Survey of viral glycoproteins for sensitivity to SERINC5
Our manuscript entitled, “Influence of different glycoproteins and of the virion core on SERINC5 antiviral activity”, is now online as a preprint at bioRxiv: https://www.biorxiv.org/content/10.1101/780577v1
William E. Diehl, Mehmet H. Guney, Pyae Phyo Kyawe, Judith M. White, Massimo Pizzato, Jeremy Luban
In 2015, we reported that HIV-1 Nef blocks the antiviral host factor SERINC5, and that the structurally unrelated MLV Glycogag acts similarly to Nef (Nature 526:212; https://www.ncbi.nlm.nih.gov/pubmed/26416734). The HIV-1 glycoprotein was identified as a viral determinant of susceptibility to restriction. In contrasts, GPs that fuse in acidic endosomes, i.e., VSV and EBOV, were resistant to restriction. Virion membrane-associated SERINC5 blocks an early step in the infection cycle but the exact mechanism of restriction has not been elucidated.
The new manuscript examined a large panel of GP pseudotypes on three types of retrovirion cores and makes the following observations:
1. we identify the first non-retroviral GPs that are sensitive to SERINC5 restriction
2. GP requirement for acidification does not necessarily make the particle SERINC5-resistant.
3. the core of the virion influences sensitivity to restriction.
Our findings extend understanding of the requirements for SERINC5 restriction, potentially expand the significance of SERINC5 beyond retroviruses, and provide useful information to those attempting to understand the SERINC5 restriction mechanism.