Nanobodies as Probes for Protein Dynamics in Vitro and in Cells

被引:83
作者
Dmitriev, Oleg Y. [1 ]
Lutsenko, Svetlana [2 ]
Muyldermans, Serge [3 ]
机构
[1] Univ Saskatchewan, Dept Biochem, Saskatoon, SK S7N 5E5, Canada
[2] Johns Hopkins Univ, Sch Med, Dept Physiol, Baltimore, MD 21205 USA
[3] Vrije Univ Brussel, Unit Cellular & Mol Immunol, B-1050 Brussels, Belgium
基金
加拿大健康研究院; 美国国家卫生研究院;
关键词
nuclear magnetic resonance (NMR); protein domain; protein dynamic; single-domain antibody (sdAb; nanobody); X-ray crystallography; nanobody; protein dynamics; protein structure; protein engineering; BETA(2)-ADRENERGIC RECEPTOR FUNCTION; SINGLE-DOMAIN ANTIBODIES; WILSONS-DISEASE PROTEIN; HEAVY-CHAIN ANTIBODIES; X-RAY-STRUCTURE; CRYSTAL-STRUCTURE; STRUCTURAL INSIGHTS; BINDING-PROTEINS; MULTIDRUG TRANSPORTER; COUPLED RECEPTOR;
D O I
10.1074/jbc.R115.679811
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Nanobodies are the recombinant antigen-recognizing domains of the minimalistic heavy chain-only antibodies produced by camels and llamas. Nanobodies can be easily generated, effectively optimized, and variously derivatized with standard molecular biology protocols. These properties have triggered the recent explosion in the nanobody use in basic and clinical research. This review focuses on the emerging use of nanobodies for understanding and monitoring protein dynamics on the scales ranging from isolated protein domains to live cells, from nanoseconds to hours. The small size and high solubility make nanobodies uniquely suited for studying protein dynamics by NMR. The ability to produce conformation-sensitive nanobodies in cells enables studies that link structural dynamics of a target protein to its cellular behavior. The link between in vitro and in-cell dynamics, afforded by nanobodies, brings the analysis of such important events as receptor signaling, membrane protein trafficking, and protein interactions to the next level of resolution.
引用
收藏
页码:3767 / 3775
页数:9
相关论文
共 84 条
[1]   Probing the N-Terminal β-Sheet Conversion in the Crystal Structure of the Human Prion Protein Bound to a Nanobody [J].
Abskharon, Romany N. N. ;
Giachin, Gahriele ;
Wohlkonig, Alexandre ;
Soror, Sameh H. ;
Pardon, Els ;
Legname, Giuseppe ;
Steyaert, Jan .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2014, 136 (03) :937-944
[2]   Structure of human Wilson protein domains 5 and 6 and their interplay with domain 4 and the copper chaperone HAM in copper uptake [J].
Achila, D ;
Banci, L ;
Bertini, I ;
Bunce, J ;
Ciofi-Baffoni, S ;
Huffman, DL .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2006, 103 (15) :5729-5734
[3]   Intracellular Expression of Camelid Single-Domain Antibodies Specific for Influenza Virus Nucleoprotein Uncovers Distinct Features of Its Nuclear Localization [J].
Ashour, Joseph ;
Schmidt, Florian I. ;
Hanke, Leo ;
Cragnolini, Juanjo ;
Cavallari, Marco ;
Altenburg, Arwen ;
Brewer, Rebeccah ;
Ingram, Jessica ;
Shoemaker, Charles ;
Ploegh, Hidde L. .
JOURNAL OF VIROLOGY, 2015, 89 (05) :2792-2800
[4]   Metal binding domains 3 and 4 of the Wilson disease protein: solution Structure and interaction with the copper(I) chaperone HAH1 [J].
Banci, Lucia ;
Bertini, Ivano ;
Cantini, Francesca ;
Rosenzweig, Amy C. ;
Yatsunyk, Liliya A. .
BIOCHEMISTRY, 2008, 47 (28) :7423-7429
[5]   An NMR Study of the Interaction of the N-terminal Cytoplasmic Tail of the Wilson Disease Protein with Copper(I)-HAH1 [J].
Banci, Lucia ;
Bertini, Ivano ;
Cantini, Francesca ;
Massagni, Chiara ;
Migliardi, Manuele ;
Rosato, Antonio .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2009, 284 (14) :9354-9360
[6]   Mapping the conformational space accessible to BACE2 using surface mutants and cocrystals with Fab fragments, Fynomers and Xaperones [J].
Banner, David W. ;
Gsell, Bernard ;
Benz, Joerg ;
Bertschinger, Julian ;
Burger, Dominique ;
Brack, Simon ;
Cuppuleri, Simon ;
Debulpaep, Maja ;
Gast, Alain ;
Grabulovski, Dragan ;
Hennig, Michael ;
Hilpert, Hans ;
Huber, Walter ;
Kuglstatter, Andreas ;
Kusznir, Eric ;
Laeremans, Toon ;
Matile, Hugues ;
Miscenic, Christian ;
Rufer, Arne C. ;
Schlatter, Daniel ;
Steyaert, Jan ;
Stihle, Martine ;
Thoma, Ralf ;
Weber, Martin ;
Ruf, Armin .
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2013, 69 :1124-1137
[7]   SbsB structure and lattice reconstruction unveil Ca2+ triggered S-layer assembly [J].
Baranova, Ekaterina ;
Fronzes, Remi ;
Garcia-Pino, Abel ;
Van Gerven, Nani ;
Papapostolou, David ;
Pehau-Arnaudet, Gerard ;
Pardon, Els ;
Steyaert, Jan ;
Howorka, Stefan ;
Remaut, Han .
NATURE, 2012, 487 (7405) :119-+
[8]   Comprehensive analysis of the factors contributing to the stability and solubility of autonomous human VH domains [J].
Barthelemy, Pierre A. ;
Raab, Helga ;
Appleton, Brent A. ;
Bond, Christopher J. ;
Wu, Ping ;
Wiesmann, Christian ;
Sidhu, Sachdev S. .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2008, 283 (06) :3639-3654
[9]   Temporal and spatial organization of ESCRT protein recruitment during HIV-1 budding [J].
Bleck, Marina ;
Itano, Michelle S. ;
Johnson, Daniel S. ;
Thomas, V. Kaye ;
North, Alison J. ;
Bieniasz, Paul D. ;
Simon, Sanford M. .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2014, 111 (33) :12211-12216
[10]   Nanobodies Targeting Mouse/Human VCAM1 for the Nuclear Imaging of Atherosclerotic Lesions [J].
Broisat, Alexis ;
Hernot, Sophie ;
Toczek, Jakub ;
De Vos, Jens ;
Riou, Laurent M. ;
Martin, Sandrine ;
Ahmadi, Mitra ;
Thielens, Nicole ;
Wernery, Ulrich ;
Caveliers, Vicky ;
Muyldermans, Serge ;
Lahoutte, Tony ;
Fagret, Daniel ;
Ghezzi, Catherine ;
Devoogdt, Nick .
CIRCULATION RESEARCH, 2012, 110 (07) :927-937