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Review
. 2021 Jan-Dec;13(1):1953220.
doi: 10.1080/19420862.2021.1953220.

The therapeutic potential of sialylated Fc domains of human IgG

Richard J Pleass  1
Affiliations
Review

The therapeutic potential of sialylated Fc domains of human IgG

Richard J Pleass. MAbs. 2021 Jan-Dec.

Abstract

Pathogens frequently use multivalent binding to sialic acid to infect cells or to modulate immunity through interactions with human sialic acid-binding immunoglobulin-type lectins (Siglecs). Molecules that interfere with these interactions could be of interest as diagnostics, anti-infectives or as immune modulators. This review describes the development of molecular scaffolds based on the crystallizable fragment (Fc) region of immunoglobulin (Ig) G that deliver high-avidity binding to innate immune receptors, including sialic acid-dependent receptors. The ways in which the sialylated Fc may be engineered as immune modulators that mimic the anti-inflammatory properties of intravenous polyclonal Ig or as blockers of sialic-acid-dependent infectivity by viruses are also discussed.

Keywords: Fc; IgG; Siglec; influenza; sialic acid; virus.

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Conflict of interest statement

R.J.P. declares that the molecules discussed within are subject to ongoing patent applications. The author has no financial conflicts of interest.

Figures

Figure 1.
Figure 1.
The crystal structure of human IgG1
Figure 2.
Figure 2.
A model of sialylated Fc
Figure 3.
Figure 3.
A model for the known interaction of sialylated Fc with Siglec-3 (CD33)
Figure 4.
Figure 4.
A model for the known interaction of the sialylated Fc with influenza hemagglutinin
See this image and copyright information in PMC

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