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The therapeutic potential of sialylated fragment crystallizable (Fc) domains of human IgG

Pleass, Richard ORCID: (2021) 'The therapeutic potential of sialylated fragment crystallizable (Fc) domains of human IgG'. mAbs, Vol 13, Issue 1.

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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.

Item Type: Article
Subjects: QU Biochemistry > QU 4 General works
QU Biochemistry > Proteins. Amino Acids. Peptides > QU 55 Proteins
QW Microbiology and Immunology > Antigens and Antibodies. Toxins and Antitoxins > QW 575 Antibodies
Faculty: Department: Biological Sciences > Department of Tropical Disease Biology
Digital Object Identifer (DOI):
Depositing User: Cathy Waldron
Date Deposited: 12 Jul 2021 11:41
Last Modified: 27 Jul 2021 13:58


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