Glycoprotein Structure and Function in Mammalian Immune Systems: Molecular Architecture and Regulatory Networks

Richard Murdoch Montgomery , Richard Murdoch Montgomery

Glycoproteins represent fundamental architectural and regulatory components of mammalian immune
systems, orchestrating complex molecular interactions through their carbohydrate modifications. This
comprehensive review examines the structural diversity, biosynthetic pathways, and functional roles
of glycoproteins in both innate and adaptive immunity. The glycan code, mediated by cell surface glycoproteins
and their cognate lectins, governs critical processes including pathogen recognition, immune
cell trafficking, and intercellular communication. In adaptive immunity, antibody glycosylation
serves as a molecular switch modulating effector functions, whilst the complement system relies extensively
on glycoprotein components for its cascading activation. Evolutionary analysis reveals the
co-evolution of glycosylation machinery with immune complexity, driven by host-pathogen interactions
and regulatory network innovations. Environmental and metabolic factors dynamically influence
glycoprotein expression, with aberrant glycosylation patterns serving as hallmarks of autoimmune diseases
and malignancy. Advanced analytical methodologies, including mass spectrometry and functional
immune assays, continue to elucidate the complexity of the mammalian glycoproteome. This review
synthesises current understanding of glycoprotein-mediated immune regulation and highlights
emerging therapeutic opportunities targeting these critical molecular mediators.