NDLI: Engineered Human Antibody Constant Domains with Increased Stability

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Engineered Human Antibody Constant Domains with Increased Stability

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Engineered Human Antibody Constant Domains with Increased Stability

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Tarasov, Sergey G. Vu, Bang K. Feng, Yang Walsh, Joseph D. Prabakaran, Ponraj Veenstra, Timothy D. Ishima, Rieko Gong, Rui Prieto, Darue A. Dimitrov, Dimiter S. Dyba, Marzena A.
Description	Author Affiliation: Gong R ( Protein Interactions Group, CCRNP, CCR, National Institutes of Health, Frederick, Maryland 21702, USA.)
Abstract	The immunoglobulin (Ig) constant CH2 domain is critical for antibody effector functions. Isolated CH2 domains are promising as scaffolds for construction of libraries containing diverse binders that could also confer some effector functions. However, previous work has shown that an isolated murine CH2 domain is relatively unstable to thermally induced unfolding. To explore unfolding mechanisms of isolated human CH2 and increase its stability gamma1 CH2 was cloned and a panel of cysteine mutants was constructed. Human gamma1 CH2 unfolded at a higher temperature (T(m) = 54.1 degrees C, as measured by circular dichroism) than that previously reported for a mouse CH2 (41 degrees C). One mutant (m01) was remarkably stable (T(m) = 73.8 degrees C). Similar results were obtained by differential scanning calorimetry. This mutant was also significantly more stable than the wild-type CH2 against urea induced unfolding (50% unfolding at urea concentration of 6.8 m versus 4.2 m). The m01 was highly soluble and monomeric. The existence of the second disulfide bond in m01 and its correct position were demonstrated by mass spectrometry and nuclear magnetic resonance spectroscopy, respectively. The loops were on average more flexible than the framework in both CH2 and m01, and the overall secondary structure was not affected by the additional disulfide bond. These data suggest that a human CH2 domain is relatively stable to unfolding at physiological temperature, and that both CH2 and the highly stable mutant m01 are promising new scaffolds for the development of therapeutics against human diseases.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	21
Volume Number	284
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2009-05-22
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Immunoglobulin Constant Regions Chemistry Immunoglobulin G Protein Engineering Amino Acid Sequence Calorimetry, Differential Scanning Circular Dichroism Disulfides Glycosylation Magnetic Resonance Spectroscopy Mass Spectrometry Molecular Sequence Data Mutant Proteins Pliability Protein Stability Protein Structure, Secondary Protein Structure, Tertiary Sequence Alignment Research Support, N.I.H., Extramural Research Support, N.I.H., Intramural Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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