Journal
MEDICAL MICROBIOLOGY AND IMMUNOLOGY
Volume 209, Issue 3, Pages 325-333Publisher
SPRINGER
DOI: 10.1007/s00430-019-00645-2
Keywords
Human adenovirus; Structural biology; X-ray crystallography; Cryoelectron microscopy; Review
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Funding
- Viral and Bacterial Adhesin Network Training Innovative Training Network, part of the European Union's Horizon 2020 Research and Innovation Programme under the Marie Skodowska-Curie Grant [765042]
- Baden-Wurttemberg Foundation (Glycobiology/Glycomics program)
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Human Adenoviruses (HAdVs) are a family of clinically and therapeutically relevant viruses. A precise understanding of their host cell attachment and entry mechanisms can be applied in inhibitor design and the construction of targeted gene delivery vectors. In this article, structural data on adenovirus attachment and entry are reviewed. HAdVs engage two types of receptors: first, an attachment receptor that is bound by the fibre knob protein protruding from the icosahedral capsid, and next, an integrin entry receptor bound by the pentameric penton base at the capsid vertices. Adenoviruses use remarkably diverse attachment receptors, five of which have been studied structurally in the context of HAdV binding: Coxsackie and Adenovirus Receptor, CD46, the glycans GD1a and polysialic acid, and desmoglein-2. Together with the integrin entry receptors, they display both symmetrical and asymmetrical modes of binding to the virus as demonstrated by the structural analyses reviewed here. The diversity of HAdV receptors contributes to the broad tropism of these viruses, and structural studies are thus an important source of information on HAdV-host cell interactions. The imbalance in structural data between the more and less extensively studied receptors remains to be addressed by future research.
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