Evidence that immunization with TP0751, a bipartite Treponema pallidum lipoprotein with an intrinsically disordered region and lipocalin fold, fails to protect in the rabbit model of experimental syphilis

Luthra, A; Montezuma-Rusca, J.; La Vake, C.; LeDoyt, M.; Delgado, K.; Davenport, T.; Fiel-Gan, M.; Caimano, M.; Radolf, J.; Hawley, K.

doi:10.1371/journal.ppat.1008871

Title: Evidence that immunization with TP0751, a bipartite Treponema pallidum lipoprotein with an intrinsically disordered region and lipocalin fold, fails to protect in the rabbit model of experimental syphilis

Journal Article · 01 January 2022 · PLoS Pathogens

DOI:https://doi.org/10.1371/journal.ppat.1008871· OSTI ID:1690189

Luthra, A; Montezuma-Rusca, J.; La Vake, C.; LeDoyt, M.; Delgado, K.; Davenport, T.; Fiel-Gan, M.; Caimano, M.; Radolf, J.; Hawley, K.

Cite

Export

Save

Research Organization:: Brookhaven National Lab. (BNL), Upton, NY (United States)

Sponsoring Organization:: ~OTHER

DOE Contract Number:: SC0012704

OSTI ID:: 1690189

Report Number(s):: BNL-220510-2020-JACI

Journal Information:: PLoS Pathogens, Vol. 16, Issue 9

Country of Publication:: United States

Language:: English

References (121)

Syphilis Hook, Edward W. The Lancet, Vol. 389, Issue 10078 https://doi.org/10.1016/S0140-6736(16)32411-4	journal	April 2017
The immune response to infection with Treponema pallidum, the stealth pathogen Salazar, Juan C.; Hazlett, Karsten R. O.; Radolf, Justin D. Microbes and Infection, Vol. 4, Issue 11 https://doi.org/10.1016/S1286-4579(02)01638-6	journal	September 2002
Syphilis Peeling, Rosanna W.; Mabey, David; Kamb, Mary L. Nature Reviews Disease Primers, Vol. 3, Issue 1 https://doi.org/10.1038/nrdp.2017.73	journal	October 2017
The global roadmap for advancing development of vaccines against sexually transmitted infections: Update and next steps Gottlieb, Sami L.; Deal, Carolyn D.; Giersing, Birgitte Vaccine, Vol. 34, Issue 26 https://doi.org/10.1016/j.vaccine.2016.03.111	journal	June 2016
Vaccine development for syphilis Lithgow, Karen V.; Cameron, Caroline E. Expert Review of Vaccines, Vol. 16, Issue 1 https://doi.org/10.1080/14760584.2016.1203262	journal	July 2016
Scientific Monogamy: Thirty Years Dancing with the Same Bug: 2007 Thomas Parran Award Lecture Lukehart, Sheila A. Sexually Transmitted Diseases, Vol. 35, Issue 1 https://doi.org/10.1097/OLQ.0b013e318162c4f2	journal	January 2008
Immune Evasion and Recognition of the Syphilis Spirochete in Blood and Skin of Secondary Syphilis Patients: Two Immunologically Distinct Compartments Cruz, Adriana R.; Ramirez, Lady G.; Zuluaga, Ana V. PLoS Neglected Tropical Diseases, Vol. 6, Issue 7 https://doi.org/10.1371/journal.pntd.0001717	journal	July 2012
IFNγ Enhances CD64-Potentiated Phagocytosis of Treponema pallidum Opsonized with Human Syphilitic Serum by Human Macrophages Hawley, Kelly L.; Cruz, Adriana R.; Benjamin, Sarah J. Frontiers in Immunology, Vol. 8 https://doi.org/10.3389/fimmu.2017.01227	journal	October 2017
Reduced Treponema pallidum –Specific Opsonic Antibody Activity in HIV-Infected Patients With Syphilis Marra, Christina M.; Tantalo, Lauren C.; Sahi, Sharon K. Journal of Infectious Diseases, Vol. 213, Issue 8 https://doi.org/10.1093/infdis/jiv591	journal	December 2015
Cryo-Electron Tomography Elucidates the Molecular Architecture of Treponema pallidum, the Syphilis Spirochete Izard, Jacques; Renken, Christian; Hsieh, Chyong-Ere Journal of Bacteriology, Vol. 191, Issue 24 https://doi.org/10.1128/JB.01031-09	journal	October 2009
Cellular Architecture of Treponema pallidum: Novel Flagellum, Periplasmic Cone, and Cell Envelope as Revealed by Cryo Electron Tomography Liu, Jun; Howell, Jerrilyn K.; Bradley, Sherille D. Journal of Molecular Biology, Vol. 403, Issue 4 https://doi.org/10.1016/j.jmb.2010.09.020	journal	November 2010
Complete Genome Sequence of Treponema pallidum, the Syphilis Spirochete Fraser, C. M. Science, Vol. 281, Issue 5375 https://doi.org/10.1126/science.281.5375.375	journal	July 1998
Major integral membrane protein immunogens of Treponema pallidum are proteolipids Chamberlain, N. R.; Brandt, M. E.; Erwin, A. L. Infection and Immunity, Vol. 57, Issue 9 https://doi.org/10.1128/IAI.57.9.2872-2877.1989	journal	September 1989
Lipoprotein computational prediction in spirochaetal genomes Setubal, João C.; Reis, Marcelo; Matsunaga, James Microbiology, Vol. 152, Issue 1 https://doi.org/10.1099/mic.0.28317-0	journal	January 2006
Characterization of lipid-modified immunogenic proteins of Treponema pallidum expressed in Escherichia coli Schouls, Leo M.; Mout, Robert; Dekker, Jan Microbial Pathogenesis, Vol. 7, Issue 3 https://doi.org/10.1016/0882-4010(89)90053-3	journal	September 1989
Reactivity of Antibodies from Syphilis Patients to a Protein Array Representing the Treponema pallidum Proteome Brinkman, Mary Beth; McKevitt, Matthew; McLoughlin, Melanie Journal of Clinical Microbiology, Vol. 44, Issue 3 https://doi.org/10.1128/JCM.44.3.888-891.2006	journal	March 2006
Acylation of the 47-kilodalton major membrane immunogen of Treponema pallidum determines its hydrophobicity Chamberlain, N. R.; DeOgny, L.; Slaughter, C. Infection and Immunity, Vol. 57, Issue 9 https://doi.org/10.1128/IAI.57.9.2878-2885.1989	journal	September 1989
The 47-kDa major lipoprotein immunogen of Treponema pallidum is a penicillin-binding protein with carboxypeptidase activity. Weigel, L. M.; Radolf, J. D.; Norgard, M. V. Proceedings of the National Academy of Sciences, Vol. 91, Issue 24 https://doi.org/10.1073/pnas.91.24.11611	journal	November 1994
Crystal Structure of the 47-kDa Lipoprotein of Treponema pallidum Reveals a Novel Penicillin-binding Protein Deka, Ranjit K.; Machius, Mischa; Norgard, Michael V. Journal of Biological Chemistry, Vol. 277, Issue 44 https://doi.org/10.1074/jbc.M207402200	journal	August 2002
The Tp38 (TpMglB-2) Lipoprotein Binds Glucose in a Manner Consistent with Receptor Function in Treponema pallidum Deka, R. K.; Goldberg, M. S.; Hagman, K. E. Journal of Bacteriology, Vol. 186, Issue 8 https://doi.org/10.1128/JB.186.8.2303-2308.2004	journal	April 2004
The PnrA (Tp0319; TmpC) Lipoprotein Represents a New Family of Bacterial Purine Nucleoside Receptor Encoded within an ATP-binding Cassette (ABC)-like Operon in Treponema pallidum Deka, Ranjit K.; Brautigam, Chad A.; Yang, Xiaofeng F. Journal of Biological Chemistry, Vol. 281, Issue 12 https://doi.org/10.1074/jbc.M511405200	journal	January 2006
The general transition metal (Tro) and Zn ²⁺ (Znu) transporters in Treponema pallidum : analysis of metal specificities and expression profiles Desrosiers, Daniel C.; Sun, Yong Cheng; Zaidi, Akbar A. Molecular Microbiology, Vol. 65, Issue 1 https://doi.org/10.1111/j.1365-2958.2007.05771.x	journal	July 2007
Structural and Biochemical Basis for Polyamine Binding to the Tp0655 Lipoprotein of Treponema pallidum: Putative Role for Tp0655 (TpPotD) as a Polyamine Receptor Machius, Mischa; Brautigam, Chad A.; Tomchick, Diana R. Journal of Molecular Biology, Vol. 373, Issue 3 https://doi.org/10.1016/j.jmb.2007.08.018	journal	October 2007
The Tp0684 (MglB-2) Lipoprotein of Treponema pallidum: A Glucose-Binding Protein with Divergent Topology Brautigam, Chad A.; Deka, Ranjit K.; Liu, Wei Z. PLOS ONE, Vol. 11, Issue 8 https://doi.org/10.1371/journal.pone.0161022	journal	August 2016
A Novel Treponema pallidum Antigen, TP0136, Is an Outer Membrane Protein That Binds Human Fibronectin Brinkman, Mary Beth; McGill, Melanie A.; Pettersson, Jonas Infection and Immunity, Vol. 76, Issue 5 https://doi.org/10.1128/IAI.01424-07	journal	March 2008
Treponema pallidum subsp. pallidum TP0136 Protein Is Heterogeneous among Isolates and Binds Cellular and Plasma Fibronectin via its NH2-Terminal End Ke, Wujian; Molini, Barbara J.; Lukehart, Sheila A. PLOS Neglected Tropical Diseases, Vol. 9, Issue 3 https://doi.org/10.1371/journal.pntd.0003662	journal	March 2015
Treponema pallidum Lipoprotein TP0435 Expressed in Borrelia burgdorferi Produces Multiple Surface/Periplasmic Isoforms and mediates Adherence Chan, Kamfai; Nasereddin, Thayer; Alter, Laura Scientific Reports, Vol. 6, Issue 1 https://doi.org/10.1038/srep25593	journal	May 2016
Treponema pallidum in gel microdroplets: a novel strategy for investigation of treponemal molecular architecture Cox, David L.; Akins, Darrin R.; Porcella, Stephen F. Molecular Microbiology, Vol. 15, Issue 6 https://doi.org/10.1111/j.1365-2958.1995.tb02288.x	journal	March 1995
Surface Immunolabeling and Consensus Computational Framework To Identify Candidate Rare Outer Membrane Proteins of Treponema pallidum Cox, David L.; Luthra, Amit; Dunham-Ems, Star Infection and Immunity, Vol. 78, Issue 12 https://doi.org/10.1128/IAI.00834-10	journal	September 2010
Insights into the potential function and membrane organization of the TP0435 (Tp17) lipoprotein from T reponema pallidum derived from structural and biophysical analyses: Disulfide-Linked Dimer of T. pallidum TP0435 Brautigam, Chad A.; Deka, Ranjit K.; Liu, Wei Z. Protein Science, Vol. 24, Issue 1 https://doi.org/10.1002/pro.2576	journal	October 2014
Emerging Roles for NlpE as a Sensor for Lipoprotein Maturation and Transport to the Outer Membrane in Escherichia coli Simpson, Brent W.; Trent, M. Stephen mBio, Vol. 10, Issue 3 https://doi.org/10.1128/mBio.01302-19	journal	June 2019
Defining the Interaction of the Treponema pallidum Adhesin Tp0751 with Laminin Cameron, Caroline E.; Brouwer, Nathan L.; Tisch, Lisa M. Infection and Immunity, Vol. 73, Issue 11 https://doi.org/10.1128/IAI.73.11.7485-7494.2005	journal	November 2005
Bifunctional Role of the Treponema pallidum Extracellular Matrix Binding Adhesin Tp0751 Houston, Simon; Hof, Rebecca; Francescutti, Teresa Infection and Immunity, Vol. 79, Issue 3 https://doi.org/10.1128/IAI.01083-10	journal	March 2011
Activation and Proteolytic Activity of the Treponema pallidum Metalloprotease, Pallilysin Houston, Simon; Hof, Rebecca; Honeyman, Lisa PLoS Pathogens, Vol. 8, Issue 7 https://doi.org/10.1371/journal.ppat.1002822	journal	July 2012
The multifunctional role of the pallilysin-associated T reponema pallidum protein, Tp0750, in promoting fibrinolysis and extracellular matrix component degradation: Host protein interactions mediated by T. pallidum Tp0750 Houston, Simon; Russell, Shannon; Hof, Rebecca Molecular Microbiology, Vol. 91, Issue 3 https://doi.org/10.1111/mmi.12482	journal	January 2014
The Structure of Treponema pallidum Tp0751 (Pallilysin) Reveals a Non-canonical Lipocalin Fold That Mediates Adhesion to Extracellular Matrix Components and Interactions with Host Cells Parker, Michelle L.; Houston, Simon; Pětrošová, Helena PLOS Pathogens, Vol. 12, Issue 9 https://doi.org/10.1371/journal.ppat.1005919	journal	September 2016
Identification of Tp0751 (Pallilysin) as a Treponema pallidum Vascular Adhesin by Heterologous Expression in the Lyme disease Spirochete Kao, Wei-Chien Andrew; Pětrošová, Helena; Ebady, Rhodaba Scientific Reports, Vol. 7, Issue 1 https://doi.org/10.1038/s41598-017-01589-4	journal	May 2017
A defined syphilis vaccine candidate inhibits dissemination of Treponema pallidum subspecies pallidum Lithgow, Karen V.; Hof, Rebecca; Wetherell, Charmaine Nature Communications, Vol. 8, Issue 1 https://doi.org/10.1038/ncomms14273	journal	February 2017
The bacterial lipocalins Bishop, Russell E. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, Vol. 1482, Issue 1-2 https://doi.org/10.1016/S0167-4838(00)00138-2	journal	October 2000
The Menagerie of Human Lipocalins: A Natural Protein Scaffold for Molecular Recognition of Physiological Compounds Schiefner, André; Skerra, Arne Accounts of Chemical Research, Vol. 48, Issue 4 https://doi.org/10.1021/ar5003973	journal	March 2015
YodA from Escherichia coli Is a Metal-binding, Lipocalin-like Protein David, Gabriel; Blondeau, Karine; Schiltz, Marc Journal of Biological Chemistry, Vol. 278, Issue 44 https://doi.org/10.1074/jbc.M304484200	journal	August 2003
Crystal structure of a novel polyisoprenoid-binding protein from Thermus thermophilus HB8 Handa, N. Protein Science, Vol. 14, Issue 4 https://doi.org/10.1110/ps.041183305	journal	March 2005
Neisseria meningitis GNA1030 is a ubiquinone‐8 binding protein Donnarumma, Danilo; Golfieri, Giacomo; Brier, Sébastien The FASEB Journal, Vol. 29, Issue 6 https://doi.org/10.1096/fj.14-263954	journal	February 2015
The membrane bound bacterial lipocalin Blc is a functional dimer with binding preference for lysophospholipids Campanacci, Valérie; Bishop, Russell E.; Blangy, Stéphanie FEBS Letters, Vol. 580, Issue 20 https://doi.org/10.1016/j.febslet.2006.07.086	journal	August 2006
The Phyre2 web portal for protein modeling, prediction and analysis Kelley, Lawrence A.; Mezulis, Stefans; Yates, Christopher M. Nature Protocols, Vol. 10, Issue 6 https://doi.org/10.1038/nprot.2015.053	journal	May 2015
PrDOS: prediction of disordered protein regions from amino acid sequence Ishida, T.; Kinoshita, K. Nucleic Acids Research, Vol. 35, Issue Web Server https://doi.org/10.1093/nar/gkm363	journal	May 2007
Prediction of protein disorder based on IUPred: Prediction of Protein Disorder Based on IUPred Dosztányi, Zsuzsanna Protein Science, Vol. 27, Issue 1 https://doi.org/10.1002/pro.3334	journal	November 2017
PONDR-FIT: A meta-predictor of intrinsically disordered amino acids Xue, Bin; Dunbrack, Roland L.; Williams, Robert W. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, Vol. 1804, Issue 4 https://doi.org/10.1016/j.bbapap.2010.01.011	journal	April 2010
Normal Mode Flexible Fitting of High-Resolution Structures of Biological Molecules toward SAXS Data Gorba, Christian; Tama, Florence Bioinformatics and Biology Insights, Vol. 4 https://doi.org/10.4137/BBI.S4551	journal	January 2010
Restoring Low Resolution Structure of Biological Macromolecules from Solution Scattering Using Simulated Annealing Svergun, D. I. Biophysical Journal, Vol. 76, Issue 6, p. 2879-2886 https://doi.org/10.1016/S0006-3495(99)77443-6	journal	June 1999
Uniqueness of ab initio shape determination in small-angle scattering Volkov, Vladimir V.; Svergun, Dmitri I. Journal of Applied Crystallography, Vol. 36, Issue 3, p. 860-864 https://doi.org/10.1107/S0021889803000268	journal	April 2003
Lipocalins – a family portrait Grzyb, Joanna; Latowski, Dariusz; Strzałka, Kazimierz Journal of Plant Physiology, Vol. 163, Issue 9 https://doi.org/10.1016/j.jplph.2005.12.007	journal	September 2006
Role of conserved residues in structure and stability: Tryptophans of human serum retinol-binding protein, a model for the lipocalin superfamily Greene, Lesley H.; Chrysina, Evangelia D.; Irons, Laurence I. Protein Science, Vol. 10, Issue 11 https://doi.org/10.1110/ps.22901	journal	November 2001
The lipocalin protein family: structural and sequence overview Flower, Darren R.; North, Anthony C. T.; Sansom, Clare E. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, Vol. 1482, Issue 1-2 https://doi.org/10.1016/S0167-4838(00)00148-5	journal	October 2000
Identification of common and distinct features of ligand-binding sites in kernel and outlier lipocalins Munussami, Ganapathiraman; Sokalingam, Sriram; Sriramulu, Dinesh Kumar Journal of Industrial and Engineering Chemistry, Vol. 78 https://doi.org/10.1016/j.jiec.2019.05.035	journal	October 2019
Structure-Based Phylogenetic Analysis of the Lipocalin Superfamily Lakshmi, Balasubramanian; Mishra, Madhulika; Srinivasan, Narayanaswamy PLOS ONE, Vol. 10, Issue 8 https://doi.org/10.1371/journal.pone.0135507	journal	August 2015
A Phylogenetic Analysis of the Lipocalin Protein Family Ganfornina, María D.; Gutiérrez, Gabriel; Bastiani, Michael Molecular Biology and Evolution, Vol. 17, Issue 1 https://doi.org/10.1093/oxfordjournals.molbev.a026224	journal	January 2000
Comparison of sequence-based and structure-based phylogenetic trees of homologous proteins: Inferences on protein evolution Balaji, S.; Srinivasan, N. Journal of Biosciences, Vol. 32, Issue 1 https://doi.org/10.1007/s12038-007-0008-1	journal	January 2007
Structure-Based Phylogeny as a Diagnostic for Functional Characterization of Proteins with a Cupin Fold Agarwal, Garima; Rajavel, Malligarjunan; Gopal, Balasubramanian PLoS ONE, Vol. 4, Issue 5 https://doi.org/10.1371/journal.pone.0005736	journal	May 2009
Dali server: conservation mapping in 3D Holm, Liisa; Rosenstrï¿½m, Pï¿½ivi Nucleic Acids Research, Vol. 38, Issue suppl_2 https://doi.org/10.1093/nar/gkq366	journal	May 2010
Structural Studies of the Cpx Pathway Activator NlpE on the Outer Membrane of Escherichia coli Hirano, Yu; Hossain, Md. Motarab; Takeda, Kazuki Structure, Vol. 15, Issue 8 https://doi.org/10.1016/j.str.2007.06.014	journal	August 2007
NMR Structure of Lipoprotein YxeF from Bacillus subtilis Reveals a Calycin Fold and Distant Homology with the Lipocalin Blc from Escherichia coli Wu, Yibing; Punta, Marco; Xiao, Rong PLoS ONE, Vol. 7, Issue 6 https://doi.org/10.1371/journal.pone.0037404	journal	June 2012
Identification of the Neuroinvasive Pathogen Host Target, LamR, as an Endothelial Receptor for the Treponema pallidum Adhesin Tp0751 Lithgow, Karen V.; Church, Brigette; Gomez, Alloysius mSphere, Vol. 5, Issue 2 https://doi.org/10.1128/mSphere.00195-20	journal	April 2020
The ligands of neutrophil gelatinase-associated lipocalin Bao, Guan-Hu; Ho, Chi-Tang; Barasch, Jonathan RSC Advances, Vol. 5, Issue 126 https://doi.org/10.1039/C5RA18736B	journal	January 2015
The Neutrophil Lipocalin NGAL Is a Bacteriostatic Agent that Interferes with Siderophore-Mediated Iron Acquisition Goetz, David H.; Holmes, Margaret A.; Borregaard, Niels Molecular Cell, Vol. 10, Issue 5 https://doi.org/10.1016/S1097-2765(02)00708-6	journal	November 2002
Protein–ligand binding site recognition using complementary binding-specific substructure comparison and sequence profile alignment Yang, Jianyi; Roy, Ambrish; Zhang, Yang Bioinformatics, Vol. 29, Issue 20 https://doi.org/10.1093/bioinformatics/btt447	journal	August 2013
3DLigandSite: predicting ligand-binding sites using similar structures Wass, Mark N.; Kelley, Lawrence A.; Sternberg, Michael J. E. Nucleic Acids Research, Vol. 38, Issue suppl_2 https://doi.org/10.1093/nar/gkq406	journal	May 2010
CASTp 3.0: computed atlas of surface topography of proteins Tian, Wei; Chen, Chang; Lei, Xue Nucleic Acids Research, Vol. 46, Issue W1 https://doi.org/10.1093/nar/gky473	journal	June 2018
AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility Morris, Garrett M.; Huey, Ruth; Lindstrom, William Journal of Computational Chemistry, Vol. 30, Issue 16 https://doi.org/10.1002/jcc.21256	journal	December 2009
Unique lipid composition of Treponema pallidum (Nichols virulent strain) Matthews, H. M.; Yang, T. K.; Jenkin, H. M. Infection and Immunity, Vol. 24, Issue 3 https://doi.org/10.1128/IAI.24.3.713-719.1979	journal	June 1979
Fatty acids of Treponema pallidum and Borrelia burgdorferi lipoproteins Belisle, J. T.; Brandt, M. E.; Radolf, J. D. Journal of Bacteriology, Vol. 176, Issue 8 https://doi.org/10.1128/JB.176.8.2151-2157.1994	journal	April 1994
LigPlot+: Multiple Ligand–Protein Interaction Diagrams for Drug Discovery Laskowski, Roman A.; Swindells, Mark B. Journal of Chemical Information and Modeling, Vol. 51, Issue 10 https://doi.org/10.1021/ci200227u	journal	October 2011
Iron Metabolism Regulates p53 Signaling through Direct Heme-p53 Interaction and Modulation of p53 Localization, Stability, and Function Shen, Jia; Sheng, Xiangpeng; Chang, ZeNan Cell Reports, Vol. 7, Issue 1 https://doi.org/10.1016/j.celrep.2014.02.042	journal	April 2014
Characterizing the Syphilis-Causing Treponema pallidum ssp. pallidum Proteome Using Complementary Mass Spectrometry Osbak, Kara K.; Houston, Simon; Lithgow, Karen V. PLOS Neglected Tropical Diseases, Vol. 10, Issue 9 https://doi.org/10.1371/journal.pntd.0004988	journal	September 2016
Identification and localization of integral membrane proteins of virulent Treponema pallidum subsp. pallidum by phase partitioning with the nonionic detergent triton X-114 Radolf, J. D.; Chamberlain, N. R.; Clausell, A. Infection and Immunity, Vol. 56, Issue 2 https://doi.org/10.1128/IAI.56.2.490-498.1988	journal	February 1988
The Transition from Closed to Open Conformation of Treponema pallidum Outer Membrane-associated Lipoprotein TP0453 Involves Membrane Sensing and Integration by Two Amphipathic Helices Luthra, Amit; Zhu, Guangyu; Desrosiers, Daniel C. Journal of Biological Chemistry, Vol. 286, Issue 48 https://doi.org/10.1074/jbc.M111.305284	journal	December 2011
TP0453, a Concealed Outer Membrane Protein of Treponema pallidum , Enhances Membrane Permeability Hazlett, Karsten R. O.; Cox, David L.; Decaffmeyer, Marc Journal of Bacteriology, Vol. 187, Issue 18 https://doi.org/10.1128/JB.187.18.6499-6508.2005	journal	September 2005
Surface-Associated Host Proteins on Virulent Treponema pallidum Alderete, John F.; Baseman, Joel B. Infection and Immunity, Vol. 26, Issue 3 https://doi.org/10.1128/IAI.26.3.1048-1056.1979	journal	December 1979
Sequence Variation of Rare Outer Membrane Protein β-Barrel Domains in Clinical Strains Provides Insights into the Evolution of Treponema pallidum subsp. pallidum , the Syphilis Spirochete Kumar, Sanjiv; Caimano, Melissa J.; Anand, Arvind mBio, Vol. 9, Issue 3 https://doi.org/10.1128/mBio.01006-18	journal	July 2018
Bipartite Topology of Treponema pallidum Repeat Proteins C/D and I Anand, Arvind; LeDoyt, Morgan; Karanian, Carson Journal of Biological Chemistry, Vol. 290, Issue 19 https://doi.org/10.1074/jbc.M114.629188	journal	May 2015
A Homology Model Reveals Novel Structural Features and an Immunodominant Surface Loop/Opsonic Target in the Treponema pallidum BamA Ortholog TP_0326 Luthra, Amit; Anand, Arvind; Hawley, Kelly L. Journal of Bacteriology, Vol. 197, Issue 11 https://doi.org/10.1128/JB.00086-15	journal	June 2015
Pathogen specificity of Treponema pallidum subsp. pallidum integral membrane proteins identified by phase partitioning with Triton X-114 Radolf, J. D.; Norgard, M. V. Infection and Immunity, Vol. 56, Issue 7 https://doi.org/10.1128/IAI.56.7.1825-1828.1988	journal	July 1988
Crystal Structure of the Tp34 (TP0971) Lipoprotein of Treponema pallidum: IMPLICATIONS OF ITS METAL-BOUND STATE AND AFFINITY FOR HUMAN LACTOFERRIN Deka, Ranjit K.; Brautigam, Chad A.; Tomson, Farol L. Journal of Biological Chemistry, Vol. 282, Issue 8 https://doi.org/10.1074/jbc.M610215200	journal	December 2006
Slam is an outer membrane protein that is required for the surface display of lipidated virulence factors in Neisseria Hooda, Yogesh; Lai, Christine Chieh-Lin; Judd, Andrew Nature Microbiology, Vol. 1, Issue 4 https://doi.org/10.1038/nmicrobiol.2016.9	journal	February 2016
Identification of a Large Family of Slam-Dependent Surface Lipoproteins in Gram-Negative Bacteria Hooda, Yogesh; Lai, Christine C. L.; Moraes, Trevor F. Frontiers in Cellular and Infection Microbiology, Vol. 7 https://doi.org/10.3389/fcimb.2017.00207	journal	May 2017
Of ticks, mice and men: understanding the dual-host lifestyle of Lyme disease spirochaetes Radolf, Justin D.; Caimano, Melissa J.; Stevenson, Brian Nature Reviews Microbiology, Vol. 10, Issue 2 https://doi.org/10.1038/nrmicro2714	journal	January 2012
Comprehensive Spatial Analysis of the Borrelia burgdorferi Lipoproteome Reveals a Compartmentalization Bias toward the Bacterial Surface Dowdell, Alexander S.; Murphy, Maxwell D.; Azodi, Christina Journal of Bacteriology, Vol. 199, Issue 6 https://doi.org/10.1128/JB.00658-16	journal	March 2017
Secretion of Bacterial Lipoproteins: Through the Cytoplasmic Membrane, the Periplasm and Beyond Zückert, Wolfram R. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, Vol. 1843, Issue 8 https://doi.org/10.1016/j.bbamcr.2014.04.022	journal	August 2014
Solution Structure of the Factor H-binding Protein, a Survival Factor and Protective Antigen of Neisseria meningitidis Cantini, Francesca; Veggi, Daniele; Dragonetti, Sara Journal of Biological Chemistry, Vol. 284, Issue 14 https://doi.org/10.1074/jbc.C800214200	journal	April 2009
Siderocalins: Siderophore binding proteins evolved for primary pathogen host defense Sia, Allyson K.; Allred, Benjamin E.; Raymond, Kenneth N. Current Opinion in Chemical Biology, Vol. 17, Issue 2 https://doi.org/10.1016/j.cbpa.2012.11.014	journal	April 2013
Characterization of heme binding to recombinant Î±1-microglobulin Karnaukhova, Elena; Rutardottir, SigurbjÃ¶rg; Rajabi, Mohsen Frontiers in Physiology, Vol. 5 https://doi.org/10.3389/fphys.2014.00465	journal	December 2014
Heme Synthesis and Acquisition in Bacterial Pathogens Choby, Jacob E.; Skaar, Eric P. Journal of Molecular Biology, Vol. 428, Issue 17 https://doi.org/10.1016/j.jmb.2016.03.018	journal	August 2016
Ferrous iron efflux systems in bacteria Pi, Hualiang; Helmann, John D. Metallomics, Vol. 9, Issue 7 https://doi.org/10.1039/C7MT00112F	journal	January 2017
Intrinsically unstructured proteins and their functions Dyson, H. Jane; Wright, Peter E. Nature Reviews Molecular Cell Biology, Vol. 6, Issue 3 https://doi.org/10.1038/nrm1589	journal	March 2005
Features of molecular recognition of intrinsically disordered proteins via coupled folding and binding Yang, Jing; Gao, Meng; Xiong, Junwen Protein Science, Vol. 28, Issue 11 https://doi.org/10.1002/pro.3718	journal	September 2019
Cell signaling, division, and organization mediated by intrinsically disordered proteins Pappu, Rohit V. Seminars in Cell & Developmental Biology, Vol. 37 https://doi.org/10.1016/j.semcdb.2015.01.003	journal	January 2015
How Common Is Disorder? Occurrence of Disordered Residues in Four Domains of Life Lobanov, Mikhail; Galzitskaya, Oxana International Journal of Molecular Sciences, Vol. 16, Issue 8 https://doi.org/10.3390/ijms160819490	journal	August 2015
Competitive recruitment of the periplasmic translocation portal TolB by a natively disordered domain of colicin E9 Loftus, S. R.; Walker, D.; Mate, M. J. Proceedings of the National Academy of Sciences, Vol. 103, Issue 33 https://doi.org/10.1073/pnas.0603433103	journal	August 2006
SilE is an intrinsically disordered periplasmic “molecular sponge” involved in bacterial silver resistance: Intrinsically Disordered Periplasmic “Molecular Sponge” Asiani, Karishma R.; Williams, Huw; Bird, Louise Molecular Microbiology, Vol. 101, Issue 5 https://doi.org/10.1111/mmi.13399	journal	May 2016
Directional Porin Binding of Intrinsically Disordered Protein Sequences Promotes Colicin Epitope Display in the Bacterial Periplasm Housden, Nicholas G.; Rassam, Patrice; Lee, Sejeong Biochemistry, Vol. 57, Issue 29 https://doi.org/10.1021/acs.biochem.8b00621	journal	June 2018
Secondary Syphilis in Cali, Colombia: New Concepts in Disease Pathogenesis Cruz, Adriana R.; Pillay, Allan; Zuluaga, Ana V. PLoS Neglected Tropical Diseases, Vol. 4, Issue 5 https://doi.org/10.1371/journal.pntd.0000690	journal	May 2010
Inverse Fusion PCR Cloning Spiliotis, Markus PLoS ONE, Vol. 7, Issue 4 https://doi.org/10.1371/journal.pone.0035407	journal	April 2012
Biomolecular solution X-ray scattering at the National Synchrotron Light Source Allaire, Marc; Yang, Lin Journal of Synchrotron Radiation, Vol. 18, Issue 1 https://doi.org/10.1107/S0909049510036022	journal	November 2010
PRIMUS: a Windows PC-based system for small-angle scattering data analysis Konarev, Petr V.; Volkov, Vladimir V.; Sokolova, Anna V. Journal of Applied Crystallography, Vol. 36, Issue 5, p. 1277-1282 https://doi.org/10.1107/S0021889803012779	journal	September 2003
Determination of the regularization parameter in indirect-transform methods using perceptual criteria Svergun, D. I. Journal of Applied Crystallography, Vol. 25, Issue 4, p. 495-503 https://doi.org/10.1107/S0021889892001663	journal	August 1992
FoXS, FoXSDock and MultiFoXS: Single-state and multi-state structural modeling of proteins and their complexes based on SAXS profiles Schneidman-Duhovny, Dina; Hammel, Michal; Tainer, John A. Nucleic Acids Research, Vol. 44, Issue W1 https://doi.org/10.1093/nar/gkw389	journal	May 2016
Deciphering conformational transitions of proteins by small angle X-ray scattering and normal mode analysis Panjkovich, Alejandro; Svergun, Dmitri I. Physical Chemistry Chemical Physics, Vol. 18, Issue 8 https://doi.org/10.1039/C5CP04540A	journal	January 2016
New developments in the ATSAS program package for small-angle scattering data analysis Petoukhov, Maxim V.; Franke, Daniel; Shkumatov, Alexander V. Journal of Applied Crystallography, Vol. 45, Issue 2 https://doi.org/10.1107/S0021889812007662	journal	March 2012
Features and development of Coot Emsley, P.; Lohkamp, B.; Scott, W. G. Acta Crystallographica Section D Biological Crystallography, Vol. 66, Issue 4 https://doi.org/10.1107/S0907444910007493	journal	March 2010
PDBsum: Structural summaries of PDB entries Laskowski, Roman A.; Jabłońska, Jagoda; Pravda, Lukáš Protein Science, Vol. 27, Issue 1 https://doi.org/10.1002/pro.3289	journal	October 2017
PROMALS3D: a tool for multiple protein sequence and structure alignments Pei, Jimin; Kim, Bong-Hyun; Grishin, Nick V. Nucleic Acids Research, Vol. 36, Issue 7 https://doi.org/10.1093/nar/gkn072	journal	February 2008
Deciphering key features in protein structures with the new ENDscript server Robert, Xavier; Gouet, Patrice Nucleic Acids Research, Vol. 42, Issue W1 https://doi.org/10.1093/nar/gku316	journal	April 2014
Predicting intrinsic disorder from amino acid sequence Obradovic, Zoran; Peng, Kang; Vucetic, Slobodan Proteins: Structure, Function, and Genetics, Vol. 53, Issue S6 https://doi.org/10.1002/prot.10532	journal	January 2003
Insights into mechanism and functional consequences of heme binding to hemolysin-activating lysine acyltransferase HlyC from Escherichia coli Peherstorfer, Sandra; Brewitz, Hans Henning; Paul George, Ajay Abisheck Biochimica et Biophysica Acta (BBA) - General Subjects, Vol. 1862, Issue 9 https://doi.org/10.1016/j.bbagen.2018.06.012	journal	September 2018
TP0326, a Treponema pallidum β-barrel assembly machinery A (BamA) orthologue and rare outer membrane protein: T. pallidum BamA orthologue and rare OMP Desrosiers, Daniel C.; Anand, Arvind; Luthra, Amit Molecular Microbiology, Vol. 80, Issue 6 https://doi.org/10.1111/j.1365-2958.2011.07662.x	journal	April 2011
TprC/D (Tp0117/131), a Trimeric, Pore-Forming Rare Outer Membrane Protein of Treponema pallidum, Has a Bipartite Domain Structure Anand, Arvind; Luthra, Amit; Dunham-Ems, Star Journal of Bacteriology, Vol. 194, Issue 9 https://doi.org/10.1128/JB.00101-12	journal	May 2012
The Tprk Protein of Treponema pallidum Is Periplasmic and Is Not a Target of Opsonic Antibody or Protective Immunity Hazlett, Karsten R. O.; Sellati, Timothy J.; Nguyen, Tung T. Journal of Experimental Medicine, Vol. 193, Issue 9 https://doi.org/10.1084/jem.193.9.1015	journal	April 2001
Fast, scalable generation of high‐quality protein multiple sequence alignments using Clustal Omega Sievers, Fabian; Wilm, Andreas; Dineen, David Molecular Systems Biology, Vol. 7, Issue 1 https://doi.org/10.1038/msb.2011.75	journal	January 2011
PVS: a web server for protein sequence variability analysis tuned to facilitate conserved epitope discovery Garcia-Boronat, M.; Diez-Rivero, C. M.; Reinherz, E. L. Nucleic Acids Research, Vol. 36, Issue Web Server https://doi.org/10.1093/nar/gkn211	journal	May 2008
Lipid modification of the 17-kilodalton membrane immunogen of Treponema pallidum determines macrophage activation as well as amphiphilicity Akins, D. R.; Purcell, B. K.; Mitra, M. M. Infection and Immunity, Vol. 61, Issue 4 https://doi.org/10.1128/IAI.61.4.1202-1210.1993	journal	April 1993
Genetic and physicochemical characterization of the recombinant DNA-derived 47-kilodalton surface immunogen of Treponema pallidum subsp. pallidum Chamberlain, N. R.; Radolf, J. D.; Hsu, P. L. Infection and Immunity, Vol. 56, Issue 1 https://doi.org/10.1128/IAI.56.1.71-78.1988	journal	January 1988

Similar Records

Immunity in experimental syphilis. VI. Successful vaccination of rabbits with Treponema pallidum, Nichols strain, attenuated by $gamma$ irradiation

Journal Article · 1973 · J. Immunol., v. 110, no. 5, pp. 1206-1215 · OSTI ID:1690189

Miller, J N

IMMUNITY IN EXPERIMENTAL SYPHILIS. IV. SEMOLOGICAL REACTIVITY OF ANTIGENS EXTRACTED FROM $gamma$-IRRADIATED TREPONEMA PALLIDUM AND TREPONEMA REITERI

Journal Article · 1966 · Journal of Bacteriology (U.S.) · OSTI ID:1690189

Miller, J N; De Bruijn, J H; Bekker, J H

IMMUNITY IN EXPERIMENTAL SYPHILIS. III. ATTENUATION OF VIRULENT TREPONEMA PALLIDUM BY $gamma$-IRRADIATION

Journal Article · 1965 · Journal of Bacteriology (U.S.) · OSTI ID:1690189

Miller, J N

Related Subjects

99 GENERAL AND MISCELLANEOUS

Title: Evidence that immunization with TP0751, a bipartite Treponema pallidum lipoprotein with an intrinsically disordered region and lipocalin fold, fails to protect in the rabbit model of experimental syphilis

Citation Formats

References (121)

Similar Records

Related Subjects