PT  - JOURNAL ARTICLE
AU  - Rex R. Gonzales
AU  - Carolyn E. Machamer
TI  - The SARS CoV-1 3a protein disrupts Golgi complex morphology and cargo trafficking
AID  - 10.1101/2021.04.19.440492
DP  - 2021 Jan 01
TA  - bioRxiv
PG  - 2021.04.19.440492
4099  - http://biorxiv.org/content/early/2021/04/19/2021.04.19.440492.short
4100  - http://biorxiv.org/content/early/2021/04/19/2021.04.19.440492.full
AB  - Coronaviruses assemble by budding into the endoplasmic reticulum-Golgi intermediate compartment, but the pathway of egress from infected cells is not well understood. Efficient egress of infectious bronchitis virus (a gamma coronavirus, CoV) requires neutralization of Golgi pH by the envelope (E) protein. This results in reduced rates of cargo traffic and disrupts Golgi morphology, but it protects the spike protein from aberrant proteolysis. The severe acute respiratory syndrome (SARS) CoV-1 E protein does not disrupt the Golgi, however. We show here that in transfected cells, the ORF3a protein of SARS CoV-1 disrupts Golgi morphology, cargo trafficking and luminal pH. Unlike the infectious bronchitis virus E protein, these functions of the SARS CoV-1 3a protein appear to require its viroporin activity. Thus, neutralization of acidic compartments may be a universal feature of CoV infection, although different viral proteins and mechanisms may be used to achieve this outcome.Competing Interest StatementThe authors have declared no competing interest.