The KxGxYR and DxE motifs in the C-tail of the Middle East respiratory syndrome coronavirus membrane protein are crucial for infectious virus assembly.

ABSTRACT: The coronavirus' (CoV) membrane (M) protein is the driving force during assembly, but this process remains poorly characterized. Previously, we described two motifs in the C-tail of the Middle East respiratory syndrome CoV (MERS-CoV) M protein involved in its endoplasmic reticulum (ER) exit (₂₁₁DxE₂₁₃) and trans-Golgi network (TGN) retention (₁₉₉KxGxYR₂₀₄). Here, their function in virus assembly was investigated by two different virus-like particle (VLP) assays and by mutating both motifs in an infectious MERS-CoV cDNA clone. It was shown that the ₁₉₉KxGxYR₂₀₄ motif was essential for VLP and infectious virus assembly. Moreover, the mislocalization of the M protein induced by mutation of this motif prevented M-E interaction.

SUBMITTER: Desmarets L 

PROVIDER: S-EPMC10632273 | biostudies-literature | 2023 Nov

REPOSITORIES: biostudies-literature