Publications
Publications authored by the PI of TCML – Arto Pulliainen:
current preprints:
Pathogenic taxa constitute a substantial portion of bat and wild bird fecal bacterial microbiota.
Poosakkannu, A., Xu, Y., Suominen, K.M., Meierhofer, M., Sorensen, I.H., Madsen, J.J., Plaquin, B., Guillemain, E., Joyeux, E., Keiss, O., Lilley, T.M., Lehikoinen, A., and Pulliainen, A.T.
https://doi.org/10.21203/rs.3.rs-3619162/v1
2024
ADP-ribosyltransferase-based biocatalysis of non-hydrolyzable NAD+ analogs.
Sakari, M., Bhadane, R., Kumar, S., Azevedo, R., Malakoutikhahh, M., Masoumi, A., Littler, D.R., Härmä, H., Kopra, K., and Pulliainen, A.T.
Journal of Biological Chemistry (in press)
https://doi.org/10.1016/j.jbc.2024.108106
Alpha1-antitrypsin inhibits pertussis toxin.
Lietz, S., Sommer, A., Sokolowski, L-M, Kling, C., Alpizar, D., King, J., Streit, L., Schröppel, B., van Erp, R., Barth, E., Schneider, M., Münch, J., Michaelis, J., Rodriguez Alfonso, A.A., Ständker, L., Wiese, S., Barth, H., Pulliainen, A.T., Scanlon, K., and Ernst, K.
Journal of Biological Chemistry 300(12):101892 (2024)
https://doi.org/10.1016/j.jbc.2024.107950
Body-wide genetic deficiency of poly(ADP-ribose) polymerase 14 sensitizes mice to colitis.
Vedantham, M., Polari, L., Poosakkannu, A., Pinto, R., Sakari, M., Laine, J., Sipilä, P., Määttä, J., Gerke, H., Rissanen, T., Rantakari, P., Toivola, D., and Pulliainen, A.T.
FASEB Journal 38:e23775 (2024)
https://doi.org/10.1096/fj.202400484R
The chaperonin TRiC/CCT inhibitor HSF1A protects cells from intoxication with pertussis toxin.
Jia, J., Zoeschg, M., Barth, H., Pulliainen, A.T., and Ernst, K.
Toxins 16:36 (cover publication of the issue) (2024)
https://doi.org/10.3390/toxins16010036
Reference genome for the Northern bat (Eptesicus nilssonii), a most northern bat species.
Laine, V.N., Pulliainen, A.T., and Lilley, T.M.
Journal of Heredity 115:149-154 (2024)
https://doi.org/10.1093/jhered/esad056
Slow-lived birds and bats carry higher pathogen loads.
Xu, Y., Laine, V.N., Meramo, K., Santangeli, A., Poosakkannu, A., Suominen, K.M., Gaultier, S., Keller, V., Brotons, L., Pulliainen, A.T., Lilley, T.L., and Lehikoinen, A.
One Earth 7:1121-1132 (2024)
https://doi.org/10.1016/j.oneear.2024.04.021
2023
Domperidone inhibits Clostridium botulinum C2 toxin and Bordetella pertussis toxin.
Jia, J., Braune-Yan, M., Lietz, S., Wahba, M., Pulliainen, A.T., Barth, H., and Ernst, K.
Toxins 15:412 (2023)
https://doi.org/10.3390/toxins15070412
DNA nanoflower eye drops with antibiotic-resistant gene regulation ability for MRSA keratitis target treatment.
Ran, M., Sun, R., Yan, J., Pulliainen, A.T., Zhang, Y., and Zhang, H.
Small 19:2304194 (2023)
https://doi.org/10.1002/smll.202304194
Continental-scale climatic gradients of pathogenic microbial taxa in birds and bats.
Xu, Y., Poosakkannu, A., Suominen, K.M., Laine, V.N., Lilley, T.M., Pulliainen, A.T., and Lehikoinen, A.
Ecography e06783 (2023)
https://doi.org/10.1111/ecog.06783
Inhibition of pertussis toxin by human α-defensins-1 and -5: differential mechanisms of action.
Kling, C., Sommer, A., Almeida-Hernandez, Y., Rodriguez, A., Perez-Erviti, J.A., Bhadane, R., Ständker, L., Wiese, S., Barth, H., Pupo-Merino, M., Pulliainen, A.T., Sanchez-Garcia, E., and Ernst, K.
International Journal of Molecular Sciences 24:10557 (2023)
https://doi.org/10.3390/ijms241310557
2022
Crystal structures of pertussis toxin with NAD+ and analogs provide structural insights into the mechanism of its cytosolic ADP-ribosylation activity.
Sakari, M., Tran, M.T., Rossjohn, J., Pulliainen, A.T.*, Beddoe, T.*, and Littler, D*. (2022)
*shared senior authorship (Editor’s pick – paper of the week)
Journal of Biological Chemistry 298(5):101892
https://doi.org/10.1016/j.jbc.2022.101892
Exotoxin-targeted drug modalities as antibiotic alternatives.
Sakari, M., Laisi, A., and Pulliainen, A.T.
ACS Infectious Diseases 8:433-456 (2022)
https://doi.org/10.1021/acsinfecdis.1c00296
2021
Human peptides α-defensin-1 and -5 inhibit pertussis toxin.
Kling, K., Pulliainen, A.T., Barth, H., and Ernst, K.
Toxins 13:480 (2021)
https://doi.org/10.3390/toxins13070480
Pharmacological targeting of host chaperones protects from pertussis toxin in vitro and in vivo.
Ernst, K., Mittler, A.-K., Kling, C., Winkelmann, V., Eberhardt, N., Anastasia, A., Sonnabend, M., Lochbaum, R., Wirsching, J., Sakari, M., Pulliainen, A.T., Skerry, C., Carbonetti, N.-H., Frick, M., and Barth, H.
Scientific Reports 11:5429 (2021)
https://doi.org/10.1038/s41598-021-84817-2
2020
iGIST – a kinetic bioassay for pertussis toxin based on its effect on inhibitory GPCR signaling.
Paramonov, V.M., Sahlgren, C., Rivero-Müller, A., and Pulliainen, A.T.
ACS Sensors 5:3438-3448 (2020)
https://doi.org/10.1021/acssensors.0c01340
Single-peptide TR-FRET detection platform for cysteine-specific post-translational modifications.
Eskonen, V., Tong-Ochoa, N., Mattsson, L., Miettinen, M., Lastusaari, M., Pulliainen, A.T., Kopra, K., and Härmä H.
Analytical Chemistry 92:13202-13210 (2020)
https://doi.org/10.1021/acs.analchem.0c02370
The guanine nucleotide exchange factor VAV3 participates in ERBB4-mediated cancer cell migration.
Ojala, V.K., Knittle, A.M., Kirjalainen, P., Merilahti, J.A.M., Kortesoja, M., Tvorogov, D., Vaparanta, K., Lin, S., Kast, J., Pulliainen, A.T., Kurppa, K.J., and Elenius, K.
Journal of Biological Chemistry 295:11559-11571 (2020)
https://doi.org/10.1074/jbc.RA119.010925
Discovery of compounds inhibiting the ADP-ribosyltransferase activity of pertussis toxin.
Ashok, Y., Miettinen, M, De Oliveira, D.K.H., Tamirat, M.Z., Näreoja, K., Tiwari, A., Hottiger, M.O., Johnson, M.S., Lehtiö, L. and Pulliainen, A.T.
ACS Infectious Diseases 6:588-602 (2020)
https://doi.org/10.1021/acsinfecdis.9b00412
Homogeneous dual-parametric coupled assay for simultaneous nucleotide exchange and KRAS/RAF-RBD interaction monitoring.
Kopra, K., Vuorinen, E., Abreu-Blanco, M., Wang, Q., Eskonen, V., Gillette, W., Pulliainen, A.T., Holderfield, M., and Härmä H.
Analytical Chemistry 92:4971-4979 (2020)
https://doi.org/10.1021/acs.analchem.9b05126
2019
Host poly(ADP-ribose) polymerases (PARPs) in acute and chronic bacterial infections.
Miettinen, M., Vedantham, M., and Pulliainen, A.T.
Microbes and Infection 21:423-431 (review) (2019)
https://doi.org/10.1016/j.micinf.2019.06.002
Combination of microbiome analysis and serodiagnostics to assess the risk of pathogen transmission by ticks to humans and animals in central Germany.
Regier, Y., Komma, K., Weigel, M., Kraiczy, P., Laisi, A., Pulliainen, A.T., Hain, T., and Kempf, V.A.J.
Parasites & Vectors 12:11 (2019)
https://doi.org/10.1186/s13071-018-3240-7
2018
Galectin-3-binding protein – a multitask glycoprotein with innate immunity functions in viral and bacterial infections.
Loimaranta, V., Hepojoki, J., Laaksoaho, O., and Pulliainen, A.T.
Journal of Leukocyte Biology 104:777-786 (review) (2018)
https://doi.org/10.1002/JLB.3VMR0118-036R
Different responses of colorectal cancer cells to alternative sequences of cetuximab and oxaliplatin.
Narvi, E., Vaparanta, K., Karrila, A., Chakroborty, D., Knuutila, S., Pulliainen, A.T., Sundvall, M. and Elenius, K.
Scientific Reports 8:16759 (2018)
https://doi.org/10.1038/s41598-018-34938-y
Microbiome analysis reveals the presence of Bartonella spp. and Acinetobacter spp. in deer keds (Lipoptena cervi).
Regier, Y., Komma, K., Weigel, M., Pulliainen, A.T., Goettig, S., Hain, T., and Kempf, V.A.J.
Frontiers in Microbiology 9:3100 (2018)
https://doi.org/10.3389/fmicb.2018.03100
2017
Molecular detection of Candidatus Bartonella mayotimonensis in North American bats.
Lilley, T.M., Wilson, C.A., Bernard, R.F., Willcox, E.V., Vesterinen, E.J., Webber, Q.M.R., Kurpiers, L., Prokkola, J.M., Ejotre, I., Kurta, A., Field, K.A., Reeder, D.M., and Pulliainen, A.T.
Vector Borne and Zoonotic Diseases 17:243-246 (2017)
https://doi.org/10.1089/vbz.2016.2080
Genome-wide screen of gamma-secretase-mediated intraembrane cleavage of receptor tyrosine kinases.
Merilahti, J.A.M., Ohaja, V.K., Knittle, A.M., Pulliainen, A.T., and Elenius, K.
Molecular Biology of the Cell 28:777-786 (2017)
https://doi.org/10.1091/mbc.e17-04-0261
Molecular evidence of Chlamydia-like organisms in the feces of Myotis daubentonii bats.
Hokynar, K., Vesterinen, E.J., Lilley, T.M., Pulliainen, A.T., Korhonen, S.J., Paavonen, J., and Puolakkainen, M.
Applied and Environmental Microbiology 2:e02951-16 (2017)
https://doi.org/10.1128/AEM.02951-16
2015
Structural insight into how bacteria prevent interference between multiple divergent type IV secretion systems.
Gillespie, J.J., Phan, I.Q.H., Scheib, H., Subramanian, S., Edwards, T.E, Lehman, S.S., Piitulainen, H., Rahman, M.S., Rennoll-Bankert, K.E., Staker, B.L., Taira, S., Stacy, R., Myler, P.J., Azad, A.F., and Pulliainen, A.T.
mBio 6:e01867-15 (2015)
https://doi.org/10.1128/mbio.01867-15
Molecular detection of Candidatus Bartonella hemsundetiensis in bats.
Lilley, T.M., Veikkolainen, V., and Pulliainen, A.T.
Vector Borne and Zoonotic Diseases 15:706-708 (2015)
https://doi.org/10.1089/vbz.2015.1783
Molecular detection of Bartonella spp. in deer ked pupae, adult keds and moose blood in Finland.
Korhonen, E., Pérez Vera, C., Pulliainen, A.T., Sironen, T., Aaltonen, K., Kortet, R., Härkönen, L., Härkönen, S., Paakkonen, T., Nieminen, P., Mustonen, A., Ylönen, H., and Vapalahti, O.
Epidemiology and Infection 143:578-585 (2015)
https://doi.org/10.1017/S0950268814001411
2014
Bats as reservoir hosts of human bacterial pathogen, Bartonella mayotimonensis.
Veikkolainen, V., Vesterinen, E.J., Lilley, T.M., and Pulliainen, A.T.
Emerging Infectious Diseases 20:960-967 (2014)
https://doi.org/10.3201/eid2006.130956
2013
Cat scratch disease caused by Bartonella grahamii in an immunocompromised patient.
Oksi, J., Rantala, S., Kilpinen, S., Silvennoinen, R., Vornanen, M., Veikkolainen, V., Eerola, E., and Pulliainen, A.T.
Journal of Clinical Microbiology 51:2781-2784 (2013)
https://doi.org/10.1128/jcm.00910-13
2012
Bacterial effector binds host cell adenylyl cyclase to potentiate Gs-dependent cAMP production.
Pulliainen, A.T., Piels, K., Brand, C., Hauert, B., Böhm, A., Quebatte, M., Wepf, A., Gstaiger, M., Aebersold, R., Dessauer, C., and Dehio, C.
Proceedings of the National Academy of Sciences USA 109:9581-9586 (2012)
https://doi.org/10.1073/pnas.1117651109
Systemic analysis of gene expression profiles identifies ErbB3 as a potential drug target in pediatric alveolar rhabdomyosarcoma.
Nordberg, J., Mpindi, J.P., Iljin, K., Pulliainen, A.T., Kallajoki, M., Kallioniemi, O., Elenius, K. and Elenius, V.
PLoS ONE 7(12):e50819 (2012)
https://doi.org/10.1371/journal.pone.0050819
Persistence of Bartonella spp. stealth pathogens: from sub-clinical infections to vasoproliferative tumor formation.
Pulliainen, A.T., and Dehio, C.
FEMS Microbiology Reviews 36:563-599 (review) (2012)
https://doi.org/10.1111/j.1574-6976.2012.00324.x
2011
Identification of a novel streptococcal adhesin P (SadP) protein recognizing galactosyl-α1-4-galactose-containing glycoconjugates
Kouki, A., Haataja, S., Loimaranta, V., Pulliainen, A.T., Nilsson, U.J., and Finne, J.
Journal of Biological Chemistry 286:38854-38864 (2011)
https://doi.org/10.1074/jbc.M111.260992
2009
Leucine rich repeats of bacterial surface proteins serve as common pattern recognition motifs of human scavenger receptor Gp340.
Loimaranta, V., Hytönen, J., Pulliainen A.T., Sharma, A., Tenovuo, J., Strömberg, N., and Finne, J.
Journal of Biological Chemistry 284: 18614-18623 (2009)
https://doi.org/10.1074/jbc.M900581200
Bartonella henselae: Subversion of vascular endothelial cell functions by translocated bacterial effector proteins.
Pulliainen, A.T., and Dehio, C.
International Journal of Biochemistry & Cell Biology 41:507-510 (review) (2009)
https://doi.org/10.1016/j.biocel.2008.10.018
2008
Structural basis of the zinc- and terbium-mediated inhibition of ferroxidase activity in Dps ferritin-like proteins.
Havukainen, H., Haataja, S., Kauko, A., Pulliainen, A.T., Salminen, A., Haikarainen, T., Finne, J., and Papageorgiou, A.C.
Protein Science 17:1513-1521 (2008)
https://doi.org/10.1110/ps.036236.108
Deficiency of the Rgg regulator promotes H2O2resistance, AhpCF-mediated H2O2 decomposition, and virulence in Streptococcus pyogenes.
Pulliainen, A.T., Hytönen, J., Haataja, S., and Finne, J.
Journal of Bacteriology 190:3225-3235 (2008)
https://doi.org/10.1128/jb.01843-07
2007
Fighting infectious diseases with technology and knowledge-transfer.
Pulliainen, A.T., Enninga, J., Fernandez-Arenas, E., and Griffiths, G.
EMBO Reports 8: 117-120 (2007)
https://doi.org/10.1038/sj.embor.740090
2006
Iron incorporation in Streptococcus suis Dps-like peroxide resistance protein Dpr requires mobility in the ferroxidase center and leads to the formation of a ferrihydrite-like core.
Kauko, A., Pulliainen, A.T., Haataja, S., Meyer-Klaucke, W., Finne, J., and Papageorgiou, A.C.
Journal of Molecular Biology 364: 97-109 (2006)
https://doi.org/10.1016/j.jmb.2006.08.061
2005
Dps/Dpr ferritin-like protein: insights into the mechanism of iron incorporation and evidence for a central role in cellular iron homeostasis in Streptococcus suis.
Pulliainen, A.T., Kauko, A., Haataja, S., Papageorgiou, A.C., and Finne, J.
Molecular Microbiology 57: 1086-1101 (cover publication of the issue) (2005)
https://doi.org/10.1111/j.1365-2958.2005.04756.x
Generation of transposon insertion mutant libraries for Gram-positive bacteria by electroporation of phage Mu DNA transposition complexes.
Pajunen, M.I., Pulliainen, A.T., Finne, J., and Savilahti, H.
Microbiology 151:1209-1218 (2005)
https://doi.org/10.1099/mic.0.27807-0
2004
Crystal structure of Streptococcus suis Dps-like peroxide resistance protein Dpr: implications for iron incorporation.
Kauko, A., Haataja, S., Pulliainen, A.T., Finne, J., and Papageorgiou, A.C.
Journal of Molecular Biology 338:547-558 (2004)
https://doi.org/10.1016/j.jmb.2004.03.009
2003
Molecular basis of H2O2 resistance mediated by streptococcal Dpr.
Pulliainen, A.T., Haataja, S., Kähkönen, S., & Finne, J.
Journal of Biological Chemistry 278:7996–8005 (2003)
https://doi.org/10.1074/jbc.M210174200
2002
Expression, purification and crystallization of Dpr, a ferritin-like protein from the gram-positive meningitis associated bacterium Streptococcus suis.
Haataja, S. Penttinen, A., Pulliainen, A.T., Tikkanen, K., Finne, J., and Papageorgiou, A.C.
Acta Crystallographica, Section D, Biological Crystallography 58:1851-1853 (2002)
https://doi.org/10.1107/S0907444902012970