Association of the anti-hen egg lysozyme antibody HyHEL-5 with avian species variant and mutant lysozymes

Kari A. Shick; K. Asish Xavier; Arvind Rajpal; Sandra J. Smith-Gill; Richard C. Willson

doi:10.1016/S0167-4838(97)00035-6

Association of the anti-hen egg lysozyme antibody HyHEL-5 with avian species variant and mutant lysozymes

Kari A. Shick, K. Asish Xavier, Arvind Rajpal, Sandra J. Smith-Gill, Richard C. Willson

Houston Methodist

Research output: Contribution to journal › Article › peer-review

20 Scopus citations

Abstract

The energetics of association of the murine anti-hen egg lysozyme antibody HyHEL-5 with bobwhite quail lysozyme, California quail lysozyme, and the Arg45 → Lys mutant of hen egg lysozyme was characterized by isothermal titration calorimetry. The association of each lysozyme with HyHEL-5 is enthalpically driven in the temperature range 10°C to 37°C. The calorimetric results indicate that the salt-links between Arg45 and Arg68 of hen egg lysozyme and GluH50 on the HyHEL-5 paratope are energetically important in HyHEL-5/HEL association. In contrast to previous studies, the results suggest that the three characteristic 'quail' mutations affect the energetics of antibody/antigen association, even though they ace buried and not in direct contact with the antibody.

Original language	English (US)
Pages (from-to)	205-214
Number of pages	10
Journal	Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Volume	1340
Issue number	2
DOIs	https://doi.org/10.1016/S0167-4838(97)00035-6
State	Published - Jul 18 1997

Keywords

Antibody
Calorimetry
Enthalpy
Lysozyme
Molecular recognition

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Structural Biology
Biophysics

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10.1016/S0167-4838(97)00035-6

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@article{0a1a1b33dfaa4045ac60739b5b625ab9,

title = "Association of the anti-hen egg lysozyme antibody HyHEL-5 with avian species variant and mutant lysozymes",

abstract = "The energetics of association of the murine anti-hen egg lysozyme antibody HyHEL-5 with bobwhite quail lysozyme, California quail lysozyme, and the Arg45 → Lys mutant of hen egg lysozyme was characterized by isothermal titration calorimetry. The association of each lysozyme with HyHEL-5 is enthalpically driven in the temperature range 10°C to 37°C. The calorimetric results indicate that the salt-links between Arg45 and Arg68 of hen egg lysozyme and GluH50 on the HyHEL-5 paratope are energetically important in HyHEL-5/HEL association. In contrast to previous studies, the results suggest that the three characteristic 'quail' mutations affect the energetics of antibody/antigen association, even though they ace buried and not in direct contact with the antibody.",

keywords = "Antibody, Calorimetry, Enthalpy, Lysozyme, Molecular recognition",

author = "Shick, \{Kari A.\} and Xavier, \{K. Asish\} and Arvind Rajpal and Smith-Gill, \{Sandra J.\} and Willson, \{Richard C.\}",

note = "Funding Information: The ITC work was supported by the Office of Naval Research under the Accelerated Research Initiative in Molecular Recognition, by the Welch Foundation and by NIH Grant GM44344 to R.C.W. The lysozyme mutagenesis work was supported by the Director, Office of Energy Research, Office of Basic Energy Sciences, Divisions of Material Sciences and of Energy Biosciences of the US Department of Energy under contract \#DE-AC03-76SF00098 (Principal investigator Dr. Jack F. Kirsch). We thank Drs. Andrew McCammon, Shawn McDonald, Shankar Subramaniam, Susan Chacko, Gerson Cohen and Steven Sheriff for helpful discussions, Dr. Ellen Prager for the generous gift of purified BWQL and CQL and Dr. Mark Hirschel for advice on cell culture. We thank Dr. John Brandts and the late Thomas Wiseman of MicroCal, Inc. for advice on calorimetric experiments. We thank Dr. Mohan Srinivasan for preparing the illustration of the HyHEL-5 Fab/BWQL complex. ",

year = "1997",

month = jul,

day = "18",

doi = "10.1016/S0167-4838(97)00035-6",

language = "English (US)",

volume = "1340",

pages = "205--214",

journal = "Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology",

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TY - JOUR

T1 - Association of the anti-hen egg lysozyme antibody HyHEL-5 with avian species variant and mutant lysozymes

AU - Shick, Kari A.

AU - Xavier, K. Asish

AU - Rajpal, Arvind

AU - Smith-Gill, Sandra J.

AU - Willson, Richard C.

N1 - Funding Information: The ITC work was supported by the Office of Naval Research under the Accelerated Research Initiative in Molecular Recognition, by the Welch Foundation and by NIH Grant GM44344 to R.C.W. The lysozyme mutagenesis work was supported by the Director, Office of Energy Research, Office of Basic Energy Sciences, Divisions of Material Sciences and of Energy Biosciences of the US Department of Energy under contract #DE-AC03-76SF00098 (Principal investigator Dr. Jack F. Kirsch). We thank Drs. Andrew McCammon, Shawn McDonald, Shankar Subramaniam, Susan Chacko, Gerson Cohen and Steven Sheriff for helpful discussions, Dr. Ellen Prager for the generous gift of purified BWQL and CQL and Dr. Mark Hirschel for advice on cell culture. We thank Dr. John Brandts and the late Thomas Wiseman of MicroCal, Inc. for advice on calorimetric experiments. We thank Dr. Mohan Srinivasan for preparing the illustration of the HyHEL-5 Fab/BWQL complex.

PY - 1997/7/18

Y1 - 1997/7/18

N2 - The energetics of association of the murine anti-hen egg lysozyme antibody HyHEL-5 with bobwhite quail lysozyme, California quail lysozyme, and the Arg45 → Lys mutant of hen egg lysozyme was characterized by isothermal titration calorimetry. The association of each lysozyme with HyHEL-5 is enthalpically driven in the temperature range 10°C to 37°C. The calorimetric results indicate that the salt-links between Arg45 and Arg68 of hen egg lysozyme and GluH50 on the HyHEL-5 paratope are energetically important in HyHEL-5/HEL association. In contrast to previous studies, the results suggest that the three characteristic 'quail' mutations affect the energetics of antibody/antigen association, even though they ace buried and not in direct contact with the antibody.

AB - The energetics of association of the murine anti-hen egg lysozyme antibody HyHEL-5 with bobwhite quail lysozyme, California quail lysozyme, and the Arg45 → Lys mutant of hen egg lysozyme was characterized by isothermal titration calorimetry. The association of each lysozyme with HyHEL-5 is enthalpically driven in the temperature range 10°C to 37°C. The calorimetric results indicate that the salt-links between Arg45 and Arg68 of hen egg lysozyme and GluH50 on the HyHEL-5 paratope are energetically important in HyHEL-5/HEL association. In contrast to previous studies, the results suggest that the three characteristic 'quail' mutations affect the energetics of antibody/antigen association, even though they ace buried and not in direct contact with the antibody.

KW - Antibody

KW - Calorimetry

KW - Enthalpy

KW - Lysozyme

KW - Molecular recognition

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U2 - 10.1016/S0167-4838(97)00035-6

DO - 10.1016/S0167-4838(97)00035-6

M3 - Article

C2 - 9252107

AN - SCOPUS:0041009405

SN - 0167-4838

VL - 1340

SP - 205

EP - 214

JO - Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

JF - Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

IS - 2

ER -

Association of the anti-hen egg lysozyme antibody HyHEL-5 with avian species variant and mutant lysozymes

Abstract

Keywords

ASJC Scopus subject areas

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