Heparan sulfate proteoglycans (HSPGs) of the ocular lens

Wishart, Tayler F.L.; Lovicu, Frank J.

doi:10.1016/j.preteyeres.2022.101118

Cited by 5 publications

(2 citation statements)

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“…Thus 3- O , 2- O and 6- O sulfation motifs in HS equip it with a diverse dynamic recognition system for the precise identification of bioactive cell regulatory molecules through a “sulfation code” [ 100 , 101 ]. This is reflected in the co-receptor functions of cell surface HS-PGs [ 68 ] and the diverse roles of HS-PGs in the stabilization and functional properties of ocular tissues [ 102 ], and neural activity in the CNS/PNS [ 103 ]. HS-PG interactions with neural cell surface cell attachment glycoproteins provide synaptic stabilization [ 104 , 105 , 106 ] and the signalling properties of neural networks [ 106 ].…”

Section: The Cell Instructive Properties Of Gagsmentioning

confidence: 99%

HS, an Ancient Molecular Recognition and Information Storage Glycosaminoglycan, Equips HS-Proteoglycans with Diverse Matrix and Cell-Interactive Properties Operative in Tissue Development and Tissue Function in Health and Disease

Hayes

Melrose

2023

IJMS

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Heparan sulfate is a ubiquitous, variably sulfated interactive glycosaminoglycan that consists of repeating disaccharides of glucuronic acid and glucosamine that are subject to a number of modifications (acetylation, de-acetylation, epimerization, sulfation). Variable heparan sulfate chain lengths and sequences within the heparan sulfate chains provide structural diversity generating interactive oligosaccharide binding motifs with a diverse range of extracellular ligands and cellular receptors providing instructional cues over cellular behaviour and tissue homeostasis through the regulation of essential physiological processes in development, health, and disease. heparan sulfate and heparan sulfate-PGs are integral components of the specialized glycocalyx surrounding cells. Heparan sulfate is the most heterogeneous glycosaminoglycan, in terms of its sequence and biosynthetic modifications making it a difficult molecule to fully characterize, multiple ligands also make an elucidation of heparan sulfate functional properties complicated. Spatio-temporal presentation of heparan sulfate sulfate groups is an important functional determinant in tissue development and in cellular control of wound healing and extracellular remodelling in pathological tissues. The regulatory properties of heparan sulfate are mediated via interactions with chemokines, chemokine receptors, growth factors and morphogens in cell proliferation, differentiation, development, tissue remodelling, wound healing, immune regulation, inflammation, and tumour development. A greater understanding of these HS interactive processes will improve therapeutic procedures and prognoses. Advances in glycosaminoglycan synthesis and sequencing, computational analytical carbohydrate algorithms and advanced software for the evaluation of molecular docking of heparan sulfate with its molecular partners are now available. These advanced analytic techniques and artificial intelligence offer predictive capability in the elucidation of heparan sulfate conformational effects on heparan sulfate-ligand interactions significantly aiding heparan sulfate therapeutics development.

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Section: The Cell Instructive Properties Of Gagsmentioning

confidence: 99%

HS, an Ancient Molecular Recognition and Information Storage Glycosaminoglycan, Equips HS-Proteoglycans with Diverse Matrix and Cell-Interactive Properties Operative in Tissue Development and Tissue Function in Health and Disease

Hayes

Melrose

2023

IJMS

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“…Typically, glycoprotein(s) gB and/or gC participate in the viral attachment process by binding to host cell receptor HSPGs (Shukla & Spear, 2001). Structurally, HSPG consists of a core protein with covalently linked heparan sulfate (HS) and glycosaminoglycan (GAG) chains (Wishart & Lovicu, 2023). The sulfation pattern plays a crucial role in determining the binding preference of HSV glycoproteins to HS.…”

Section: Ke Y Host-v Ir Al Protein Inter Actions During Hsv At Tachme...mentioning

confidence: 99%

A critical review on antiviral peptides derived from viral glycoproteins and host receptors to decoy herpes simplex virus

Rahangdale,

Tender,

Balireddy

et al. 2023

Microbial Biotechnology

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The health of the human population has been continuously challenged by viral infections. Herpes simplex virus (HSV) is one of the common causes of illness and can lead to death in immunocompromised patients. Existing anti‐HSV therapies are not completely successful in eliminating the infection due to anti‐viral drug resistance, ineffectiveness against the latent virus and high toxicity over prolonged use. There is a need to update our knowledge of the current challenges faced in anti‐HSV therapeutics and realize the necessity of developing alternative treatment approaches. Protein therapeutics are now being explored as a novel approach due to their high specificity and low toxicity. This review highlights the significance of HSV viral glycoproteins and host receptors in the pathogenesis of HSV infection. Proteins or peptides derived from HSV glycoproteins gC, gB, gD, gH and host cell receptors (HSPG, nectin and HVEM) that act as decoys to inhibit HSV attachment, entry, or fusion have been discussed. Few researchers have tried to improve the efficacy and stability of the identified peptides by modifying them using a peptidomimetic approach. With these efforts, we think developing an alternative treatment option for immunocompromised patients and drug‐resistant organisms is not far off.

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