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Functional characterization of a VEGF-A-targeting Anticalin, prototype of a novel therapeutic human protein class.
Gille, Hendrik; Hülsmeyer, Martin; Trentmann, Stefan; Matschiner, Gabriele; Christian, Hans Jürgen; Meyer, Todd; Amirkhosravi, Ali; Audoly, Laurent P; Hohlbaum, Andreas M; Skerra, Arne.
Afiliación
  • Gille H; Pieris Pharmaceuticals GmbH, Lise-Meitner-Strasse 30, 85354, Freising, Germany.
  • Hülsmeyer M; Silence Therapeutics GmbH, Robert-Rössle-Str. 10, 13125, Berlin, Germany.
  • Trentmann S; Pieris Pharmaceuticals GmbH, Lise-Meitner-Strasse 30, 85354, Freising, Germany.
  • Matschiner G; Pieris Pharmaceuticals GmbH, Lise-Meitner-Strasse 30, 85354, Freising, Germany.
  • Christian HJ; Pieris Pharmaceuticals GmbH, Lise-Meitner-Strasse 30, 85354, Freising, Germany. Matschiner@pieris.com.
  • Meyer T; Pieris Pharmaceuticals GmbH, Lise-Meitner-Strasse 30, 85354, Freising, Germany.
  • Amirkhosravi A; Center for Thrombosis Research, Florida Hospital, Orlando, FL, USA.
  • Audoly LP; Center for Thrombosis Research, Florida Hospital, Orlando, FL, USA.
  • Hohlbaum AM; Pieris Pharmaceuticals GmbH, Lise-Meitner-Strasse 30, 85354, Freising, Germany.
  • Skerra A; Pieris Pharmaceuticals GmbH, Lise-Meitner-Strasse 30, 85354, Freising, Germany.
Angiogenesis ; 19(1): 79-94, 2016 Jan.
Article en En | MEDLINE | ID: mdl-26650228
Human tear lipocalin (Tlc) was utilized as a protein scaffold to engineer an Anticalin that specifically binds and functionally blocks vascular endothelial growth factor A (VEGF-A), a pivotal inducer of physiological angiogenesis that also plays a crucial role in several neovascular diseases. Starting from a naive combinatorial library where residues that form the natural ligand-binding site of Tlc were randomized, followed by affinity maturation, the final Anticalin PRS-050 was selected to bind all major splice forms of VEGF-A with picomolar affinity. Moreover, this Anticalin cross-reacts with the murine ortholog. PRS-050 efficiently antagonizes the interaction between VEGF-A and its cellular receptors, and it inhibits VEGF-induced mitogenic signaling as well as proliferation of primary human endothelial cells with subnanomolar IC50 values. Intravitreal administration of the Anticalin suppressed VEGF-induced blood-retinal barrier breakdown in a rabbit model. To allow lasting systemic neutralization of VEGF-A in vivo, the plasma half-life of the Anticalin was extended by site-directed PEGylation. The modified Anticalin efficiently blocked VEGF-mediated vascular permeability as well as growth of tumor xenografts in nude mice, concomitantly with reduction in microvessel density. In contrast to bevacizumab, the Anticalin did not trigger platelet aggregation and thrombosis in human FcγRIIa transgenic mice, thus suggesting an improved safety profile. Since neutralization of VEGF-A activity is well known to exert beneficial effects in cancer and other neovascular diseases, including wet age-related macular degeneration, this Anticalin offers a novel potent small protein antagonist for differentiated therapeutic intervention in oncology and ophthalmology.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Factor A de Crecimiento Endotelial Vascular / Lipocalinas / Terapia Molecular Dirigida Tipo de estudio: Clinical_trials / Prognostic_studies Límite: Animals / Female / Humans Idioma: En Revista: Angiogenesis Asunto de la revista: HEMATOLOGIA Año: 2016 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Alemania

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Factor A de Crecimiento Endotelial Vascular / Lipocalinas / Terapia Molecular Dirigida Tipo de estudio: Clinical_trials / Prognostic_studies Límite: Animals / Female / Humans Idioma: En Revista: Angiogenesis Asunto de la revista: HEMATOLOGIA Año: 2016 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Alemania