Literature DB >> 10224373

The apparent monovalency of human IgG4 is due to bispecificity.

R C Aalberse1, J Schuurman, R van Ree.   

Abstract

A hypothesis is put forward to explain the apparent monovalency of human IgG4. It is based upon the known instability of the IgG4 hinge. IgG4 is secreted as a regular bivalent antibody, but after secretion interacts with another IgG4 molecule. This interaction results in the exchange of half molecules (a combination of one heavy chain and one light chain) between the two IgG4 molecules. The postulated bispecific IgG4 antibodies can indeed be found in selected human sera following repeated immunization with two non-crossreacting antigens.

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Year:  1999        PMID： 10224373     DOI： 10.1159/000024062

Source DB:  PubMed          Journal:  Int Arch Allergy Immunol        ISSN： 1018-2438            Impact factor:   2.749


  7 in total

1.  IgG4 production against adalimumab during long term treatment of RA patients.

Authors:  Pauline A van Schouwenburg; Charlotte L Krieckaert; Michael Nurmohamed; Margreet Hart; Theo Rispens; Lucien Aarden; Diana Wouters; Gerrit Jan Wolbink
Journal:  J Clin Immunol       Date:  2012-05-24       Impact factor: 8.317

2.  Immunogenicity and efficacy of Cryptococcus neoformans capsular polysaccharide glucuronoxylomannan peptide mimotope-protein conjugates in human immunoglobulin transgenic mice.

Authors:  Robert W Maitta; Kausik Datta; Andrew Lees; Shelley Sims Belouski; Liise-anne Pirofski
Journal:  Infect Immun       Date:  2004-01       Impact factor: 3.441

3.  Production of native bispecific antibodies in rabbits.

Authors:  Wei Wang; Ruihuan Xu; Jinming Li
Journal:  PLoS One       Date:  2010-06-14       Impact factor: 3.240

4.  Identification of natural bispecific antibodies against cyclic citrullinated peptide and immunoglobulin G in rheumatoid arthritis.

Authors:  Wei Wang; Jinming Li
Journal:  PLoS One       Date:  2011-01-27       Impact factor: 3.240

Review 5.  An Overview of the Relevance of IgG4 Antibodies in Allergic Disease with a Focus on Food Allergens.

Authors:  Thomas A E Platts-Mills; Behnam Keshavarz; Jeffrey M Wilson; Rung-Chi Li; Peter W Heymann; Diane R Gold; Emily C McGowan; Elizabeth A Erwin
Journal:  Children (Basel)       Date:  2021-05-20

6.  Dynamics of inter-heavy chain interactions in human immunoglobulin G (IgG) subclasses studied by kinetic Fab arm exchange.

Authors:  Theo Rispens; Anna M Davies; Pleuni Ooijevaar-de Heer; Samira Absalah; Onno Bende; Brian J Sutton; Gestur Vidarsson; Rob C Aalberse
Journal:  J Biol Chem       Date:  2014-01-14       Impact factor: 5.157

7.  The Fab conformations in the solution structure of human immunoglobulin G4 (IgG4) restrict access to its Fc region: implications for functional activity.

Authors:  Lucy E Rayner; Gar Kay Hui; Jayesh Gor; Richard K Heenan; Paul A Dalby; Stephen J Perkins
Journal:  J Biol Chem       Date:  2014-05-29       Impact factor: 5.157
  7 in total

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