Key result
A cryo-EM structure of the Atlas virus GC protein from the human hookworm Ancylostoma ceylanicum reveals a class II viral membrane fusion protein fold not previously seen in retroviruses.
Why the study?
Endogenous retroviruses serve as a genetic reservoir from which new genes can emerge, and nematode ERVs are particularly diverse and informative of retrovirus evolution.
Answers are grounded in this paper and cite their sources.
Expands retroviral fusion protein diversity; leaves open functional roles and therapeutic relevance in parasitic infections.
Endogenous retroviruses (ERVs), accounting for 14% of our genome, serve as a genetic reservoir from which new genes can emerge. Nematode ERVs are particularly diverse and informative of retrovirus evolution. We identify Atlas virus – a novel, intact ERV in the human hookworm Ancylostoma ceylanicum with an envelope protein genetically related to G N -G C glycoproteins from phleboviruses. A cryo-EM structure of Atlas G C reveals a class II viral membrane fusion protein fold not previously seen in retroviruses. Atlas G C has the structural hallmarks of an active fusogen. Atlas G C trimers insert into membranes with endosomal lipid compositions and low pH. When expressed on the plasma membrane, Atlas G C has cell-cell fusion activity. Atlas virus is transcriptionally active at specific stages of hookworm development. The preserved activities and expression pattern of Atlas G C suggest it has acquired a cellular function. Our work reveals an unexpected degree of structural and genetic plasticity in retroviruses.
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Merchant et al. (2021) studied Endogenous retrovirus in Ancylostoma ceylanicum. Cryo-EM structural analysis was evaluated on Molecular structure of Atlas GC. A cryo-EM structure of the Atlas virus GC protein from the human hookworm Ancylostoma ceylanicum reveals a class II viral membrane fusion protein fold not previously seen in retroviruses.
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