface “pits” or “canyons” restrict flagellar rotation, leading to envelope deformation, and providing a mechanical signal [27].”
BackgroundJia, X., Gu, M., Dai, J., Wang, J., Zhang, Y., & Pang, Z. (2024) · Inflammopharmacology · doi:10.1007/s10787-023-01416-5 · Cited by 38 · see citing works
“Furthermore, P. aeruginosa infection was found to induce the activation of PI3K, AKT and NF-κB (Bucior et al. 2012; Joseph et al. 2005).”
Khan, H., Nair, V. R., Ruhl, C. R., Álvarez-Arguedas, S., Rendiz, J. L. G., Franco, L. H., Huang, L., Shaul, P. W., Kim, J., Xie, Y., et al. (2020) · eLife · doi:10.7554/elife.52551 · Cited by 36 · see citing works
“aeruginosa (Bucior et al., 2012), Bacillus anthracis (Russell et al.”
Modulation of innate immunity in airway epithelium for host-directed therapy
Myszor, I. T., & Gudmundsson, G. H. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1197908 · Cited by 35 · see citing works
Zhang, Y., Lü, P., Pan, Z., Zhu, Y., Ma, J., Zhong, X., Dong, W., Lu, C., & Yao, H. (2018) · Applied and Environmental Microbiology · doi:10.1128/aem.01385-18 · Cited by 31 · see citing works
“adhesion to and invasion in the host or escape from the host defense systems (19, 29).”
BackgroundXuan, G., Lin, H., Kong, J., & Wang, J. (2022) · Microbiology Spectrum · doi:10.1128/spectrum.01356-22 · Cited by 30 · see citing works
Ammendola, S., D'Amico, Y., Chirullo, B., Drumo, R., Ciavardelli, D., Pasquali, P., & Battistoni, A. (2016) · Metallomics · doi:10.1039/c6mt00108d · Cited by 30 · see citing works
Hayashi, N., Nishizawa, H., Kitao, S., Deguchi, S., Nakamura, T., Fujimoto, A., Shikata, M., & Gotoh, N. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.02.031 · Cited by 29 · see citing works
“The flagella and TFP are adhesins for host cells [22].”
BackgroundInfluentialMicrobial uptake by the respiratory epithelium: outcomes for host and pathogen
Bertuzzi, M., Hayes, G., & Bignell, E. (2019) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuy045 · Cited by 29 · see citing works
Taouai, M., Chakroun, K., Sommer, R., Michaud, G., Giacalone, D., Maaouia, M. A. B., Vallin, A., Mathiron, D., Abidi, R., Darbre, T., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b00481 · Cited by 28 · see citing works
“aeruginosa as do the negatively charged glycosaminoglycan heparane sulfates of host cell walls.(57)”
BackgroundWolfson, E. B., Elvidge, J., Tahoun, A. A. E., Gillespie, T., Mantell, J., McAteer, S. P., Rossez, Y., Paxton, E. A., Lane, F. M., Shaw, D. J., et al. (2020) · Microbiology · doi:10.1099/mic.0.000959 · Cited by 28 · see citing works
“Pseudomonas aeruginosa flagella bind to MUC1 and heparin-sulphated proteoglycans and E. coli flagella bind to ganglio-side receptor GM1 and charged glycerolipids, resulting in immuno-modulation and invasion [28, 52–54].”
BackgroundTan, R. M., Kuang, Z., Hao, Y., & Lau, G. W. (2013) · Journal of Innate Immunity · doi:10.1159/000354304 · Cited by 28 · see citing works
McDaniel, M. S., Lindgren, N. R., Billiot, C. E., Valladares, K. N., Sumpter, N. A., & Swords, W. E. (2022) · Microbiology Spectrum · doi:10.1128/spectrum.03846-22 · Cited by 27 · see citing works
Heparin, Heparan Sulphate and Sepsis: Potential New Options for Treatment
Hogwood, J., Gray, E., & Mulloy, B. (2023) · Pharmaceuticals · doi:10.3390/ph16020271 · Cited by 28 · see citing works
“aeruginosa utilises interactions between its pili and host N-glycans to attach to and invade the apical surface of fully polarised epithelial cells, at the basolateral surface interactions between bacterial flagella and host HS perform the same function [58,59].”
BackgroundWagener, B. M., Hu, R.-H., Wu, S., Pittet, J., Ding, Q., & Che, P. (2021) · Toxins · doi:10.3390/toxins13110776 · Cited by 26 · see citing works
Epithelial Uptake of Flagella Initiates Proinflammatory Signaling
Parker, D., & Prince, A. S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0059932 · Cited by 26 · see citing works
“through the paracellular spaces to reach the basolateral aspects of the polarized airway epithelium [31], where in vitro studies suggest that attachment occurs [5].”
BackgroundEvidence for intracellular Pseudomonas aeruginosa
Resko, Z. J., Suhi, R. F., Thota, A. V., & Kroken, A. R. (2024) · Journal of Bacteriology · doi:10.1128/jb.00109-24 · Cited by 25 · see citing works
“Other bacterial surface factors that are predicted to influence surface attachment and subsequent invasion include the flagella, which is thought to facilitate cellular association through binding of N-glycans of polarized epithelial cells (55, 56).”
BackgroundTorres, I. M., Demirdjian, S., Vargas, J., Goodale, B. C., & Berwin, B. L. (2017) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00524.2016 · Cited by 23 · see citing works
Glycobiology of syndecan-1 in bacterial infections
Aquino, R. S., Teng, Y. H.-F., & Park, P. W. (2018) · Biochemical Society Transactions · doi:10.1042/bst20170395 · Cited by 23 · see citing works
“For example, while both Gram-positive Staphylococcus aureus [16] and Gram-negative Pseudomonas aeruginosa [17] can bind to HS, they do not bind to Sdc1 [18,19].”
BackgroundBanerjee, P., Chanchal, & Jain, D. (2019) · ACS Chemical Biology · doi:10.1021/acschembio.9b00255 · Cited by 23 · see citing works
Molecular interactions betweenNeisseria meningitidisand its human host
Coureuil, M., Jamet, A., Bille, E., Lécuyer, H., Bourdoulous, S., & Nassif, X. (2019) · Cellular Microbiology · doi:10.1111/cmi.13063 · Cited by 22 · see citing works
Beasley, K. L., Cristy, S. A., Elmassry, M. M., Dzvova, N., Colmer‐Hamood, J. A., & Hamood, A. N. (2020) · PLoS ONE · doi:10.1371/journal.pone.0240351 · Cited by 22 · see citing works
“To survive within different host niches and to combat host defenses, P . aeruginosa adjusts the production of numerous extracellular and cell-associated virulence factors [10–15].”
Shippy, D. C., Eakley, N. M., Mikheil, D. M., & Fadl, A. A. (2014) · Current Microbiology · doi:10.1007/s00284-014-0521-z · Cited by 22 · see citing works
Susilowati, H., Murakami, K., Yumoto, H., Amoh, T., Hirao, K., Hirota, K., Matsuo, T., & Miyake, Y. (2017) · BioMed Research International · doi:10.1155/2017/3191752 · Cited by 22 · see citing works
“The bind between the adhesins with a membrane receptor initiates bacterial attachment to the epithelial cells [22].”
BackgroundReceptor recognition by meningococcal type IV pili relies on a specific complex N -glycan
Guennec, L. L., Virion, Z., Bouzinba-Ségard, H., Masselot, C. R., Léonard, R., Nassif, X., Bourdoulous, S., & Coureuil, M. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1919567117 · Cited by 21 · see citing works
“For instance, Tfp of Vibrio parahaemolyticus, a naturally occurring bacterium common in coastal waters, can interact with chitin, a long-chain polymer of N-acetylglucosamine abundantly found in the ocean (8), while Tfp from Pseudomonas aeruginosa, an important opportunistic pathogen causing acute and chronic pulmonary…”
BackgroundGu, M., Su, W., Dai, J., Wang, J., Jia, X., Yao, J., Zhang, G., Zhu, Q., & Pang, Z. (2023) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2023.116899 · Cited by 20 · see citing works
Host cell binding of the flagellar tip protein ofCampylobacter jejuni
Freitag, C. M., Strijbis, K., & van Putten, J. P. M. (2016) · Cellular Microbiology · doi:10.1111/cmi.12714 · Cited by 20 · see citing works
Synthesized Heparan Sulfate Competitors Attenuate Pseudomonas aeruginosa Lung Infection
Lorè, N. I., Veraldi, N., Riva, C., Sipione, B., Spagnuolo, L., Fino, I. D., Melessike, M., Calzi, E., Bragonzi, A., Naggi, A., et al. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19010207 · Cited by 20 · see citing works
“aeruginosa and a binding site for bacterial flagella, and this could suggest another role during infection [32,33].”
BackgroundGarai, P., Lahiri, A., Ghosh, D., Chatterjee, J., & Chakravortty, D. (2015) · Microbiology · doi:10.1099/mic.0.000204 · Cited by 20 · see citing works
Yamazaki, K., Kashimoto, T., Morita, M., Kado, T., Matsuda, K., Yamasaki, M., & Ueno, S. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.00123 · Cited by 19 · see citing works
“Adhesion and Biofilm Formation Type IV pili are known to play a role in cell adhesion, twitching motility, and the uptake of foreign genes (Paranjpye and Strom, 2005; Bucior et al., 2012).”
BackgroundCnm of Streptococcus mutans is important for cell surface structure and membrane permeability
Naka, S., Matsuoka, D., Goto, K., Misaki, T., Nagasawa, Y., Ito, S., Nomura, R., Nakano, K., & Matsumoto‐Nakano, M. (2022) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2022.994014 · Cited by 19 · see citing works
“Surface components for bacterial contact with environmental niches are involved in bacterial adhesion to and invasion of a host, and escape from host defense systems (Bucior et al., 2012; Chagnot et al., 2013).”
BackgroundAssessing Pseudomonas Virulence Using Host Cells
Bucior, I., Tran, C. S., & Engel, J. N. (2014) · Methods in molecular biology · doi:10.1007/978-1-4939-0473-0_57 · Cited by 19 · see citing works
Pletzer, D., Sun, E., Ritchie, C., Wilkinson, L., Liu, L. T., Trimble, M. J., Wolfmeier, H., Blimkie, T. M., & Hancock, R. E. W. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1008444 · Cited by 19 · see citing works
“To establish an infection, it has been proposed that Pseudomonas type IV pili are involved in binding to the apical epithelial surface, while flagellar-mediated motility is proposed to be important for the colonization of the basolateral surface of airway epithelium [7].”
BackgroundAl-kafaween, M. A., Hilmi, A. B. M., Al‐Jamal, H. A. N., Elsahoryi, N. A., Jaffar, N., & Zahri, M. K. (2020) · PubMed Central · doi:10.30498/ijb.2020.2542 · Cited by 19 · see citing works
“aeruginosa, and each represents important virulence factors with respect to binding and signaling for cell–cell communication (43, 44).”
BackgroundDemirdjian, S., Hopkins, D. C., Cumbal, N., Lefort, C. T., & Berwin, B. L. (2020) · Infection and Immunity · doi:10.1128/iai.00011-20 · Cited by 18 · see citing works
“basolateral surface of the polarized epithelium (21, 22).”
BackgroundLiu, Y., Hussain, F., Negm, O. H., Paiva, A. C., Halliday, N., Dubern, J., Singh, S., Muntaka, S., Wheldon, L. M., Luckett, J., et al. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.03018 · Cited by 18 · see citing works
Pseudomonas aeruginosa clinical blood isolates display significant phenotypic variability
Scheffler, R. J., Bratton, B. P., & Gitai, Z. (2022) · PLoS ONE · doi:10.1371/journal.pone.0270576 · Cited by 17 · see citing works
- Authors
- Bucior, I., Pielage, J. F., & Engel, J. N.
- Affiliations
- University of California, San Francisco (US)
- Corresponding author
- Bucior, Iwona
- Pielage, Julia F.
- Engel, Joanne N.
- ORCID
- Engel, Joanne N.
- Venue
- PLoS Pathogens
- Publisher
- Public Library of Science (PLoS)
- Published
- 2012-04-05
- Volume
- 8
- Issue
- 4
- Pages
- e1002616
- ISSN
- 1553-7366 (ISSN-L)
- 1553-7374
- PMC
- PMC3320588
- OpenAlex
- W2073200952
- Cited by
- 221
- References
- 66
- Citations by year
- 2026: 9 · 2025: 17 · 2024: 13 · 2023: 21 · 2022: 15 · 2021: 13 · 2020: 17 · 2019: 17 · 2018: 15 · 2017: 20 · 2016: 14 · 2015: 10 · 2014: 24 · 2013: 14 · 2012: 2
- FWCI
- 6.42
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS Pathogens (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- Funders
- National Institutes of Health
- National Institute of Allergy and Infectious Diseases (P01AI053194, R01AI065902)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bacterial biofilms and quorum sensing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Escherichia coli research studies
- Keywords
- Pseudomonas aeruginosa, type IV pili, bacterial flagellum, bacterial adhesion, lung epithelium, N-glycans, heparan sulfate proteoglycans, phosphatidylinositol 3-kinase/Akt signaling, epidermal growth factor receptor, Shc adaptor protein, bacterial invasion, host-pathogen interaction, airway infection
- MeSH terms
- Bacterial Adhesion, Cell Line, Enzyme Activation, Flagella, Heparin, Humans, Lung, Mutation, Fimbriae, Bacterial, Pseudomonas aeruginosa, Pseudomonas Infections, Adhesins, Bacterial, Heparan Sulfate Proteoglycans, Phosphatidylinositol 3-Kinases, Respiratory Mucosa, Proto-Oncogene Proteins c-akt, ErbB Receptors
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 ›
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