Barbara Tizzano

Research Center Borstel - Leibniz Lung Center

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Pasquale Palladino

University of Florence

Menotti Ruvo

Institute of Biostructure and Bioimaging

Carlo Pedone

Institute of Biostructure and Bioimaging

Daniela Marasco

University of Naples Federico II

Raffaele Ragone

Università Campus Bio-Medico

Ettore Benedetti

University of Naples Federico II

Filomena Rossi

University of Naples Federico II

Luisa Ronga

Régulations Naturelle et Artificielle

Rita Berisio

Institute of Biostructure and Bioimaging

Matthias Wilmanns

European Molecular Biology Laboratory

Cooperative Institutions

University of Naples Federico II

National Research Council

Institute of Biostructure and Bioimaging

Centro Interuniversitario di Ricerca sui Peptidi Bioattivi

Federico II University Hospital

National Academies of Sciences, Engineering, and Medicine

Institute for Experimental Endocrinology and Oncology

University of Sannio

Naples Anesthesia & Physician Associates

University of Campania "Luigi Vanvitelli"

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Does tetracycline bind helix 2 of prion? An integrated spectroscopical and computational study of the interaction between the antibiotic and α helix 2 human prion protein fragments

Proteins Structure Function and Bioinformatics (2006)

Luisa Ronga Emma Langella Pasquale Palladino Daniela Marasco Barbara Tizzano

Abstract We demonstrate here that tetracycline (TC) can strongly interact ( K D ′ = 189 ± 7 n M ) with model peptides derived from the C‐terminal globular domain of the prion protein, hPrP [173‐195], and that interaction concerns residues within the C‐terminal half of the helix 2, a short region previously indicated as endowed with ambivalent conformational behavior and implicated in PrP conversion to the β‐sheet‐rich, infective scrapie variant. Data have been confirmed by binding studies with the N‐terminal truncated 180‐195 variant that displays a dissociation constant of 483 ± 30 n M . Remarkably, TC does not influence the structure of the N‐terminally fluoresceinated peptides that both show α‐helical conformations. Docking calculations and molecular dynamics simulations suggest a direct, strong interaction of the antibiotic with exposed side chain functional groups of threonines 190‐193 on the solvent‐exposed surface of helix 2. Proteins 2007 © 2006 Wiley‐Liss, Inc.

Dissociation constant

Helix (gastropod)

C-terminus

Docking (animal)

Side chain

10.1002/prot.21204

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Citations (27)

Survival of hypoxia-induced dormancy is not a common feature of all strains of the Mycobacterium tuberculosis complex

Scientific Reports (2021)

Barbara Tizzano Tobias Dallenga Christian Utpatel Jochen Behrends Susanne Homolka

Abstract While persistence in a dormant state is crucial for the life cycle of Mycobacterium tuberculosis , no investigation regarding dormancy survival of different strains across different lineages was performed so far. We analyzed responses to oxygen starvation and recovery in terms of growth, metabolism, and transcription. All different strains belonging to the Euro-American lineage (L4) showed similar survival and resuscitation characteristics. Different clinical isolates from the Beijing (L2), East African-Indian (L3), and Delhi/Central Asian (L1) lineage did not survive oxygen starvation. We show that dormancy survival is lineage-dependent. Recovery from O 2 starvation was only observed in strains belonging to the Euro-American (L4) lineage but not in strains belonging to different lineages (L1, L2, L3). Thus, resuscitation from dormancy after oxygen starvation is not a general feature of all M. tuberculosis strains as thought before. Our findings are of key importance to understand infection dynamics of non-Euro-American vs Euro-American strains and to develop drugs targeting the dormant state.

Lineage (genetic)

Multidrug tolerance

10.1038/s41598-021-81223-6

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The effect of the osmolyte trimethylamine N‐oxide on the stability of the prion protein at low pH

Biopolymers (2006)

Vincenzo Granata Pasquale Palladino Barbara Tizzano Alessandro Negro Rita Berisio

Abstract A study of the effect of trimethylamine N‐oxide on the stability of two recombinant forms of the prion protein PrP, an ovine full‐length and a human truncated form, is here reported. Both thermal denaturation and denaturation at room temperature were analyzed at pH values above and below the pKa of trimethylamine N‐oxide, which is close to 4.7. Surprisingly, results showed that not only is trimethylamine N‐oxide able to decrease PrP thermal stability at low pH but it also acts as a strong denaturant at room temperature. Likely, this destabilization is due to the capability of the cationic form of trimethylamine N‐oxide to interact with the protein backbone as well as to weaken electrostatic interactions which are important for PrP fold. These results constitute the first experimental measurement of the effect of trimethylamine N‐oxide on PrP stability and provide an unambiguous proof of the destabilizing effect of this osmolyte on PrP at low pH. © 2006 Wiley Periodicals, Inc. Biopolymers 82: 234–240, 2006 This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

Osmolyte

Trimethylamine N-oxide

Protein Stability

10.1002/bip.20481

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Citations (28)

Crystal Structure of the Resuscitation-Promoting Factor ΔDUFRpfB from M. tuberculosis

Journal of Molecular Biology (2008)

Alessia Ruggiero Barbara Tizzano Emilia Pedone Carlo Pedone Matthias Wilmanns

Globular protein

10.1016/j.jmb.2008.10.042

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Citations (75)

Protein interactions mediated by α-helical domains

Barbara Tizzano

10.6092/unina/fedoa/2614

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Citations (0)

Structure of Rv1477, hypothetical invasion protein of Mycobacterium tuberculosis

Vivian Pogenberg Barbara Tizzano Matthias Wilmanns

10.2210/pdb2xiv/pdb

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Tyrosine Phosphorylation of Phosphoinositide-Dependent Kinase 1 by the Insulin Receptor IsNecessary for Insulin Metabolic Signaling

Molecular and Cellular Biology (2005)

Francesca Fiory Anna Teresa Alberobello Claudia Miele Francesco Oriente Iolanda Esposito

In L6 myoblasts, insulin receptors with deletion of the C-terminal 43 amino acids (IR(Delta43)) exhibited normal autophosphorylation and IRS-1/2 tyrosine phosphorylation. The L6 cells expressing IR(Delta43) (L6(IRDelta43)) also showed no insulin effect on glucose uptake and glycogen synthase, accompanied by a >80% decrease in insulin induction of 3-phosphoinositide-dependent protein kinase 1 (PDK-1) activity and tyrosine phosphorylation and of protein kinase B (PKB) phosphorylation at Thr(308). Insulin induced the phosphatidylinositol 3 kinase-dependent coprecipitation of PDK-1 with wild-type IR (IR(WT)), but not IR(Delta43). Based on overlay blotting, PDK-1 directly bound IR(WT), but not IR(Delta43). Insulin-activated IR(WT), and not IR(Delta43), phosphorylated PDK-1 at tyrosines 9, 373, and 376. The IR C-terminal 43-amino-acid peptide (C-terminal peptide) inhibited in vitro PDK-1 tyrosine phosphorylation by the IR. Tyr-->Phe substitution prevented this inhibitory action. In the L6(hIR) cells, the C-terminal peptide coprecipitated with PDK-1 in an insulin-stimulated fashion. This peptide simultaneously impaired the insulin effect on PDK-1 coprecipitation with IR(WT), on PDK-1 tyrosine phosphorylation, on PKB phosphorylation at Thr(308), and on glucose uptake. Upon insulin exposure, PDK-1 membrane persistence was significantly reduced in L6(IRDelta43) compared to control cells. In L6 cells expressing IR(WT), the C-terminal peptide also impaired insulin-dependent PDK-1 membrane persistence. Thus, PDK-1 directly binds to the insulin receptor, followed by PDK-1 activation and insulin metabolic effects.

Insulin receptor substrate

10.1128/mcb.25.24.10803-10814.2005

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Expression, purification, crystallization and preliminary X-ray crystallographic analysis of a resuscitation-promoting factor fromMycobacterium tuberculosis

Acta Crystallographica Section F Structural Biology and Crystallization Communications (2007)

Alessia Ruggiero Barbara Tizzano Arie Geerlof Emilia Pedone Carlo Pedone

The resuscitation-promoting factor RpfB, the most complex of the five resuscitation-promoting factors produced by M. tuberculosis, is devoted to bacterial reactivation from the dormant state. RpfB consists of 362 residues predicted to form five domains. An RpfB fragment containing the protein catalytic domain and a G5 domain has been successfully crystallized using vapour-diffusion methods. This is the first crystallographic study of a resuscitation-promoting factor. Crystals of this protein belong to space group I422, with unit-cell parameters a = 97.63, b = 97.63, c = 114.87 Å. Diffraction data have also been collected from a selenomethionine derivative at 2.9 Å resolution. Model building using the phases derived from the multiwavelength anomalous dispersion experiment is in progress.

10.1107/s1744309107043217

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Citations (10)