Legionella pneumophila Exploits PI(4)P to Anchor Secreted Effector Proteins to the Replicative Vacuole

The genome of the social amoeba Dictyostelium discoideum

Eichinger, L., Pachebat, J. A., Glöckner, G., Rajandream, M.-A., Sucgang, R., Berriman, M., Song, J., Olsen, R., Szafranski, K., Xu, Q., et al. (2005) · Nature · doi:10.1038/nature03481 · Cited by 1,351

Legionnaires' Disease

McDade, J. E., Shepard, C. C., Fraser, D. W., Tsai, T. F., Redus, M. A., & Dowdle, W. R. (1977) · New England Journal of Medicine · doi:10.1056/nejm197712012972202 · Cited by 1,230

Conjugative Transfer by the Virulence System of Legionella pneumophila

Vogel, J. P., Andrews, H. L., Wong, S. K., & Isberg, R. R. (1998) · Science · doi:10.1126/science.279.5352.873 · Cited by 721

Chemotaxis: signalling the way forward

Haastert, P. J. M. V., & Devreotes, P. N. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1435 · Cited by 706

The Legionnaires' disease bacterium (Legionella pneumophila) inhibits phagosome-lysosome fusion in human monocytes.

Horwitz, M. A. (1983) · The Journal of Experimental Medicine · doi:10.1084/jem.158.6.2108 · Cited by 706

Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity

Cazalet, C., Rusniok, C., Brüggemann, H., Zidane, N., Magnier, A., Ma, L., Tichit, M., Jarraud, S., Bouchier, C., Vandenesch, F., et al. (2004) · Nature Genetics · doi:10.1038/ng1447 · Cited by 656

Charcoal-yeast extract agar: primary isolation medium for Legionella pneumophila

FEELEY, J. C., Gibson, R. J., GORMAN, G. W., Langford, N. C., Rasheed, J. K., Mackel, D. C., & Baine, W. B. (1979) · Journal of Clinical Microbiology · doi:10.1128/jcm.10.4.437-441.1979 · Cited by 643

Chapter 2 Cultivation and Synchronous Morphogenesis of Dictyostelium under Controlled Experimental Conditions

Sussman, M. (1987) · Methods in cell biology · doi:10.1016/s0091-679x(08)61635-0 · Cited by 595

FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns(4)P

Godi, A., Campli, A. D., Konstantakopoulos, A., Tullio, G. D., Alessi, D. R., Kular, G. S., Daniele, T., Marra, P., Lucocq, J. M., & Matteis, M. A. D. (2004) · Nature Cell Biology · doi:10.1038/ncb1119 · Cited by 554

A Bacterial Guanine Nucleotide Exchange Factor Activates ARF on Legionella Phagosomes

Nagai, H., Kagan, J. C., Zhu, X., Kahn, R., & Roy, C. R. (2002) · Science · doi:10.1126/science.1067025 · Cited by 551

Oligomerization Inhibits Legionella pneumophila PlaB Phospholipase A Activity

Kuhle, K., Krausze, J., Curth, U., Rößle, M., Heuner, K., Lang, C., & Flieger, A. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.573196 · Cited by 14

Legionella pneumophila effector Lem4 is a membrane-associated protein tyrosine phosphatase

Beyrakhova, K. A., Li, L., Xu, C., Gagarinova, A. G., & Cygler, M. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.003845 · Cited by 18

PtdIns(4)P Signalling and Recognition Systems

Lenoir, M., & Overduin, M. (2013) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-6331-9_5 · Cited by 14

Cellular cholesterol licenses Legionella pneumophila intracellular replication in macrophages

Ondari, E., Wilkins, A., Latimer, B., Dragoi, A., & Ivanov, S. S. (2023) · Microbial Cell · doi:10.15698/mic2023.01.789 · Cited by 13

Immunomagnetic Purification of Fluorescent Legionella-Containing Vacuoles

Finsel, I., Hoffmann, C., & Hilbi, H. (2013) · Methods in molecular biology · doi:10.1007/978-1-62703-302-2_24 · Cited by 13

Global cellular changes induced by Legionella pneumophila infection of bone marrow-derived macrophages

Fortier, A. H., Faucher, S. P., Diallo, K., & Gros, P. (2011) · Immunobiology · doi:10.1016/j.imbio.2011.06.008 · Cited by 13

CRISPR/Cas9 mutagenesis reveals an essential role of PI4KB in promoting growth and resisting hemorrhagic disease caused by GCRV-II infection in juvenile grass carp

Zhang, J., Zhang, L. Q., Wu, X. M., Tao, M. H., Chen, Y., & Chang, M. X. (2024) · Water Biology and Security · doi:10.1016/j.watbs.2024.100323 · Cited by 12

Subversion of host cell signaling: The arsenal of Rickettsial species

Huang, D. Y., Luo, J., Ouyang, X., & Song, L. (2022) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2022.995933 · Cited by 12

Hostile Takeover: Hijacking of Endoplasmic Reticulum Function by T4SS and T3SS Effectors Creates a Niche for Intracellular Pathogens

Tsai, A. Y., English, B. C., & Tsolis, R. M. (2019) · Microbiology Spectrum · doi:10.1128/microbiolspec.psib-0027-2019 · Cited by 12

Phagocytic Entry of Legionella pneumophila into Macrophages through Phosphatidylinositol 3,4,5-Trisphosphate-Independent Pathway

Harada, T., Tanikawa, T., Iwasaki, Y., Yamada, M., Imai, Y., & Miyake, M. (2012) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b11-00011 · Cited by 11

Migration of Acanthamoeba through Legionella biofilms is regulated by the bacterial Lqs‐LvbR network, effector proteins and the flagellum

Hochstrasser, R., Michaelis, S., Brülisauer, S., Sura, T., Fan, M., Maaß, S., Becher, D., & Hilbi, H. (2022) · Environmental Microbiology · doi:10.1111/1462-2920.16008 · Cited by 11

Correction: Legionella Eukaryotic-Like Type IV Substrates Interfere with Organelle Trafficking

de Felipe, K. S., Glover, R. T., Charpentier, X., Anderson, O. R., Reyes, M., Pericone, C. D., & Shuman, H. A. (2010) · PLoS Pathogens · doi:10.1371/annotation/c7438c1b-5b65-4f4c-aaa3-062909e89525 · Cited by 11

Correction: Structural Basis for Rab1 De-AMPylation by the Legionella pneumophila Effector SidD

Chen, Y., Tascón, I., Neunuebel, M. R., Pallara, C., Brady, J. M., Kinch, L. N., Fernández-Recio, J., Rojas, A. L., Machner, M. P., & Hierro, A. (2013) · PLoS Pathogens · doi:10.1371/annotation/2b8e6418-2496-4ffb-b230-95d90b748086 · Cited by 11

Heterologous Expression and Assembly of Human TLR Signaling Components in Saccharomyces cerevisiae

Coronas-Serna, J. M., del Val, E., Kagan, J. C., Molina, M., & Cid, V. J. (2021) · Biomolecules · doi:10.3390/biom11111737 · Cited by 10

Cross-family small GTPase ubiquitination by the intracellular pathogen Legionella pneumophila

Steinbach, A. M., Bhadkamkar, V., Jimenez‐Morales, D., Stevenson, E. J., Jang, G. Μ., Krogan, N. J., Swaney, D. L., & Mukherjee, S. (2023) · Molecular Biology of the Cell · doi:10.1091/mbc.e23-06-0260 · Cited by 10

Dictyostelium Host Response to Legionella Infection: Strategies and Assays

Bozzaro, S., Peracino, B., & Eichinger, L. (2012) · Methods in molecular biology · doi:10.1007/978-1-62703-161-5_26 · Cited by 11

Interactions of Legionella Effector Proteins with Host Phosphoinositide Lipids

Weber, S., Dolinsky, S., & Hilbi, H. (2012) · Methods in molecular biology · doi:10.1007/978-1-62703-161-5_23 · Cited by 10

The Yeast Arf GTPase-activating Protein Age1 Is Regulated by Phospholipase D for Post-Golgi Vesicular Transport

Benjamin, J. J. R., Poon, P. P., Lewis, S. M., Auger, A., Wong, T. A., Singer, R. A., & Johnston, G. C. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.185108 · Cited by 10

Cell biology and immunology lessons taught by Legionella pneumophila

Zhu, W., & Luo, Z. (2015) · Science China Life Sciences · doi:10.1007/s11427-015-4945-x · Cited by 9

Structural insight into the membrane targeting domain of the Legionella deAMPylase SidD

Tascón, I., Li, X., Lucas, M., Nelson, D. M., Vidaurrazaga, A., Lin, Y.-H., Rojas, A. L., Hierro, A., & Machner, M. P. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1008734 · Cited by 8

Small molecule communication of Legionella : the ins and outs of autoinducer and nitric oxide signaling

Michaelis, S., Gómez-Valero, L., Chen, T., Schmid, C., Buchrieser, C., & Hilbi, H. (2024) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00097-23 · Cited by 7

The large GTPase atlastin controls ER remodeling around a pathogen vacuole

Steiner, B., Weber, S., Kaech, A., Ziegler, U., & Hilbi, H. (2018) · Communicative & Integrative Biology · doi:10.1080/19420889.2018.1440880 · Cited by 7

Expanding Francisella models: Pairing up the soil amoeba Dictyostelium with aquatic Francisella

Brenz, Y., Winther-Larsen, H. C., & Hagedorn, M. (2017) · International Journal of Medical Microbiology · doi:10.1016/j.ijmm.2017.08.001 · Cited by 7

Legionella pneumophila infection is enhanced in a RacH-null mutant of Dictyostelium

Balest, A., Peracino, B., & Bozzaro, S. (2011) · Communicative & Integrative Biology · doi:10.4161/cib.4.2.14381 · Cited by 7

Bacterial pathogens hijack host cell peroxisomes for replication vacuole expansion and integrity

Hossain, M. J., Romanov, K. A., Jian, J., Swaby, L. C., Bandyopadhyay, S., Guan, I., Thomas, S. M., Olive, A. J., & O’Connor, T. J. (2025) · Science Advances · doi:10.1126/sciadv.adr8005 · Cited by 6

Dictyostelium Host Response to Legionella Infection: Strategies and Assays

Bozzaro, S., Buracco, S., Peracino, B., & Eichinger, L. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9048-1_23 · Cited by 6

The intracellular growth of the vacuolar pathogen Legionella pneumophila is dependent on the acyl chain composition of host membranes

Wilkins, A. A., Schwarz, B. H., Torres-Escobar, A., Castore, R., Landry, L., Latimer, B., Bohrnsen, E., Bosio, C. M., Dragoi, A., & Ivanov, S. S. (2024) · Frontiers in Bacteriology · doi:10.3389/fbrio.2024.1322138 · Cited by 6

Molecular evolution and adaptations of Legionella pneumophila from amoebae hosts to macrophages

Shin, C. J., & Kwaik, Y. A. (2026) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2026.1787137 · Cited by 4

Dictyostelium Dynamin Superfamily GTPases Implicated in Vesicle Trafficking and Host-Pathogen Interactions

Katic, A., Hüsler, D., Letourneur, F., & Hilbi, H. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.731964 · Cited by 5

Comparative genomics analyses of Actinobacteriota identify Golgi phosphoprotein 3 (GPP34) as a widespread ancient protein family associated with sponge symbiosis

Ferreira, C., Burgsdorf, I., Perez, T., Ramírez, G. A., Lalzar, M., Huchon, D., & Steindler, L. (2025) · Microbiome · doi:10.1186/s40168-024-01963-1 · Cited by 4

The Structural Basis for Calcium Inhibition of Lipid Kinase PI4K IIα and Comparison With the Apo State

Bäumlová, A., GREGOR, J., & Bouřa, E. (2016) · Physiological Research · doi:10.33549/physiolres.933344 · Cited by 4

Analysis of Legionella Metabolism by Pathogen Vacuole Proteomics

Manske, C., Finsel, I., Hoffmann, C., & Hilbi, H. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-8695-8_6 · Cited by 4

Exploiting the ubiquitin and phosphoinositide pathways by the Legionella pneumophila effector, SidC

Wasilko, D. J., & Mao, Y. (2015) · Current Genetics · doi:10.1007/s00294-015-0521-y · Cited by 4

The Legionella pneumophila Chaperonin 60 and the Art of Keeping Several Moonlighting Jobs

Garduño, R. A., & Chong, A. (2013) · Heat shock proteins · doi:10.1007/978-94-007-6787-4_9 · Cited by 4

The hidden dancers in water: the symbiotic mystery of Legionella pneumophila and free-living amoebae

Wang, Y., Jiang, L., Zhou, F., Zhang, Y., Fine, R. D., & Li, M. (2025) · Frontiers in Microbiology · doi:10.3389/fmicb.2025.1634806 · Cited by 3

Regulation of ribosome hibernation controls Legionella survival, infection, antibiotic tolerance, and phenotypic heterogeneity

Schmid, C., Trinkler, S. N., Vittori, E., Oborská‐Oplová, M., Panse, V. G., & Hilbi, H. (2026) · mBio · doi:10.1128/mbio.03762-25 · Cited by 4

Rapid Icm/Dot T4SS Inactivation Prevents Resuscitation of Heat‐Induced VBNC Legionella pneumophila by Amoebae

Schmid, C., & Hilbi, H. (2025) · Environmental Microbiology · doi:10.1111/1462-2920.70035 · Cited by 3

Defective lysosome maturation and Legionella pneumophila replication in Dictyostelium ArfGAP ACAP-A mutant cells

Baïlo, N., Cosson, P., Charette, S. J., Paquet, V. E., Doublet, P., & Letourneur, F. (2014) · Journal of Cell Science · doi:10.1242/jcs.154559 · Cited by 3

Quantitative Imaging Flow Cytometry of Legionella-Containing Vacuoles in Dually Fluorescence-Labeled Dictyostelium

Welin, A., Weber, S., & Hilbi, H. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9048-1_10 · Cited by 3

Survival strategies of intracellular bacterial pathogens

Vázquez-Boland, J. A., Cain, R. J., Strugnell, R. A., Newton, H. J., & Kupz, A. (2024) · Elsevier eBooks · doi:10.1016/b978-0-12-818619-0.00105-2 · Cited by 3

Methods for Determining Protein Translocation by the Legionella pneumophila Dot/Icm Type IV Secretion System

Zhu, W., & Luo, Z. (2012) · Methods in molecular biology · doi:10.1007/978-1-62703-161-5_19 · Cited by 3

A Role for Phosphoinositide Metabolism in Phagocytosis and Intracellular Replication ofLegionella pneumophila

Weber, S. S., Ragaz, C., Reus, K., & Hilbi, H. (2014) · ASM Press eBooks · doi:10.1128/9781555815660.ch71 · Cited by 3

Deciphering Legionella effector delivery by Icm/Dot secretion system reveals a new role for c-diGMP signalingPreprint

Allombert, J., Jaboulay, C., Michard, C., Andréa, C., Charpentier, X., Vianney, A., & Doublet, P. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/754762 · Cited by 3

Overexpression of ORP1C gene increases the rice resistance to Xanthomonas oryzae pv. oryzae through negatively regulating transcription activator-like effectors translocation

Ji, H., Zhou, L., Yang, R., Xu, M., Qian, H., Tong, J., & Sun, M. (2024) · Plant Signaling & Behavior · doi:10.1080/15592324.2024.2441864 · Cited by 2

An effector of phosphatidylinositol 3-kinase activity promotes Rickettsia rickettsii virulence by enhancing autophagy

Huang, D. Y., Ouyang, X., Peng, Z., Chen, D., Song, L., & Luo, Z. (2025) · mBio · doi:10.1128/mbio.02284-25 · Cited by 2

More than just membranes: membrane contact sites as crossroads for infections

Bonde, B., & Herhaus, L. (2025) · Trends in Microbiology · doi:10.1016/j.tim.2025.12.001 · Cited by 2

Bacterial pathogenesis: Legionella phosphoinositide tailoring

Hartland, E. L. (2017) · Nature Microbiology · doi:10.1038/nmicrobiol.2017.13 · Cited by 2

Legionella pneumophila Infection of Human Macrophages Retains Golgi Structure but Reduces O-Glycans

Fu, Y., Macwan, V. J., Heineman, R. E.-S., Terebiznik, M. R., & Harrison, R. E. (2022) · Pathogens · doi:10.3390/pathogens11080908 · Cited by 2

Tools and mechanisms of vacuolar escape leading to host egress in Legionella pneumophila infection: Emphasis on bacterial phospholipases

Neuber, J., Lang, C., Auraß, P., & Flieger, A. (2023) · Molecular Microbiology · doi:10.1111/mmi.15183 · Cited by 3

Microbial genotoxin-elicited host DNA mutations related to mitochondrial dysfunction, a momentous contributor for colorectal carcinogenesis

Xue, Y., Gan, Y., Zhang, Y., Liu, Z., Geng, J., & Wang, W. (2024) · mSystems · doi:10.1128/msystems.00887-24 · Cited by 2

Inter-kingdom signaling by the Legionella autoinducer LAI-1 involves the antimicrobial guanylate binding protein GBP

Solger, F., Rauch, J., Vormittag, S., Fan, M., Raykov, L., Charki, P., Katic, A., Letourneur, F., Soldati, T., Seibel, J., et al. (2025) · PLoS Pathogens · doi:10.1371/journal.ppat.1013026 · Cited by 2

Identification of Lipid-Binding Effectors

Kale, S. D., & Tyler, B. M. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-501-5_24 · Cited by 2

Immunofluorescence Imaging of Legionella Infection In Vitro

Weber, S. S., & Oxenius, A. (2012) · Methods in molecular biology · doi:10.1007/978-1-62703-161-5_16 · Cited by 2

Survival Strategies of Intracellular Bacterial Pathogens

Cain, R. J., & Vázquez‐Boland, J. A. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-397169-2.00028-7 · Cited by 2

Hostile Takeover: Hijacking of Endoplasmic Reticulum Function by T4SS and T3SS Effectors Creates a Niche for Intracellular Pathogens

Tsai, A. Y., English, B. C., & Tsolis, R. M. (2019) · ASM Press eBooks · doi:10.1128/9781683670285.ch23 · Cited by 2

Dictyostelium discoideum: a Model Phagocyte and a Model for Host-Pathogen Interactions

Li, Z., & Isberg, R. R. (2014) · ASM Press eBooks · doi:10.1128/9781555816650.ch32 · Cited by 2

Solution structure of the phosphatidylinositol 3-phosphate binding domain from the Legionella effector SetAPreprint

Beck, W. H. J., Enoki, T. A., Wu, X., Zhang, Q., Nicholson, L. K., Oswald, R. E., & Mao, Y. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.02.13.480292 · Cited by 2

Legionella pneumophila

Swart, A. L., & Hilbi, H. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.11624-1 · Cited by 2

The Legionella effector RidL binds the large fission GTPase Drp1 to promote mitochondrial fragmentation

Katic, A., Vittori, E., Halter, S., Steiner, K., Swart, A. L., Radiom, M., García-Rodríguez, F. J., Jaggi, T., Li, X., Mears, J. A., et al. (2026) · EMBO Reports · doi:10.1038/s44319-026-00823-3 · Cited by 1

Potential roles of the chaperonin (HtpB), polyamines, and the polyamine binding protein (PotD) in Legionella pneumophila pathogenesis

Nasrallah, G. K. (2011) · Library and Archives Canada (Government of Canada) · Cited by 1

Imaging Flow Cytometry of Legionella-Containing Vacuoles in Intact and Homogenized Wild-Type and Mutant Dictyostelium

Welin, A., Hüsler, D., & Hilbi, H. (2023) · Methods in molecular biology · doi:10.1007/978-1-0716-3020-4_4 · Cited by 1

Bacterial intracellular pathogens: Offense and defense strategies

Розов, С. М., & Дейнеко, Е. В. (2016) · Biology Bulletin Reviews · doi:10.1134/s2079086416020067 · Cited by 1

Chemical Inhibitors of Phosphatidylinositol Transfer Proteins Enable Highly Selective Interference With Specific Pathways of Phosphoinositide Signaling in Cells

Nile, A. H. (2019) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/xdt3-hc64 · Cited by 1

The Dot/Icm Type IVB Secretion System

LeBlanc, J. J., & Vogel, J. P. (2007) · Springer eBooks · doi:10.1007/978-0-387-70896-6_3 · Cited by 1

Legionella Pneumophila

Ingmundson, A., & Roy, C. R. (2009) · Wiley eBooks · doi:10.1002/9783527629176.ch18 · Cited by 1

Correction: Legionella pneumophila Secretes a Mitochondrial Carrier Protein during Infection

Doležal, P., Aili, M., Tong, J., Jiang, J., Marobbio, C. M. T., Lee, S. F., Schuelein, R., Belluzzo, S., Bínová, E., Mousnier, A., et al. (2012) · PLoS Pathogens · doi:10.1371/annotation/ee7c807b-032c-4d1f-b5ac-0f6620a2ef24 · Cited by 1

Mechanisms and Applications of RecA-independent recombination in Legionella pneumophila.

Bryan, A. B. (2013) · Deep Blue (University of Michigan)

Genome Plasticity inLegionella pneumophilaandLegionella longbeachae: Impact on Host Cell Exploitation

Gómez-Valero, L., Rusniok, C., & Buchrieser, C. (2014) · ASM Press eBooks · doi:10.1128/9781555817213.ch5

Cellular Model Systems Used to Study Phagosome Biogenesis

Steinert, M. (2009) · Wiley eBooks · doi:10.1002/9783527629176.ch4

Two Important Bacterial Pathogens Causing Community Acquired Pneumonia:Streptococcus pneumoniaeandLegionella pneumophila

Henriques‐Normark, B., & Buchrieser, C. (2010) · Wiley eBooks · doi:10.1002/9783527629664.ch6

Identification of a Cytotoxic Legionella pneumophila LpxB Paralogue in a Multicopy Suppressor Screen using Acanthamoeba castellanii as a Selective Host

Albers, U., Reus, K., & Hilbi, H. (2014) · ASM Press eBooks · doi:10.1128/9781555815660.ch51

Exploiting the host

Amoils, S. (2006) · Nature Reviews Microbiology · doi:10.1038/nrmicro1451

Identification and characterisation of novel Legionella pneumophila virulence genes

Vogrin, A. J. (2015) · Minerva Access (University of Melbourne)

Modulation of host polyubiquitination by the ankb f-box protein of Legionella pneumophila.

Bruckert, W. M. (2014) · doi:10.18297/etd/1724

Legionella pneumophila multiplication is enhanced by chronic AMPK signalling in mitochondrially diseased Dictyostelium cells

Francione, L. M., Smith, P. K., Accari, S. L., Taylor, P. E., Bokko, P. B., Bozzaro, S., Beech, P. L., & Fisher, P. R. (2009) · Disease Models & Mechanisms · doi:10.1242/dmm.004275

Identification of Anti‐infective Compounds Using Amoebae

Harrison, C. F., & Hilbi, H. (2016) · Wiley eBooks · doi:10.1002/9783527682386.ch8

The influence of cell-free Lactobacillus rhamnosus GG conditioned medium on macrophage functional activity

Nanjundaiah, Y. S. (2016)

Intracellular Growth of Bacterial Pathogens: The Role of Secreted Effector Proteins in the Control of Phagocytosed Microorganisms

Poirier, V., & Av‐Gay, Y. (2016) · ASM Press eBooks · doi:10.1128/9781555819286.ch24

Correction: Legionella Eukaryotic-Like Type IV Substrates Interfere with Organelle Trafficking

de Felipe, K. S., Glover, R. T., Charpentier, X., Anderson, O. R., Reyes, M., Pericone, C. D., & Shuman, H. A. (2010) · PLoS Pathogens · doi:10.1371/annotation/f079872b-7bce-41fe-bc16-c2e45d44b19e

Lysosomal evasion of legionella pneumophilia the effector.

Vaughn, B. (2022) · doi:10.18297/etd/3833

A Legionella pneumophila T4SS effector protein (Ravl) triggers mitochondrial fragmentation through phosphoinositide phosphatase activity

Zhang, R., Zhang, M., Li, X., Lu, Z., Chen, S., Du, Y., Chesterman, C. C., van Staalduinen, L., Wang, Y., Pei, H., et al. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.148613

The Legionella phosphocholinase AnkX modulates IMPDH2 regulation and cytoophidia dynamicsPreprint

Stauffer, P., Kaspers, M. S., Swart, A. L., Ochtrop, P., Siebels, B., Pogenberg, V., Otero, D. F., Brockmeyer, A., Schmid, C., Janning, P., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.26.701698

Localization of the PelC and PelE effectors to the Legionella -containing vacuole through host-mediated prenylation and their role in intracellular proliferation

Shin, C. J., Price, C. T. D., Da'as, M. S. J., & Kwaik, Y. A. (2026) · Infection and Immunity · doi:10.1128/iai.00605-25

Étude de la prolifération d'Acanthamoeba castellanii suite à l'infection par Legionella pneumophila

Mengue, L. (2017) · doi:10.70675/df922d30zee1fz461fza8eazf3afa8c425ec

Biochimie structurale de la régulation des petites GTPases à la surface des membranes

Dubois, P. (2023) · theses.fr (ABES) · doi:10.70675/a1d247bdz8c78z46ecz83faz8fbc9f6736a0

Single-cell metabolomics reveals infection-specific metabolic reprogramming of human macrophagesPreprint

Martínez-Oca, P., Meng, A., Vanbellingen, Q., Albert, M., Thomas, A., Bomme, P., García-Rodríguez, F. J., COSIPOP study group, Tinévez, J.-Y., Aros-Calt, S., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.09.03.749052

Multi-Dot/Icm effector mutants reveal distinct host responses in Legionella infected macrophages

Wibawa, R., Li, P., Gearing, L. J., Pidot, S. J., Faidiuk, Y., Wong, W., Ng, G. Z., McCaffrey, K., Hertzog, P. J., Pasricha, S., et al. (2026) · PLoS Pathogens · doi:10.1371/journal.ppat.1014083

PIrates of the vacuole: phosphoinositide hijacking by T4SS intracellular pathogens

Bonazzi, M. (2026) · microLife · doi:10.1093/femsml/uqag032

Modulation of phosphoinositide metabolism by intracellular pathogenic bacteria Listeria monocytogenes

Wang, J. (2012) · Research Explorer (The University of Manchester)

A Role for Phosphoinositide Metabolism in Phagocytosis and Intracellular Replication ofLegionella pneumophila

Weber, S. S., Ragaz, C., Reus, K., & Hilbi, H. (2014) · ASM Press eBooks · doi:10.1128/9781555815660.ch71 · Cited by 3

Anchors for Effectors: Subversion of Phosphoinositide Lipids by Legionella

Hilbi, H., Weber, S., & Finsel, I. (2011) · Frontiers in Microbiology · doi:10.3389/fmicb.2011.00091 · Cited by 88

Live-Cell Imaging of Phosphoinositide Dynamics and Membrane Architecture during Legionella Infection

Weber, S., Wagner, M. A., & Hilbi, H. (2014) · mBio · doi:10.1128/mbio.00839-13 · Cited by 110

Phosphoinositides and the Fate of Legionella in Phagocytes

Swart, A. L., & Hilbi, H. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00025 · Cited by 58

The Machinery at Endoplasmic Reticulum-Plasma Membrane Contact Sites Contributes to Spatial Regulation of Multiple Legionella Effector Proteins

Hubber, A. M., Arasaki, K., Nakatsu, F., Hardiman, C. A., Lambright, D. G., Camilli, P. V. D., Nagai, H., & Roy, C. R. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1004222 · Cited by 76