Antibodies play an essential role in host defence against pathogens by recognizing
microorganisms or infected cells. Although preventing pathogen entry is one potential …

Immunoglobulin G (IgG) antibodies are a critical component of the adaptive immune system,
binding to and neutralizing pathogens and other foreign substances. Recent advances in …

Glycosylation of the immunoglobulin G (IgG)-Fc tail is required for binding to Fc-gamma
receptors (FcγRs) and complement-component C1q. A variety of IgG1-glycoforms is …

Antibody-based proteins have become an important class of biologic therapeutics, due in
large part to the stability, specificity, and adaptability of the antibody framework. Indeed …

IgG3 is unique among the IgG subclasses due to its extended hinge, allotypic diversity and
enhanced effector functions, including highly efficient pathogen neutralisation and …

Glycosylation is the most abundant and complex protein modification, and can have a
profound structural and functional effect on the conjugate. The oligosaccharide fraction is …

Human IgG is the most abundant glycoprotein in serum and is crucial for protective
immunity. In addition to conserved IgG Fc glycans,∼ 15–25% of serum IgG contains glycans …

Antibodies play a critical role in linking the adaptive immune response to the innate immune
system. In humans, antibodies are categorized into five classes, IgG, IgM, IgA, IgE, and IgD …

IgG3 comprises only a minor fraction of IgG and has remained relatively understudied until
recent years. Key physiochemical characteristics of IgG3 include an elongated hinge region …

In the past two years, the world has faced the pandemic caused by the severe acute
respiratory syndrome 2 coronavirus (SARS-CoV-2), which by August of 2022 has infected …