A bioactive phlebovirus-like envelope protein in a hookworm endogenous virus.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 35544562.
- Also identified by DOI 10.1126/sciadv.abj6894 and PMC identifier 9094657.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
Endogenous viral elements (EVEs), accounting for 15% of our genome, serve as a genetic reservoir from which new genes can emerge. Nematode EVEs are particularly diverse and informative of virus evolution. We identify Atlas virus-an intact retrovirus-like EVE in the human hookworm <i>Ancylostoma ceylanicum</i>, with an envelope protein genetically related to G<sub>N</sub>-G<sub>C</sub> glycoproteins from the family Phenuiviridae. A cryo-EM structure of Atlas G<sub>C</sub> reveals a class II viral membrane fusion protein fold not previously seen in retroviruses. Atlas G<sub>C</sub> has the structural hallmarks of an active fusogen. Atlas G<sub>C</sub> trimers insert into membranes with endosomal lipid compositions and low pH. When expressed on the plasma membrane, Atlas G<sub>C</sub> has cell-cell fusion activity. With its preserved biological activities, Atlas G<sub>C</sub> has the potential to acquire a cellular function. Our work reveals structural plasticity in reverse-transcribing RNA viruses.
Medical subject headings
- Phlebovirus
- RNA Viruses