Human IgG2 Can Form Covalent Dimers | Zendy

Esther M. Yoo | Zendy; Letitia A. Wims | Zendy; Lisa A. Chan | Zendy; Sherie L. Morrison | Zendy

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Human IgG2 Can Form Covalent Dimers

Author(s) -

Esther M. Yoo,

Letitia A. Wims,

Lisa A. Chan,

Sherie L. Morrison

Publication year - 2003

Publication title -

the journal of immunology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.737

H-Index - 372

eISSN - 1550-6606

pISSN - 0022-1767

DOI - 10.4049/jimmunol.170.6.3134

Subject(s) - covalent bond , dimer , chemistry , cyanogen bromide , recombinant dna , cleavage (geology) , non covalent interactions , antibody , immunoglobulin g , immunoglobulin light chain , biochemistry , biology , peptide sequence , gene , immunology , molecule , paleontology , hydrogen bond , organic chemistry , fracture (geology)

Unlike IgA and IgM, IgG has not yet been shown to form covalent polymers. However in the presence of specific Ag, murine IgG3 has been shown to polymerize through noncovalent interactions. In contrast to the noncovalent oligomers found with murine IgG3, we have detected covalent dimers in three different recombinant human IgG2 Abs produced in myeloma cells. Both IgG2,kappa and IgG2,lambda can form dimers. In addition, analysis of pooled human gamma globulin and several normal sera revealed the presence of IgG2 dimers. The IgG2 dimers are in contrast to the noncovalent IgG dimers found in pooled sera of multiple donors resulting from idiotype/anti-idiotype (Id/anti-Id) interactions. Cyanogen bromide cleavage analysis suggests that one or more Cys residues in the gamma 2 hinge are involved in dimer assembly. The potential role of IgG2 dimers in immunity against carbohydrate Ags is discussed.

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