Antibodies and antibody-derived macromolecules have established themselves as the
mainstay in protein-based therapeutic molecules (biologics). Our knowledge of the structure …

Abstract The Immunoglobulin G (IgG) glycome is well known for its heterogeneity and shows
a significant degree of variation within populations. IgG glycome composition is influenced …

Antibodies and Fc-fusion antibody-like proteins have become successful biologics
developed for cancer treatment, passive immunity against infection, addiction, and …

Herein we will review the role of glycans in the immune system. Specific topics covered
include: the glycosylation sites of IgE, IgM, IgD, IgE, IgA, and IgG; how glycans can encode …

Therapeutic monoclonal antibodies are the fastest growing class of biological therapeutics
for the treatment of various cancers and inflammatory disorders. In cancer immunotherapy …

Understanding the impact of glycosylation and keeping a close control on glycosylation of
product candidates are required for both novel and biosimilar monoclonal antibodies (mAbs) …

Intravenous immunoglobulin (IVIG) preparations comprise pooled IgG antibodies from the
serum of thousands of donors and were initially used as an IgG replacement therapy in …

Recombinant human IgG antibodies (hIgGs) completely devoid of binding to Fcγ receptors
(FcγRs) and complement protein C1q, and thus with abolished immune effector functions …

Protein glycosylation is post-translational modification (PTM) which is important for
pharmacokinetics and immunogenicity of recombinant glycoprotein therapeutics. As a result …

Antibody-mediated cellular cytotoxicity (ADCC), a key immune effector mechanism, relies on
the binding of antigen–antibody complexes to Fcγ receptors expressed on immune cells …