Daniela Volke

Leipzig University

Author Statistics

Papers

Citation

H-Index

i-10 index

Research Trends

Author Order

Document Type

Co-Authors

Ralf Hoffmann

Leipzig University

Felix Fingas

CS Diagnostics

Andor Krizsan

Leipzig University

Rayk Hassert

Leipzig University

Christian Wilhelm

Leipzig University

Reimund Goss

Leipzig University

Daniel Knappe

Leipzig University

Juliane Fornefett

Leipzig University

David Singer

Leipzig University

Petra Bielefeldt

CS Diagnostics

Cooperative Institutions

Leipzig University

119

University Hospital Leipzig

Leibniz-Institut für Naturstoff-Forschung und Infektionsbiologie e. V. - Hans-Knöll-Institut (HKI)

Charité - Universitätsmedizin Berlin

Leibniz Association

Martin Luther University Halle-Wittenberg

Centre National de la Recherche Scientifique

Humboldt-Universität zu Berlin

Heidelberg University

Johannes Gutenberg University Mainz

Author Statistics

Papers

Citation

H-Index

i-10 index

Research Field

Sensitive and immunogen-specific serological detection of Rodentibacter pneumotropicus infections in mice

BMC Microbiology (2019)

Felix Fingas Daniela Volke Rayk Hassert Juliane Fornefett Sophie Funk

Rodentibacter (R.) pneumotropicus colonizes the respiratory and urogenital tracts of laboratory mice with a reported moderate serological prevalence from 4 to 13%. Thus, regular tests to identify this pathogen in mice are recommended for animal facilities. However, a recent study indicated that current serological assays are partly insensitive, as C57BL/6 and BALB/c mice infected with R. pneumotropicus were incorrectly screened as seronegative. Here, we report a systematic analysis of protein and lipopolysaccharides antigens by immunoblot and ELISA that allowed establishing a sensitive test system able to differentiate between R. pneumotropicus and the closely related species R. heylii. Furthermore, the main immunogen, designated as 'characteristic antigen for Rodentibacter of laboratory origin 1' (CARLO-1), was identified by two-dimensional gel electrophoresis followed by immunoblot and tandem mass spectrometry in a preparation of outer membrane proteins. An indirect ELISA relying on the recombinantly expressed protein provided high sensitivity, specificity, and selectivity. The corresponding carlo1 gene was highly conserved (> 97%) among 21 isolates of R. pneumotropicus and R. heylii. The newly identified protein CARLO-1 is well suited for the sensitive and specific serological detection of Rodentibacter infections in mice. Indirect differentiation of R. pneumotropicus and R. heylii infections may be possible using an ELISA based on a whole-cell antigen preparation. All four established ELISA systems using a whole-cell preparation, lipopolysaccharides, outer-membrane proteins and protein CARLO-1 as antigen, respectively, outperformed a commercial ELISA in terms of sensitivity.

Immunogen

10.1186/s12866-019-1417-7

Cite

Citations (11)

Additional file 5: of Detection of mammalian orthoreovirus type-3 (Reo-3) infections in mice based on serotype-specific hemagglutination protein sigma-1

Figshare (2018)

Felix Fingas Daniela Volke Petra Bielefeldt Rayk Hassert Ralf Hoffmann

Excel Sheet Raw data of ELISA validation. Sheet 1: Raw data of repeatability, intermediate precision and calculation of the limit of detection. Sheet 2: Raw data of stability experiments. Sheet 3: Raw data of ROC analysis. (XLSX 21 kb)

Sigma

Hemagglutination assay

10.6084/m9.figshare.6870344

Cite

Citations (0)

Isoserine‐Based Biotinylated Photoaffinity Probes that Interact with Penicillin‐Binding Protein 1b.

ChemInform (2002)

Thomas Ruehl Daniela Volke Katherina Stembera Yasumaru Hatanaka Horst Hennig

10.1002/chin.200246053

Cite

Citations (2)

Tierexperimentelle Untersuchungen zu Rodentibacter pneumotropicus und R. heylii: Die Maus als natürlicher Wirt

Pneumologie (2019)

J Fornefett S Funk K Klose U Müller Thomas Grünwald

Einleitung: Rodentibacter (R.) pneumotropicus und R. heylii gehören aktuell zu den häufigsten Pathogenen in Labortierhaltungen. Ziel dieser Arbeit war die Bestimmung der Virulenz aktueller Isolate beider Arten. Weiterhin sollte die Immunantwort von experimentell infizierten BALB/c- und C57BL/6-Mäuse analysiert und neue Erreger-spezifische ELISA-Tests evaluiert werden.

10.1055/s-0039-1692849

Cite

Citations (0)

Identification of Api88 Binding Partners in Escherichia coli Using a Photoaffinity-Cross-Link Strategy and Label-Free Quantification

Journal of Proteome Research (2015)

Daniela Volke Andor Krizsan Nicole Berthold Daniel Knappe Ralf Hoffmann

Gene-encoded antimicrobial peptides (AMPs) kill bacteria very efficiently by either lytic mechanisms or inhibition of specific bacterial targets. Proline-rich AMPs (PrAMPs), for example, produced in insects and mammals rely on the second mechanism. They bind to the 70 kDa bacterial heat shock protein DnaK and the 60 kDa chaperonin GroEL and interfere with protein folding, but this does not explain their strong bactericidal effects. Thus, we looked for further binding partners of apidaecin 1b, originally identified in honey bees, and two rationally optimized analogues (Api88 and Api137). Because affinity chromatography using Api88 as an immobilized ligand enriched only a few proteins at low levels besides DnaK, we synthesized Api88 analogues substituting Tyr7 with p-benzoyl-phenylalanine (Bpa), which can cross-link the peptide to binding partners after UV irradiation. Escherichia coli was incubated with biotinylated Api88 Tyr7Bpa or the corresponding all-d-peptide, irradiated, and lysed. The protein extract was enriched by streptavidin, separated by SDS-PAGE, digested with trypsin, and analyzed by nanoRP-UPLC-ESI-QqTOF-MS/MS. Among the 41 proteins identified, 34 were detected only in the l-Api88 Tyr7Bpa sample, including five 70S ribosomal proteins, DNA-directed RNA polymerase, and pyruvate dehydrogenase, indicating that PrAMPs might interfere with protein translation and energy metabolism.

Photoaffinity labeling

10.1021/acs.jproteome.5b00283

Cite

Citations (16)

Quantitation of a Novel Engineered Anti-infective Host Defense Peptide, ARV-1502: Pharmacokinetic Study of Different Doses in Rats and Dogs

Frontiers in Chemistry (2019)

Alexandra Brakel Daniela Volke Carl N. Kraus László Ötvös Ralf Hoffmann

The designer proline-rich antimicrobial peptide (PrAMP) Chex1-Arg20 amide (ARV-1502) is active against Gram-negative and Gram-positive pathogens in different murine infection models when administered parenterally and possesses a wide therapeutic index. Here we studied the pharmacokinetics of ARV-1502 for the first time when administered intramuscularly or intravenously (IV) in Sprague Dawley rats and Beagle dogs. First, a specific and robust quantitation method relying on parallel reaction monitoring (PRM) using a high-resolution hybrid quadrupole-Orbitrap mass spectrometer coupled on-line to reversed-phase uHPLC was established and validated. The limit of detection was 2 ng/mL and the limit of quantitation was 4 ng/mL when spiked to pooled rat and dog plasma. When ARV-1502 was administered IV at doses of 75 and 250 μg/kg in dogs and rats, the plasma concentrations were 0.7 and 3.4 μg/mL 2 min post-administration, respectively. ARV-1502 plasma concentrations declined exponentially reaching levels between 2 and 4 ng/mL after 2 h. Intramuscular administration of 0.75 mg/kg in dogs and 2.5 mg/kg in rats resulted in a different pharmacokinetics profile. The plasma concentrations peaked at 15 min post-injection at 1 μg/mL (dogs) and 12 μg/mL (rats) and decreased exponentially within 3 h to 4 and 16 ng/mL, respectively. The initial plasma concentrations of ARV-1502 and the decay timing afterwards indicated that the peptide circulated in the blood stream for several hours, at some point above the minimal inhibitory concentration against multidrug-resistant Enterobacteriaceae, with blood concentrations sufficient to suppress bacterial growth and to modulate the immune system.

Beagle

10.3389/fchem.2019.00753

Cite

Citations (6)

Identification of Disease-Associated Cryptococcal Proteins Reactive With Serum IgG From Cryptococcal Meningitis Patients

Frontiers in Immunology (2021)

A. Elisabeth Gressler Daniela Volke Carolina Firacative Christiane L. Schnabel Uwe Müller

Cryptococcus neoformans , an opportunistic fungal pathogen ubiquitously present in the environment, causes cryptococcal meningitis (CM) mainly in immunocompromised patients, such as AIDS patients. We aimed to identify disease-associated cryptococcal protein antigens targeted by the human humoral immune response. Therefore, we used sera from Colombian CM patients, with or without HIV infection, and from healthy individuals living in the same region. Serological analysis revealed increased titers of anti-cryptococcal IgG in HIV-negative CM patients, but not HIV-positive CM patients, compared to healthy controls. In contrast, titers of anti-cryptococcal IgM were not affected by CM. Furthermore, we detected pre-existing IgG and IgM antibodies even in sera from healthy individuals. The observed induction of anti-cryptococcal IgG but not IgM during CM was supported by analysis of sera from C. neoformans -infected mice. Stronger increase in IgG was found in wild type mice with high lung fungal burden compared to IL-4Rα-deficient mice showing low lung fungal burden. To identify the proteins targeted by human anti-cryptococcal IgG antibodies, we applied a quantitative 2D immunoproteome approach identifying cryptococcal protein spots preferentially recognized by sera from CM patients or healthy individuals followed by mass spectrometry analysis. Twenty-three cryptococcal proteins were recombinantly expressed and confirmed to be immunoreactive with human sera. Fourteen of them were newly described as immunoreactive proteins. Twelve proteins were classified as disease-associated antigens, based on significantly stronger immunoreactivity with sera from CM patients compared to healthy individuals. The proteins identified in our screen significantly expand the pool of cryptococcal proteins with potential for (i) development of novel anti-cryptococcal agents based on implications in cryptococcal virulence or survival, or (ii) development of an anti-cryptococcal vaccine, as several candidates lack homology to human proteins and are localized extracellularly. Furthermore, this study defines pre-existing anti-cryptococcal immunoreactivity in healthy individuals at a molecular level, identifying target antigens recognized by sera from healthy control persons.

Cryptococcal meningitis

10.3389/fimmu.2021.709695

Cite

Citations (10)

Ligand Substituent Effects on the Electronic Properties of Lindqvist‐Type Polyoxometalate Multi‐Level‐Switches in the Gas Phase, Solution and on Surfaces

Advanced Materials Interfaces (2024)

Fangshun Yang Givi Kalandia Marco Moors Jonas Lorenz Markus Rohdenburg

Abstract Although the intrinsic electronic properties of polyoxometalates (POMs) can be greatly influenced by modifying them with organic substituents, their resistive switching behavior on surfaces dependent on the organic substituents remains largely unexplored. In this work, we assessed the importance of electron‐withdrawing and electron‐donating ligand substituents on the material properties of a series of hybrid Lindqvist‐type hexavanadates TBA 2 [V 6 O 13 ((OCH 2 ) 3 CCH 2 OH) 2 ] (TBA 2 V 6 ‐OH), TBA 2 [V 6 O 13 ((OCH 2 ) 3 CMe) 2 ] (TBA 2 V 6 ‐Me), TBA 2 [V 6 O 13 ((OCH 2 ) 3 CNHCOCH 2 Cl) 2 ] (TBA 2 V 6 ‐Cl), and TBA 2 [V 6 O 13 ((OCH 2 ) 3 CNHCOCH 2 ‐OOCC 10 H 15 ) 2 ] (TBA 2 V 6 ‐Ad) as potential resistive random‐access memory (ReRAM) components. Compared to their redox behavior in solution, changing the ligand substituents on surfaces results in no significant effect on the potential and, thus, no effect on the resistance steps in the current‐voltage profiles. However, while the current‐voltage characteristics do not change, the peripheral metal‐free substituents in the trisalkoxide framework of Lindqvist‐type hexavanadate molecules influence the adsorption and switching stability of these POMs on gold. This work highlights the noticeable differences between hexavanadate's redox properties in solution (which follow the trend observed in the gas phase) and hexavanadate's resistive switching properties on conducting surfaces. Importantly, their multi‐state switching behavior is not significantly altered by the different type of substituent at the periphery of the trisalkoxo ligands.

Polyoxometalate

Polar effect

10.1002/admi.202400411

Cite

Citations (1)

Prolinreiche antimikrobielle Peptide aus Insekten töten Bakterien durch Hemmung der Proteinbiosynthese am 70S‐Ribosom

Angewandte Chemie (2014)

Andor Krizsan Daniela Volke Stefanie Weinert Norbert Sträter Daniel Knappe

Abstract Prolinreiche antimikrobielle Peptide (PrAMPs) wurden bereits von mehreren Forschungsgruppen und Firmen als vielversprechende Leitverbindungen zur Behandlung systemischer Infektionen mit Gram‐negativen Bakterien untersucht und optimiert. PrAMPs, wie Apidaecine und Oncocine, dringen in Bakterien ein und töten diese wahrscheinlich durch Inhibition spezifischer Zielstrukturen, ohne lytische Wirkung auf die Membranen. Wir zeigen hier, dass Apidaecine und Oncocine mit Dissoziationskonstanten im nanomolaren Bereich an das 70S‐Ribosom binden. Apidaecine wechselwirken mindestens über die beiden C‐terminalen Reste (Arg‐17 und Leu‐18) stark mit dem 70S‐Ribosom, während die Reste Lys‐3, Tyr‐6, Leu‐7 und Arg‐11 die die wichtigsten Bindungsstellen der Oncocine sind. Letztere inhibierten die Proteinbiosynthese in vitro sehr effizient mit IC 50 ‐Werten von 150–240 nmol L −1 . Das Chaperon DnaK ist höchstwahrscheinlich kein Ziel der PrAMPs, bindet diese aber mit niedrigerer Affinität.

10.1002/ange.201407145

Cite

Citations (6)

Insect‐Derived Proline‐Rich Antimicrobial Peptides Kill Bacteria by Inhibiting Bacterial Protein Translation at the 70 S Ribosome

Angewandte Chemie International Edition (2014)

Andor Krizsan Daniela Volke Stefanie Weinert Norbert Sträter Daniel Knappe

Abstract Proline‐rich antimicrobial peptides (PrAMPs) have been investigated and optimized by several research groups and companies as promising lead compounds to treat systemic infections caused by Gram‐negative bacteria. PrAMPs, such as apidaecins and oncocins, enter the bacteria and kill them apparently through inhibition of specific targets without a lytic effect on the membranes. Both apidaecins and oncocins were shown to bind with nanomolar dissociation constants to the 70S ribosome. In apidaecins, at least the two C‐terminal residues (Arg17 and Leu18) interact strongly with the 70S ribosome, whereas residues Lys3, Tyr6, Leu7, and Arg11 are the major interaction sites in oncocins. Oncocins inhibited protein biosynthesis very efficiently in vitro with half maximal inhibitory concentrations (IC 50 values) of 150 to 240 nmol L −1 . The chaperone DnaK is most likely not the main target of PrAMPs but it binds them with lower affinity.

Lytic cycle

Chaperone (clinical)

10.1002/anie.201407145

Cite

Citations (214)