AI Article Synopsis
- Three different avian adenoviral strains use the coxsackievirus-adenovirus receptor (CAR) for binding, but they have different affinities and attachment modes.
- A crystal structure of the FAdV-4 fiber knob was determined, revealing its interaction with CAR.
- The study found that while all three adenoviruses primarily target CAR domain 1, the CELO strains show weak interaction with CAR domain 2, which helps understand how these viruses invade host cells.
Article Abstract
According to previous studies, three representative avian adenoviral strains utilize coxsackievirus-adenovirus receptor (CAR) as a receptor and seem to exhibit diverse binding affinities and modes. Thus, further revealing the exact molecular mechanism underlying the interaction between different FAdVs and the attachment receptor CAR is necessary. In this study, we successfully solved the crystal structure of the FAdV-4 fiber1 knob at 1.6 Å resolution. The interaction between the fibre knob and different domains of CAR was verified by confocal microscopy, coimmunoprecipitation and surface plasmon resonance (SPR) analysis. The fibre knobs of the three representative fowl adenoviruses specifically recognized CAR domain 1 (D1), but the recognition of CAR domain 2 (D2) by chicken embryo lethal orphan (CELO) strains was weak. These results provide insights into the differences in adenovirus‒host cell interactions and have important implications for the exploration of viral invasion mechanisms.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10875832 | PMC |
| http://dx.doi.org/10.1186/s13567-024-01277-y | DOI Listing |
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