8ofs

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Current revision (07:32, 21 November 2024) (edit) (undo)
 
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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/M0QTV3_9ADEN M0QTV3_9ADEN]
[https://www.uniprot.org/uniprot/M0QTV3_9ADEN M0QTV3_9ADEN]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Human adenoviruses (HAdV) are widespread pathogens causing usually mild infections. The Species D (HAdV-D) cause gastrointestinal tract infections and epidemic keratoconjunctivitis (EKC). Despite being significant pathogens, knowledge around HAdV-D mechanism of cell infection is lacking. Sialic acid (SA) usage has been proposed as a cell infection mechanism for EKC causing HAdV-D. Here we highlight an important role for SA engagement by many HAdV-D. We provide apo state crystal structures of 7 previously undetermined HAdV-D fiber-knob proteins, and structures of HAdV-D25, D29, D30 and D53 fiber-knob proteins in complex with 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. Our data indicates variable usage of SA and CAR across HAdV-D. Better defining these interactions will enable improved development of antivirals and engineering of the viruses into refined therapeutic vectors.
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Broad sialic acid usage amongst species D human adenovirus.,Mundy RM, Baker AT, Bates EA, Cunliffe TG, Teijeira-Crespo A, Moses E, Rizkallah PJ, Parker AL Npj Viruses. 2023;1(1):1. doi: 10.1038/s44298-023-00001-5. Epub 2023 Sep 26. PMID:38665237<ref>PMID:38665237</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 8ofs" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Human adenovirus type 30 fiber-knob protein complexed with sialic acid

PDB ID 8ofs

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