Structural Features Of Human Immunoglobulin G That Determine ...

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Abstract

Although very similar in sequence, the four subclasses of human immunoglobulin G (IgG) differ markedly in their ability to activate complement. Glu318-Lys320-Lys322 has been identified as a key binding motif for the first component of complement, C1q, and is present in all isotypes of Ig capable of activating complement. This motif, however, is present in all subclasses of human IgG, including those that show little (IgG2) or even no (IgG4) complement activity. Using point mutants of chimeric antibodies, we have identified specific residues responsible for the differing ability of the IgG subclasses to fix complement. In particular, we show that Ser at position 331 in gamma 4 is critical for determining the inability of that isotype to bind C1q and activate complement. Additionally, we provide further evidence that levels of C1q binding do not necessarily correlate with levels of complement activity, and that C1q binding alone is not sufficient for complement activation.

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References

1. 1. Proc Natl Acad Sci U S A. 1981 Jan;78(1):524-8 - PubMed
2. 1. Biochemistry. 1981 Apr 28;20(9):2361-70 - PubMed
3. 1. Nature. 1984 Jan 12-18;307(5947):136-40 - PubMed
4. 1. DNA. 1984 Dec;3(6):479-88 - PubMed
5. 1. Mol Immunol. 1985 Mar;22(3):161-206 - PubMed

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• 5 T32 GM07104-18/GM/NIGMS NIH HHS/United States
• AI-29470/AI/NIAID NIH HHS/United States
• CA-16858/CA/NCI NIH HHS/United States

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