Deep-Time Structural Evolution of Retroviral and Filoviral Surface Envelope Proteins.

ABSTRACT: The retroviral surface envelope protein subunit (SU) mediates receptor binding and triggers membrane fusion by the transmembrane (TM) subunit. SU evolves rapidly under strong selective conditions, resulting in seemingly unrelated SU structures in highly divergent retroviruses. Structural modeling of the SUs of several retroviruses and related endogenous retroviral elements with AlphaFold 2 identifies a TM-proximal SU β-sandwich structure that has been conserved in the orthoretroviruses for at least 110 million years. The SU of orthoretroviruses diversified by the differential expansion of the β-sandwich core to form domains involved in virus-host interactions. The β-sandwich domain is also conserved in the SU equivalent GP₁ of Ebola virus although with a significantly different

SUBMITTER: Hotzel I 

PROVIDER: S-EPMC9006886 | biostudies-literature | 2022 Apr

REPOSITORIES: biostudies-literature