BIOMAT Database Logo BIOMAT Database Logo

Synthetic peptides from mouse Fc receptor (MoFc gamma RII) that alter the binding of IgG to MoFc gamma RII. 1997

E B Goldsmith, and B W Erickson, and N L Thompson
Department of Chemistry, University of North Carolina, Chapel Hill 27599-3290, USA.

Fc receptors are transmembrane proteins, found on the surfaces of immune cells, that aid in the removal of foreign pathogens by binding to antibody-coated targets via the Fc regions of the antibodies. Using peptides synthesized on pins, overlapping dodecapeptides (170) were synthesized to cover the extracellular region of the mouse Fc receptor for IgG, moFc gamma RII. The peptides were screened for antibody binding activity by using multivalent immune complexes composed of anti-dinitrophenyl monoclonal mouse IgG1 (ANO6) and dinitrophenyl conjugated to human serum albumin (DNP-HSA). Assays were also carried out with an anti-moFc gamma RII monoclonal rat IgG (2.4G2). The peptides that interacted with these antibodies prompted the synthesis of two soluble peptides: peptide A [Fc gamma RII-(108-119), RCHSWRNKLLNRamide] and peptide B [Fc gamma RII-(153-165), CKGSLGRTLHQSKamide]. Monomeric S-alkylated (A, B), homodimeric (AA, BB), heterodimeric (AB), and scrambled homodimeric (CC, DD) forms of these peptides were synthesized and examined for their ability to inhibit immune-complex binding to immobilized soluble Fc gamma RII. Peptides AA and CC completely inhibited immune-complex binding while each of the other peptides partially inhibited binding (AB, 80%; A, 80%; BB, 65%; DD, 64%; B, 52%). The pair of monomeric moFc gamma RII peptides and the set of five dimeric peptides showed the same increase in binding inhibition with increasing net positive charge per residue. These results suggest that the Fc region of IgG binds to the solvent-exposed B/C and F/G loops of the moFc gamma RII receptor through predominantly electrostatic forces.

UI MeSH Term Description Entries
D007074 Immunoglobulin G The major immunoglobulin isotype class in normal human serum. There are several isotype subclasses of IgG, for example, IgG1, IgG2A, and IgG2B. Gamma Globulin, 7S,IgG,IgG Antibody,Allerglobuline,IgG(T),IgG1,IgG2,IgG2A,IgG2B,IgG3,IgG4,Immunoglobulin GT,Polyglobin,7S Gamma Globulin,Antibody, IgG,GT, Immunoglobulin
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009842 Oligopeptides Peptides composed of between two and twelve amino acids. Oligopeptide
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D011994 Recombinant Proteins Proteins prepared by recombinant DNA technology. Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA
D006224 Cricetinae A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS. Cricetus,Hamsters,Hamster
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D000936 Antigen-Antibody Complex The complex formed by the binding of antigen and antibody molecules. The deposition of large antigen-antibody complexes leading to tissue damage causes IMMUNE COMPLEX DISEASES. Immune Complex,Antigen-Antibody Complexes,Immune Complexes,Antigen Antibody Complex,Antigen Antibody Complexes,Complex, Antigen-Antibody,Complex, Immune,Complexes, Antigen-Antibody,Complexes, Immune

Related Publications

E B Goldsmith, and B W Erickson, and N L Thompson
Functional mapping of the Fc gamma RII binding site on human IgG1 by synthetic peptides.
April 2004, European journal of immunology,
E B Goldsmith, and B W Erickson, and N L Thompson
Human epidermal Langerhans cells secrete a soluble receptor for IgG (Fc gamma RII/CD32) that inhibits the binding of immune complexes to Fc gamma R+ cells.
January 1994, Journal of immunology (Baltimore, Md. : 1950),
E B Goldsmith, and B W Erickson, and N L Thompson
Multiple regions of human Fc gamma RII (CD32) contribute to the binding of IgG.
September 1995, The Journal of biological chemistry,
E B Goldsmith, and B W Erickson, and N L Thompson
The Fc receptor for IgG (Fc gamma RII; CD32) on human neonatal B lymphocytes.
July 2001, Human immunology,
E B Goldsmith, and B W Erickson, and N L Thompson
Direct demonstration of binding of aggregated mouse IgG1 to the 40-kDa Fc receptor for IgG (Fc gamma RII) in both high and low responders.
April 1992, Immunology letters,
E B Goldsmith, and B W Erickson, and N L Thompson
Binding of the soluble, truncated form of an Fc receptor (mouse Fc gamma RII) to membrane-bound IgG as measured by total internal reflection fluorescence microscopy.
January 1997, Journal of molecular recognition : JMR,
E B Goldsmith, and B W Erickson, and N L Thompson
Human basophils selectively express the Fc gamma RII (CDw32) subtype of IgG receptor.
December 1989, The Journal of allergy and clinical immunology,
E B Goldsmith, and B W Erickson, and N L Thompson
Effect of protease inhibitors on human monocyte IgG Fc receptor II. Evidence that serine esterase activity is essential for Fc gamma RII-mediated binding.
September 1990, Journal of immunology (Baltimore, Md. : 1950),
E B Goldsmith, and B W Erickson, and N L Thompson
Murine soluble Fc gamma receptors/IgG-binding factors (IgG-BF): analysis of the relation to Fc gamma RII and production of milligram quantities of biologically active recombinant IgG-BF.
January 1992, Immunologic research,
E B Goldsmith, and B W Erickson, and N L Thompson
Dissociation kinetics between a mouse Fc receptor (Fc gamma RII) and IgG: measurement by total internal reflection with fluorescence photobleaching recovery.
September 1995, Biochemistry,
Copied contents to your clipboard!