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Your search keyword '"Dimitrov, Jordan D."' showing total 275 results
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275 results on '"Dimitrov, Jordan D."'

1. TCTP regulates genotoxic stress and tumorigenicity via intercellular vesicular signaling

Author

Amson, Robert, Senff-Ribeiro, Andrea, Karafin, Teele, Lespagnol, Alexandra, Honoré, Joane, Baylot, Virginie, Banroques, Josette, Tanner, N Kyle, Chamond, Nathalie, Dimitrov, Jordan D, Hoebeke, Johan, Droin, Nathalie M, Job, Bastien, Piard, Jonathan, Bommer, Ulrich-Axel, Choi, Kwang-Wook, Abdelfatah, Sara, Efferth, Thomas, Telerman, Stephanie B, Geyer, Felipe Correa, Reis-Filho, Jorge, and Telerman, Adam

Published
2024
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3. Broad sarbecovirus neutralization by combined memory B cell antibodies to ancestral SARS-CoV-2

Author

Planchais, Cyril, Fernández, Ignacio, Chalopin, Benjamin, Bruel, Timothée, Rosenbaum, Pierre, Beretta, Maxime, Dimitrov, Jordan D., Conquet, Laurine, Donati, Flora, Prot, Matthieu, Porrot, Françoise, Planas, Delphine, Staropoli, Isabelle, Guivel-Benhassine, Florence, Baquero, Eduard, van der Werf, Sylvie, Haouz, Ahmed, Simon-Lorière, Etienne, Montagutelli, Xavier, Maillère, Bernard, Rey, Félix A., Guardado-Calvo, Pablo, Nozach, Hervé, Schwartz, Olivier, and Mouquet, Hugo

Published
2024
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6. Transplacental delivery of therapeutic proteins by engineered immunoglobulin G: a step toward perinatal replacement therapy

Author

Mimoun, Angelina, Bou-Jaoudeh, Melissa, Delignat, Sandrine, Daventure, Victoria, Reyes Ruiz, Alejandra, Lecerf, Maxime, Azam, Aurélien, Noe, Remi, Peyron, Ivan, Christophe, Olivier D., Lenting, Peter J., Proulle, Valérie, McIntosh, Jenny, Nathwani, Amit C., Dimitrov, Jordan D., Denis, Cécile V., and Lacroix-Desmazes, Sébastien

Published
2023
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26. Polyreactivity of antibodies from different B-cell subpopulations is determined by distinct sequence patterns of variable region.

Author

Lecerf, Maxime, Lacombe, Robin V., and Dimitrov, Jordan D.

Subjects
IMMUNOGLOBULIN light chains, IMMUNOGLOBULIN heavy chains, IMMUNOGLOBULINS, AMINO acid residues, TALL-1 (Protein), SEQUENCE analysis
Abstract

An antibody molecule that can bind to multiple distinct antigens is defined as polyreactive. In the present study, we performed statistical analyses to assess sequence correlates of polyreactivity of >600 antibodies cloned from different Bcell types of healthy humans. The data revealed several sequence patterns of variable regions of heavy and light immunoglobulin chains that determine polyreactivity. The most prominent identified patterns were increased number of basic amino acid residues, reduced frequency of acidic residues, increased number of aromatic and hydrophobic residues, and longer length of CDR L1. Importantly, our study revealed that antibodies isolated from different B-cell populations used distinct sequence patterns (or combinations of them) for polyreactive antigen binding. Furthermore, we combined the data from sequence analyses with molecular modeling of selected polyreactive antibodies and demonstrated that human antibodies can use multiple pathways for achieving antigen-binding promiscuity. These data reconcile some contradictions in the literature regarding the determinants of antibody polyreactivity. Moreover, our study demonstrates that the mechanism of polyreactivity of antibodies evolves during immune response and might be tailored to specific functional properties of different B-cell compartments. Finally, these data can be of use for efforts in the development and engineering of therapeutic antibodies. [ABSTRACT FROM AUTHOR]

Published
2023
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33. Assessment of the breadth of binding promiscuity of heme towards human proteins

Author

Roumenina, Lubka T., Dimitrov, Jordan D., Centre de Recherche des Cordeliers (CRC (UMR_S_1138 / U1138)), École pratique des hautes études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Université Paris Cité (UPCité), and Jordan, Dimitrov

Subjects
protein microarrays, Clinical Biochemistry, DNA binding proteins, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Humans, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, binding promiscuity, heme, Molecular Biology, Biochemistry, Protein Binding
Abstract

Heme regulates important biological processes by transient interactions with many human proteins. The goal of the present study was to assess extends of protein binding promiscuity of heme. To this end we evaluated interaction of heme with >9000 human proteins. Heme manifested high binding promiscuity by binding to most of the proteins in the array. Nevertheless, some proteins have outstanding heme binding capacity. Bioinformatics analyses revealed that apart from typical haemoproteins, these proteins are frequently involved in metal binding or have the potential to recognize DNA. This study can contribute for understanding the regulatory functions of labile heme.

Published
2022

34. Hyperoxidized Species of Heme Have a Potent Capacity to Induce Autoreactivity of Human IgG Antibodies.

Author

Wiatr, Marie, Hadzhieva, Maya, Lecerf, Maxime, Noé, Rémi, Justesen, Sune, Lacroix-Desmazes, Sébastien, Dragon-Durey, Marie-Agnès, and Dimitrov, Jordan D.

Subjects
FC receptors, HEME, IMMUNOGLOBULINS, IMMUNOGLOBULIN G, IRON oxidation, OXIDIZING agents, IRON in the body
Abstract

The interaction of some human antibodies with heme results in posttranslational acquisition of binding to various self- and pathogen-derived antigens. The previous studies on this phenomenon were performed with oxidized heme (Fe3+). In the present study, we elucidated the effect of other pathologically relevant species of heme, i.e., species that were formed after contact of heme with oxidizing agents such as hydrogen peroxide, situations in which heme's iron could acquire higher oxidation states. Our data reveal that hyperoxidized species of heme have a superior capacity to heme (Fe3+) in triggering the autoreactivity of human IgG. Mechanistic studies demonstrated that oxidation status of iron was of critical importance for the heme's effect on antibodies. We also demonstrated that hyperoxidized heme species interacted at higher affinities with IgG and that this binding occurred through a different mechanism as compared to heme (Fe3+). Regardless of their profound functional impact on the antigen-binding properties of antibodies, hyperoxidized species of heme did not affect Fc-mediated functions of IgG, such as binding to the neonatal Fc receptor. The obtained data contribute to a better understanding of the pathophysiological mechanism of hemolytic diseases and of the origin of elevated antibody autoreactivity in patients with some hemolytic disorders. [ABSTRACT FROM AUTHOR]

Published
2023
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38. Evolutionary trajectory of receptor binding specificity and promiscuity of the spike protein of SARS‐CoV‐2.

Author

Planchais, Cyril, Reyes‐Ruiz, Alejandra, Lacombe, Robin, Zarantonello, Alessandra, Lecerf, Maxime, Revel, Margot, Roumenina, Lubka T., Atanasov, Boris P., Mouquet, Hugo, and Dimitrov, Jordan D.

Abstract

SARS‐CoV‐2 infects cells by attachment to its receptor—the angiotensin converting enzyme 2 (ACE2). Regardless of the wealth of structural data, little is known about the physicochemical mechanism of interactions of the viral spike (S) protein with ACE2 and how this mechanism has evolved during the pandemic. Here, we applied experimental and computational approaches to characterize the molecular interaction of S proteins from SARS‐CoV‐2 variants of concern (VOC). Data on kinetics, activation‐, and equilibrium thermodynamics of binding of the receptor binding domain (RBD) from VOC with ACE2 as well as data from computational protein electrostatics revealed a profound remodeling of the physicochemical characteristics of the interaction during the evolution. Thus, as compared to RBDs from Wuhan strain and other VOC, Omicron RBD presented as a unique protein in terms of conformational dynamics and types of non‐covalent forces driving the complex formation with ACE2. Viral evolution resulted in a restriction of the RBD structural dynamics, and a shift to a major role of polar forces for ACE2 binding. Further, we investigated how the reshaping of the physicochemical characteristics of interaction affects the binding specificity of S proteins. Data from various binding assays revealed that SARS‐CoV‐2 Wuhan and Omicron RBDs manifest capacity for promiscuous recognition of unrelated human proteins, but they harbor distinct reactivity patterns. These findings might contribute for mechanistic understanding of the viral tropism and capacity to evade immune responses during evolution. [ABSTRACT FROM AUTHOR]

Published
2022
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40. Hyperfunctional C3 convertase leads to complement deposition on endothelial cells and contributes to atypical hemolytic uremic syndrome

Author

Roumenina, Lubka T., Jablonski, Mathieu, Hue, Christophe, Blouin, Jacques, Dimitrov, Jordan D., Dragon-Durey, Marie-Agnes, Cayla, Mathieu, Fridman, Wolf H., Macher, Marie-Alice, Ribes, David, Moulonguet, Luc, Rostaing, Lionel, Satchell, Simon C., Mathieson, Peter W., Sautes-Fridman, Catherine, Loirat, Chantal, Regnier, Catherine H., Halbwachs-Mecarelli, Lise, and Fremeaux-Bacchi, Veronique

Published
2009
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41. Heme Interferes With Complement Factor I-Dependent Regulation by Enhancing Alternative Pathway Activation.

Author

Gerogianni, Alexandra, Dimitrov, Jordan D., Zarantonello, Alessandra, Poillerat, Victoria, Chonat, Satheesh, Sandholm, Kerstin, McAdam, Karin E., Ekdahl, Kristina N., Mollnes, Tom E., Mohlin, Camilla, Roumenina, Lubka T., and Nilsson, Per H.

Subjects
HEME, PAROXYSMAL hemoglobinuria, COMPLEMENT factor H, BLOOD proteins, SICKLE cell anemia, COMPLEMENT receptors
Abstract

Hemolysis, as a result of disease or exposure to biomaterials, is characterized by excess amounts of cell-free heme intravascularly and consumption of the protective heme-scavenger proteins in plasma. The liberation of heme has been linked to the activation of inflammatory systems, including the complement system, through alternative pathway activation. Here, we investigated the impact of heme on the regulatory function of the complement system. Heme dose-dependently inhibited factor I-mediated degradation of soluble and surface-bound C3b, when incubated in plasma or buffer with complement regulatory proteins. Inhibition occurred with factor H and soluble complement receptor 1 as co-factors, and the mechanism was linked to the direct heme-interaction with factor I. The heme-scavenger protein hemopexin was the main contaminant in purified factor I preparations. This led us to identify that hemopexin formed a complex with factor I in normal human plasma. These complexes were significantly reduced during acute vasoocclusive pain crisis in patients with sickle cell disease, but the complexes were normalized at their baseline outpatient clinic visit. Hemopexin exposed a protective function of factor I activity in vitro, but only when it was present before the addition of heme. In conclusion, we present a mechanistic explanation of how heme promotes uncontrolled complement alternative pathway amplification by interfering with the regulatory capacity of factor I. Reduced levels of hemopexin and hemopexin-factor I complexes during an acute hemolytic crisis is a risk factor for heme-mediated factor I inhibition. [ABSTRACT FROM AUTHOR]

Published
2022
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