Human Antibody Effector Function

Dennis R. Burton (Lead / Corresponding author), Jenny M. Woof

Research output: Contribution to journalArticle

211 Citations (Scopus)

Abstract

This chapter focuses on human antibody effector function. A molecular explanation of antibody effector function requires the description of multiple antibody molecules cross-linking an array of antigen molecules to multiple effector molecules. The antigen molecules are likely to be on a cell surface and the effector molecules are either large, as for complement, or on a cell surface, as for fragment crystallizable (Fc) receptors. The chapter presents crystal structures for (1) Fab fragments, (2) Fab fragments complexed with a number of antigens, and (3) Fc from immunoglobulin (IgG). It also has the low-resolution structures of two mutant whole IgG molecules. These mutant molecules lack the hinge region and generally show poor effector activity. They crystallize and show a complete diffraction pattern because the loss of the hinge reduces their flexibility. The crystal structures of human and rabbit Fc from IgG are determined to intermediate resolution and analyzed in detail in terms of potential interacting sites. The chapter discusses complement activation by antibodies. The complement cascade can be usefully divided into two phases: (1) the deposition of C3 on the antigenic cell surface, thereby facilitating phagocytosis, in the classical pathway this requires the sequential activation of C1 and C42, (2) the formation of the membrane attack complex resulting in cell lysis, this requires the activation of C5 and attachment of C6–9.

Original languageEnglish
Pages (from-to)1-84
Number of pages84
JournalAdvances in Immunology
Volume51
DOIs
Publication statusPublished - 1992

Fingerprint

Immunoglobulin Fab Fragments
Antibodies
Immunoglobulin G
Antigens
Complement Membrane Attack Complex
Immunoglobulin Fragments
Complement Activation
Phagocytosis
Rabbits

Cite this

Burton, Dennis R. ; Woof, Jenny M. / Human Antibody Effector Function. In: Advances in Immunology. 1992 ; Vol. 51. pp. 1-84.
@article{b9359a07e86a414daebedaf643cc1b2a,
title = "Human Antibody Effector Function",
abstract = "This chapter focuses on human antibody effector function. A molecular explanation of antibody effector function requires the description of multiple antibody molecules cross-linking an array of antigen molecules to multiple effector molecules. The antigen molecules are likely to be on a cell surface and the effector molecules are either large, as for complement, or on a cell surface, as for fragment crystallizable (Fc) receptors. The chapter presents crystal structures for (1) Fab fragments, (2) Fab fragments complexed with a number of antigens, and (3) Fc from immunoglobulin (IgG). It also has the low-resolution structures of two mutant whole IgG molecules. These mutant molecules lack the hinge region and generally show poor effector activity. They crystallize and show a complete diffraction pattern because the loss of the hinge reduces their flexibility. The crystal structures of human and rabbit Fc from IgG are determined to intermediate resolution and analyzed in detail in terms of potential interacting sites. The chapter discusses complement activation by antibodies. The complement cascade can be usefully divided into two phases: (1) the deposition of C3 on the antigenic cell surface, thereby facilitating phagocytosis, in the classical pathway this requires the sequential activation of C1 and C42, (2) the formation of the membrane attack complex resulting in cell lysis, this requires the activation of C5 and attachment of C6–9.",
author = "Burton, {Dennis R.} and Woof, {Jenny M.}",
year = "1992",
doi = "10.1016/S0065-2776(08)60486-1",
language = "English",
volume = "51",
pages = "1--84",
journal = "Advances in Immunology",
issn = "0065-2776",
publisher = "Academic Press Inc.",

}

Human Antibody Effector Function. / Burton, Dennis R. (Lead / Corresponding author); Woof, Jenny M.

In: Advances in Immunology, Vol. 51, 1992, p. 1-84.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Human Antibody Effector Function

AU - Burton, Dennis R.

AU - Woof, Jenny M.

PY - 1992

Y1 - 1992

N2 - This chapter focuses on human antibody effector function. A molecular explanation of antibody effector function requires the description of multiple antibody molecules cross-linking an array of antigen molecules to multiple effector molecules. The antigen molecules are likely to be on a cell surface and the effector molecules are either large, as for complement, or on a cell surface, as for fragment crystallizable (Fc) receptors. The chapter presents crystal structures for (1) Fab fragments, (2) Fab fragments complexed with a number of antigens, and (3) Fc from immunoglobulin (IgG). It also has the low-resolution structures of two mutant whole IgG molecules. These mutant molecules lack the hinge region and generally show poor effector activity. They crystallize and show a complete diffraction pattern because the loss of the hinge reduces their flexibility. The crystal structures of human and rabbit Fc from IgG are determined to intermediate resolution and analyzed in detail in terms of potential interacting sites. The chapter discusses complement activation by antibodies. The complement cascade can be usefully divided into two phases: (1) the deposition of C3 on the antigenic cell surface, thereby facilitating phagocytosis, in the classical pathway this requires the sequential activation of C1 and C42, (2) the formation of the membrane attack complex resulting in cell lysis, this requires the activation of C5 and attachment of C6–9.

AB - This chapter focuses on human antibody effector function. A molecular explanation of antibody effector function requires the description of multiple antibody molecules cross-linking an array of antigen molecules to multiple effector molecules. The antigen molecules are likely to be on a cell surface and the effector molecules are either large, as for complement, or on a cell surface, as for fragment crystallizable (Fc) receptors. The chapter presents crystal structures for (1) Fab fragments, (2) Fab fragments complexed with a number of antigens, and (3) Fc from immunoglobulin (IgG). It also has the low-resolution structures of two mutant whole IgG molecules. These mutant molecules lack the hinge region and generally show poor effector activity. They crystallize and show a complete diffraction pattern because the loss of the hinge reduces their flexibility. The crystal structures of human and rabbit Fc from IgG are determined to intermediate resolution and analyzed in detail in terms of potential interacting sites. The chapter discusses complement activation by antibodies. The complement cascade can be usefully divided into two phases: (1) the deposition of C3 on the antigenic cell surface, thereby facilitating phagocytosis, in the classical pathway this requires the sequential activation of C1 and C42, (2) the formation of the membrane attack complex resulting in cell lysis, this requires the activation of C5 and attachment of C6–9.

UR - http://www.scopus.com/inward/record.url?scp=0026657624&partnerID=8YFLogxK

U2 - 10.1016/S0065-2776(08)60486-1

DO - 10.1016/S0065-2776(08)60486-1

M3 - Article

C2 - 1502974

AN - SCOPUS:0026657624

VL - 51

SP - 1

EP - 84

JO - Advances in Immunology

JF - Advances in Immunology

SN - 0065-2776

ER -