Crystal structure of the C2 fragment of streptococcal protein G in complex with the Fc domain of human IgG

Sauer‐Eriksson, A. Elisabeth; Kleywegt, Gerard J.; Uhlén, Mathias; Jones, T. Alwyn

doi:10.1016/s0969-2126(01)00157-5

Cited by 345 publications

(315 citation statements)

References 52 publications

(98 reference statements)

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“…Met256 and Met432 are in the CH2-CH3 interface, where residues that are important for the binding to protein A [3], protein G [11], and the neonatal receptor (FcRn) [12] reside. Oxidation of Met256 and Met432 resulted in significant conformational changes in the CH2 domain [3], which decreased binding to protein A and protein G [4].…”

Section: Discussionmentioning

confidence: 99%

Mass spectrometry analysis of photo-induced methionine oxidation of a recombinant human monoclonal antibody

Liu

Gaza-Bulseco

Zhou

2009

J. Am. Soc. Mass Spectrom.

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Oxidation of methionine (Met) residues of a recombinant fully human monoclonal antibody after exposure to light was investigated and compared with chemically induced oxidation using tert-butyl-hydroperoxide (tBHP). Met256 and Met432 in the Fc region in the samples exposed to light or incubated with tBHP were oxidized. The Fc mass spectra of the antibody exposed to light showed mainly peaks with a molecular weight (MW) increase of 32 Da, however the sample treated with tBHP showed peaks with increase of only 16 Da. These results suggested that either oxidation of one Met residue (either Met256 or Met432) catalyzed the oxidation of the second Met residue on the same heavy chain (HC) or Met residues of one HC were preferentially oxidized when the antibody was exposed to light, while Met256 and Met432 were randomly oxidized when the antibody was incubated with tBHP. (J Am Soc Mass Spectrom 2009, 20, 525-528)

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Section: Discussionmentioning

confidence: 99%

Mass spectrometry analysis of photo-induced methionine oxidation of a recombinant human monoclonal antibody

Liu

Gaza-Bulseco

Zhou

2009

J. Am. Soc. Mass Spectrom.

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“…The migration of Fc receptor function may have been a consequence of the need to shift the binding site in the antibody Fc from the C3/C4 interface in the IgY-like ancestor of IgG and IgE, due to competition from bacterial Fc-binding proteins. Such proteins are known to bind to the C␣2/C␣3 interface in IgA (60) and the C␥2/C␥3 interface in IgG (61,62), thereby disabling the immune response by blocking FcR interactions. This selection pressure has led to co-evolution of IgA and its receptor (63); a receptor mutating too slowly to keep up with changing bacterial peptide sequences becomes redundant and may persist only as a pseudogene (as in rabbits) (63) or be eliminated altogether (as in mouse) (64).…”

Section: Discussionmentioning

confidence: 99%

Avian IgY Binds to a Monocyte Receptor with IgG-like Kinetics Despite an IgE-like Structure

Taylor¹,

Gould

Sutton

et al. 2008

Journal of Biological Chemistry

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An ancestor of avian IgY was the evolutionary precursor of mammalian IgG and IgE, and present day chicken IgY performs the function of human IgG despite having the domain structure of human IgE. The kinetics of IgY binding to its receptor on a chicken monocyte cell line, MQ-NCSU, were measured, the first time that the binding of a non-mammalian antibody to a nonmammalian cell has been investigated (k ؉1 ‫؍‬ 1.14 ؎ 0. 46 ). IgE has an extra pair of immunoglobulin domains when compared with IgG. Their presence reduces the dissociation rate of IgE from its receptor 20-fold, thus contributing to the high affinity of IgE. To assess the effect of the equivalent domains on the kinetics of IgY binding, IgY-Fc fragments with and without this domain were cloned and expressed in mammalian cells. In contrast to IgE, their presence in IgY has little effect on the association rate and no effect on dissociation. Whatever the function of this extra domain pair in avian IgY, it has persisted for at least 310 million years and has been co-opted in mammalian IgE to generate a uniquely slow dissociation rate and high affinity.IgY is the principal serum antibody of amphibians, reptiles, and birds and shares a common ancestor with both mammalian IgG and IgE (1, 2). The cDNA sequence of the chicken upsilon () heavy chain (3) reveals that, like more basal amphibian IgY (4, 5), avian IgY contains a domain pair (C2) 4 that has been conserved in mammalian IgE (as C⑀2) but truncated to form the "hinge" region in mammalian IgG (3). Thus, an orthologous domain pair must have existed in the common (IgY-like) ancestor prior to its duplication and subsequent divergence in the mammalian lineage. Avian IgY is the closest extant protein to this ancestor and therefore the most logical choice for study of the evolution of modern IgG and IgE from an ancient IgY-like ancestor.IgG, the principal mammalian serum antibody, aggregates and facilitates opsonization of antigens, activates complement, and provides protection for the fetus following transport across the placenta. IgE does not activate complement nor cross the placenta but can sensitize effector cells (principally mast cells and basophils) and typically mediates anaphylactic reactions (6). It is well known for its involvement in allergic disease but probably also provides defense against parasitic infections (7).Avian IgY appears to combine the functions of mammalian IgG and IgE. As the major serum antibody, it provides defense against infection (8) but also mediates anaphylaxis (9). Chicken mast cells activated by IgY are responsible for local anaphylactic reactions in the gut, which play a role in defense against protozoan infections (10, 11). Antibody-dependent hypersensitivity and fatal systemic anaphylactic shock have also been demonstrated in chickens (9, 12, 13) and shown to be mediated by basophils (14), which are much more numerous than mast cells in birds (in contrast to mammals in which the reverse is true) (15). These phenomena constitute indirect evidence for the presence of IgY...

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“…In addition, also the *Corresponding author. Fax: (46) (8) 6954084. structures of SPG immunoglobulin-binding domains in complex with Fab [18] or Fc [19] have been described. The structure of an individual domain consists of a mixed parallel/antiparallel fl-sheet of four strands, with a single c~-helix packed onto the sheet.…”

Section: Introductionmentioning

confidence: 99%

The serum albumin‐binding domain of streptococcal protein G is a three‐helical bundle: a heteronuclear NMR study

Kraulis¹,

Jonasson

Nygren

et al. 1996

FEBS Letters

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Crystal structure of the C2 fragment of streptococcal protein G in complex with the Fc domain of human IgG

Cited by 345 publications

References 52 publications

Mass spectrometry analysis of photo-induced methionine oxidation of a recombinant human monoclonal antibody

Mass spectrometry analysis of photo-induced methionine oxidation of a recombinant human monoclonal antibody

Avian IgY Binds to a Monocyte Receptor with IgG-like Kinetics Despite an IgE-like Structure

The serum albumin‐binding domain of streptococcal protein G is a three‐helical bundle: a heteronuclear NMR study

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