Publications

Publications authored by the PI of TCML – Arto Pulliainen:

current preprints:

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.
bioRxiv (2024)
https://doi.org/10.1101/2024.01.12.575356

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.
Research Square (2023)
https://doi.org/10.21203/rs.3.rs-3619162/v1

2024

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

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