Adenovirus serotype 26 utilises sialic acid bearing glycans as a primary cell entry receptor

Baker, Alex; Mundy, R.M.; Davies, James A.; Rizkillah, Pierre T.; Parker, Alan L.

doi:10.1101/580076

Cited by 2 publications

(2 citation statements)

References 82 publications

(98 reference statements)

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“…However, it has been shown that endocytosis of the human adenovirus type 37 in species D (HAdV-D37) into corneal cells uses caveolin-1 proteins clustered in lipid rafts [132]. Based on reduction of fiber knob/virus binding and infection of sialidase-treated cells, 6 types of ocular pathogens in HAdV species D including 8, 26, 37, 53 (a natural intertypic recombinant of HAdV types 8, 22 and 37), 54 (believed to be an HAdV-D8 variant strain), and 64 (formally known as 19a, a natural recombinant of HAdV types 19p (p ¼ prototype), 22 and 37) [133] have so far been shown to use Sia as a primary cellular receptor for binding that is mediated by their trimeric fiber knobs [134][135][136]. Pretreatment of cells with an NA reduced interactions of HAdV-D19p, which does not cause an eye infection, but did not affect its productive infection, suggesting that Sia may support the virus attachment but is not used as a functional receptor for virus infection [134].…”

Section: Adenoviridaementioning

confidence: 99%

“…Amino acid sequence analysis revealed that fiber knobs of HAdV-D37 and HAdV-D64 have identity of 100% [136], suggesting that HAdV-D64 possesses the same binding pocket with preferential binding to O-linked glycoproteins bearing GD1a glycan. Fiber knobs of HAdV-D8, HAdV-D26, HAdV-D53, and HAdV-D54 carrying some amino acids that are different from those in the above fiber knobs [135,136] should be further identified for determining positions of amino acids in 3D structures of the fiber knobs and screened for their receptorbinding specificity.…”

Section: Adenoviridaementioning

confidence: 99%

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Sialoglycovirology of Lectins: Sialyl Glycan Binding of Enveloped and Non-enveloped Viruses

Sriwilaijaroen

Suzuki

2020

Methods in Molecular Biology

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On the cell sur "face", sialoglycoconjugates act as receptionists that have an important role in the first step of various cellular processes that bridge communication between the cell and its environment. Loss of Sia production can cause the developmental of defects and lethality in most animals; hence, animal cells are less prone to evolution of resistance to interactions by rapidly evolved Sia-binding viruses. Obligative intracellular viruses mostly have rapid evolution that allows escape from host immunity, leading to an epidemic variant, and that allows emergence of a novel strain, occasionally leading to pandemics that cause healthsocial-economic problems. Recently, much attention has been given to the mutual recognition systems via sialosugar chains between viruses and their host cells and there has been rapid growth of the research field "sialoglycovirology." In this chapter, the structural diversity of sialoglycoconjugates is overviewed, and enveloped and non-enveloped viruses that bind to Sia are reviewed. Also, interactions of viral lectins-host Sia receptors, which determine viral transmission, host range, and pathogenesis, are presented. The future direction of new therapeutic routes targeting viral lectins, development of easy-to-use detection methods for diagnosis and monitoring changes in virus binding specificity, and challenges in the development of suitable viruses to use in virus-based therapies for genetic disorders and cancer are discussed.

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Section: Adenoviridaementioning

confidence: 99%

Section: Adenoviridaementioning

confidence: 99%

Sialoglycovirology of Lectins: Sialyl Glycan Binding of Enveloped and Non-enveloped Viruses

Sriwilaijaroen

Suzuki

2020

Methods in Molecular Biology

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Broad sialic acid usage amongst species D human adenovirus

Mundy

Baker

Bates

et al. 2023

Preprint

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Human adenoviruses (HAdV) are widespread pathogens causing infections of the respiratory and gastrointestinal tracts, genitourinary system and the eye. Species D (HAdV-D) are the most diverse species and cause both gastrointestinal tract infections and epidemic keratoconjunctivitis (EKC). Despite being significant pathogens, HAdV-D are understudied and knowledge around basic mechanisms of cell infection is lacking. Sialic acid (SA) usage has been proposed as a major mechanism of cell infection for EKC causing HAdV-D. Here, we provide apo state crystal structures for fiber knob proteins of 7 previously undetermined HAdV-D, and provide crystal structures of HAdV-D25, HAdV-D29 and HAdV-D53 knob proteins bound to SA. Biologically, we demonstrate that removal of cell surface SA reduced infectivity of HAdV-C5 vectors pseudotyped with HAdV-D fiber knob proteins, whilst engagement of the classical HAdV receptor, CAR was variable. Together, these data indicate an important role for SA engagement in the tropism of many HAdV-D and may facilitate the development of suitable antivirals to control EKC outbreaks.

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Adenovirus serotype 26 utilises sialic acid bearing glycans as a primary cell entry receptor

Abstract: word count: 150 26 Main text word count: 5009 27 Figure legend word count: 462 28

Cited by 2 publications

References 82 publications

Sialoglycovirology of Lectins: Sialyl Glycan Binding of Enveloped and Non-enveloped Viruses

Sialoglycovirology of Lectins: Sialyl Glycan Binding of Enveloped and Non-enveloped Viruses

Broad sialic acid usage amongst species D human adenovirus

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