NDLI: High-resolution mapping of the HyHEL-10 epitope of chicken lysozyme by site-directed mutagenesis.

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High-resolution mapping of the HyHEL-10 epitope of chicken lysozyme by site-directed mutagenesis.

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High-resolution mapping of the HyHEL-10 epitope of chicken lysozyme by site-directed mutagenesis.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Zhang, L. Wilson, A. C. Taylor, M. G. Kam-morgan, L. N. Smith-gill, S. J. Kirsch, J. F.
Description	Author Affiliation: Kam-Morgan LN ( Department of Molecular and Cell Biology, University of California, Berkeley 94720.);
Abstract	The complex formed between hen egg white lysozyme (HEL) and the monoclonal antibody HyHEL-10 Fab fragment has an interface composed of van der Waals interactions, hydrogen bonds, and a single ion pair. The antibody overlaps part of the active site cleft. Putative critical residues within the epitope region of HEL, identified from the x-ray crystallographic structure of the complex, were replaced by site-directed mutagenesis to probe their relative importance in determining affinity of the antibody for HEL. Twenty single mutations of HEL at three contact residues (Arg-21HEL, Asp-101HEL, and Gly-102HEL) and at a partially buried residue (Asn-19HEL) in the epitope were made, and the effects on the free energies of dissociation were measured. A correlation between increased amino acid side-chain volume and reduced affinity for HELs with mutations at position 101 was observed. The D101GHEL mutant is bound to HyHEL-10 as tightly as wild-type enzyme, but the delta delta Gdissoc is increased by about 2.2 kcal (9.2 kJ)/mol for the larger residues in this position. HEL variants with lysine or histidine replacements for arginine at position 21 are bound 1.4-2.7 times more tightly than those with neutral or negatively charged amino acids in this position. These exhibit 1/40 the affinity for HyHEL-10 Fab compared with wild type. There is no side-chain volume correlation with delta delta Gdissoc at position 21. Although Gly-102HEL and Asn-19HEL are in the epitope, replacements at these positions have no effect on the affinity of HEL for the antibody.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	9
Volume Number	90
Language	English
Publisher	National Academy of Sciences
Publisher Date	1993-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Antibodies, Monoclonal Metabolism Epitopes Muramidase Amino Acid Sequence Animals Binding Sites, Antibody Binding, Competitive Chemistry Genetics Kinetics Mathematics Mutagenesis, Site-Directed Thermodynamics Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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