⚙
AI-generated deep summary
by claude@2026-07, 2026-07-03
· read from full text
ⓘ
This paper is a comprehensive (preprint, version 1) review examining how mammalian immune-system glycoproteins—including cell-surface lectin/glycan interactions, antibody glycosylation, and complement-system glycoprotein components—control key processes such as pathogen recognition, immune-cell trafficking, intercellular communication, and complement activation. It surveys glycoprotein structural diversity, glycan biosynthetic pathways, and evolutionary co-adaptation between glycosylation machinery and immune complexity, emphasizing host-pathogen driven regulatory network innovations. The authors also discuss how environmental and metabolic factors can alter glycoprotein expression and how aberrant glycosylation patterns are highlighted as hallmarks of autoimmune diseases and malignancy, while noting that advanced mass spectrometry and functional immune assays are used to elucidate glycoproteome complexity. This paper does not explicitly discuss endometriosis or adenomyosis; it was included in the corpus via a keyword match in the upstream search index.
Abstract
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.
Full text
2,176 characters
· extracted from
oa-doi-fallback
· click to expand
This is a Preprint and has not been peer reviewed. This is version 1 of this Preprint.
You must log in to post a comment.
There are no comments or no comments have been made public for this article.
This is a Preprint and has not been peer reviewed. This is version 1 of this Preprint.
Add a Comment
You must log in to post a comment.
Comments
There are no comments or no comments have been made public for this article.
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.
https://doi.org/10.32942/X2434D
Life Sciences
Keywords: glycoproteins, immune system, glycosylation, antibodies, complement system, lectins, mammalian immunity, molecular recognition
Published: 2025-07-10 04:04
Last Updated: 2025-07-10 04:04
CC BY Attribution 4.0 International
Language:
English
Text is read by the "Ask this paper" AI Q&A widget below.
Extraction quality varies by source — PMC NXML preserves structure
cleanly, OA-HTML may include some navigation residue, and OA-PDF can
have broken hyphenation. The publisher copy
(via DOI)
is the canonical version.