Person: UYSAL, SERDAR
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Publication Open Access Large-Scale Production of Anti-RNase A VHH Expressed in pyrG Auxotrophic Aspergillus oryzae(2023-05-01) Karaman, Elif; Eyupoglu, Alp Ertunga; Mahmoudi Azar, Lena; Uysal, Serdar; KARAMAN, ELİF; UYSAL, SERDARNanobodies, also referred to as VHH antibodies, are the smallest fragments of naturally produced camelid antibodies and are ideal affinity reagents due to their remarkable properties. They are considered an alternative to monoclonal antibodies (mAbs) with potential utility in imaging, diagnostic, and other biotechnological applications given the difficulties associated with mAb expression.Aspergillus oryzae (A. oryzae)is a potential system for the large-scale expression and production of functional VHH antibodies that can be used to meet the demand for affinity reagents. In this study, anti-RNase A VHH was expressed under the control of the glucoamylase promoter inpyrGauxotrophicA. oryzaegrown in a fermenter. The feature ofpyrGauxotrophy, selected for the construction of a stable and efficient platform, was established using homologous recombination. Pull-down assay, size exclusion chromatography, and surface plasmon resonance were used to confirm the binding specificity of anti-RNase A VHH to RNase A. The affinity of anti-RNase A VHH was nearly 18.3-fold higher (1.9 nM) when expressed inpyrGauxotrophicA. oryzaerather than inEscherichia coli. This demonstrates thatpyrGauxotrophicA. oryzaeis a practical, industrially scalable, and promising biotechnological platform for the large-scale production of functional VHH antibodies with high binding activity.Publication Metadata only Transient receptor potential cation channel, subfamily C, member 5 (TRPC5) is a cold-transducer in the peripheral nervous system.(2011-11-01T00:00:00Z) Zimmermann, K; Lennerz, JK; Hein, A; Link, AS; Kaczmarek, JS; Delling, M; Uysal, SERDAR; Pfeifer, JD; Riccio, A; Clapham, DE; UYSAL, SERDARPublication Metadata only Structure of active β-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide.(2013-05-02T00:00:00Z) Shukla, AK; Manglik, A; Kruse, AC; Xiao, K; Reis, RI; Tseng, WC; Staus, DP; Hilger, D; Uysal, SERDAR; Huang, LY; Paduch, M; Tripathi-Shukla, P; Koide, A; Koide, S; Weis, WI; Kossiakoff, AA; Kobilka, BK; Lefkowitz, RJ; UYSAL, SERDARPublication Metadata only Mechanism of activation gating in the full-length KcsA K+ channel.(2011-07-19T00:00:00Z) Uysal, SERDAR; Cuello, LG; Cortes, DM; Koide, S; Kossiakoff, AA; Perozo, E; UYSAL, SERDARPublication Open Access The Preserved HTH-Docking Cleft of HIV-1 Integrase Is Functionally Critical.(2016-11-01T00:00:00Z) Galilee, M; Britan-Rosich, E; Griner, SL; Uysal, SERDAR; Baumgärtel, V; Lamb, DC; Kossiakoff, AA; Kotler, M; Stroud, RM; Marx, A; Alian, A; UYSAL, SERDARHIV-1 integrase (IN) catalyzes viral DNA integration into the host genome and facilitates multifunctional steps including virus particle maturation. Competency of IN to form multimeric assemblies is functionally critical, presenting an approach for anti-HIV strategies. Multimerization of IN depends on interactions between the distinct subunit domains and amongst the flanking protomers. Here we elucidate an overlooked docking cleft of IN core domain that anchors the Nterminal helix-turn-helix (HTH)-motif in a highly preserved and functionally critical configuration. Crystallographic structure of IN core domain in complex with Fab specifically targeting this cleft reveals a steric overlap that would inhibit HTH-docking, C-terminal domain contacts, DNA binding and subsequent multimerization. While Fab inhibits in vitro IN integration activity, in vivo it abolishes virus particle production by specifically associating with preprocessedIN within Gag-Pol and interfering with early cytosolic Gag/Gag-Pol assemblies. The HTHdocking cleft may offer a fresh hotspot for future anti-HIV intervention strategies.Publication Metadata only Characterization of engineered actin binding proteins that control filament assembly and structure.(2010-11-12T00:00:00Z) Brawley, CM; Uysal, SERDAR; Kossiakoff, AA; Rock, RS; UYSAL, SERDARPublication Metadata only Generating conformation-specific synthetic antibodies to trap proteins in selected functional states.(2013-03-15T00:00:00Z) Paduch, M; Koide, A; Uysal, SERDAR; Rizk, SS; Koide, S; Kossiakoff, AA; UYSAL, SERDAR