Monoclonal antibodies for the structural analysis of the Na+/H+ antiporter NhaA 
from Escherichia coli

Venturi, Miro; Hunte, Carola

doi:10.1016/S0005-2736(02)00713-7

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Monoclonal antibodies for the structural analysis of the Na⁺/H⁺ antiporter NhaA from Escherichia coli

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Hunte, Carola
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Venturi, M., & Hunte, C. (2003). Monoclonal antibodies for the structural analysis of the Na⁺/H⁺ antiporter NhaA from Escherichia coli. Biochimica et Biophysica Acta-Biomembranes, 1610(1), 46-50. doi:10.1016/S0005-2736(02)00713-7.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-DB88-4

Abstract

Since their advent some 25 years ago, monoclonal antibodies have developed into powerful tools for structural and functional analysis of their cognate antigens. Together with the respective antigen binding fragments, antibodies offer exclusive capacities in detection, characterization, purification and functional assays for every given ligand.

Antibody-fragment mediated crystallization represents a major advance in determining the three-dimensional structure of membrane-bound protein complexes. In this review, we focus on the methods used to generate monoclonal antibodies against the NhaA antiporter from Escherichia coli as a paradigm of secondary transporters. We describe examples on how antibodies are helpful in understanding structure and function relationships for this important class of integral membrane proteins.

The generated conformation-specific antibody fragments are highly valuable reagents for co-crystallization attempts and structure determination of the antiporter.