Decreased IgG-FcyRII dissociation kinetics in the presence of a protein antigen

Erin D. Sheets; Lixin Chen; Nancy L. Thompson

doi:10.1016/S0161-5890(97)00057-6

Decreased IgG-FcyRII dissociation kinetics in the presence of a protein antigen

Erin D. Sheets, Lixin Chen, Nancy L. Thompson

Chemistry & Biochemistry

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4 Scopus citations

Abstract

Total internal reflection fluorescence microscopy has been used to examine the interaction of a mouse monoclonal IgG2b, in the absence and presence of its protein antigen, with mouse FcyRII in substrate-supported planar membranes. Equilibrium association and kinetic dissociation constants were measured for the antibody S6-34.11, which is specific for bovine prothrombin fragment 1 (BF1). These measurements showed that BF1 induces a statistically significant decrease (30-40%) in the IgG-FcyRII dissociation kinetics. A corresponding increase in the equilibrium association constant was not observed, perhaps because the statistical accuracy of the equilibrium measurements is lower than that for the kinetic measurements. The consequences of these results for understanding the mechanism by which macrophages recognize and ingest opsonized targets are discussed.

Original language	English (US)
Pages (from-to)	519-526
Number of pages	8
Journal	Molecular Immunology
Volume	34
Issue number	7
DOIs	https://doi.org/10.1016/S0161-5890(97)00057-6
State	Published - May 1997

Bibliographical note

Funding Information:
Ackrlowlengonenrs--We thank David Klapper, Sawsun Mahassni and Richard Hiskey (University of North Carolina at Chapel Hill) for the S6-34.11 hybridoma, Betty Diamond (Albert Einstein College of Medicine) for the 2.462 hybridoma. Harden M. McConnell (Stanford University) for the AN05 hybridoma, Pola Berkowitz and Richard Hiskey (University of North Carolina at Chapel Hill) for bovine prothrombin fragment 1, and Christian R. Lombard0 (University of North Carolina at Chapel Hill) for assistancew ith BIAcore measurement and analysis. We also thank Edie B. Goldsmith. HeleVn. Hsieh, Evalonda Moore and Jean Wang for assistance with biochemical preparations. This work was supported by National Institutes of Health Grant GM-37145 and National Science Foundation Grant GER-9024028.

Keywords

Antibody-antigen interactions
Evanescent wave
Fc receptors
Fluorescence microscopy
Fluorescence photobleaching recovery
Substrate-supported planar membranes
Total internal reflection

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title = "Decreased IgG-FcyRII dissociation kinetics in the presence of a protein antigen",

abstract = "Total internal reflection fluorescence microscopy has been used to examine the interaction of a mouse monoclonal IgG2b, in the absence and presence of its protein antigen, with mouse FcyRII in substrate-supported planar membranes. Equilibrium association and kinetic dissociation constants were measured for the antibody S6-34.11, which is specific for bovine prothrombin fragment 1 (BF1). These measurements showed that BF1 induces a statistically significant decrease (30-40%) in the IgG-FcyRII dissociation kinetics. A corresponding increase in the equilibrium association constant was not observed, perhaps because the statistical accuracy of the equilibrium measurements is lower than that for the kinetic measurements. The consequences of these results for understanding the mechanism by which macrophages recognize and ingest opsonized targets are discussed.",

keywords = "Antibody-antigen interactions, Evanescent wave, Fc receptors, Fluorescence microscopy, Fluorescence photobleaching recovery, Substrate-supported planar membranes, Total internal reflection",

author = "Sheets, {Erin D.} and Lixin Chen and Thompson, {Nancy L.}",

note = "Funding Information: Ackrlowlengonenrs--We thank David Klapper, Sawsun Mahassni and Richard Hiskey (University of North Carolina at Chapel Hill) for the S6-34.11 hybridoma, Betty Diamond (Albert Einstein College of Medicine) for the 2.462 hybridoma. Harden M. McConnell (Stanford University) for the AN05 hybridoma, Pola Berkowitz and Richard Hiskey (University of North Carolina at Chapel Hill) for bovine prothrombin fragment 1, and Christian R. Lombard0 (University of North Carolina at Chapel Hill) for assistancew ith BIAcore measurement and analysis. We also thank Edie B. Goldsmith. HeleVn. Hsieh, Evalonda Moore and Jean Wang for assistance with biochemical preparations. This work was supported by National Institutes of Health Grant GM-37145 and National Science Foundation Grant GER-9024028.",

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N2 - Total internal reflection fluorescence microscopy has been used to examine the interaction of a mouse monoclonal IgG2b, in the absence and presence of its protein antigen, with mouse FcyRII in substrate-supported planar membranes. Equilibrium association and kinetic dissociation constants were measured for the antibody S6-34.11, which is specific for bovine prothrombin fragment 1 (BF1). These measurements showed that BF1 induces a statistically significant decrease (30-40%) in the IgG-FcyRII dissociation kinetics. A corresponding increase in the equilibrium association constant was not observed, perhaps because the statistical accuracy of the equilibrium measurements is lower than that for the kinetic measurements. The consequences of these results for understanding the mechanism by which macrophages recognize and ingest opsonized targets are discussed.

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Decreased IgG-FcyRII dissociation kinetics in the presence of a protein antigen

Abstract

Bibliographical note

Keywords

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