• CoV E

    I/V plot for a truncated CoV E protein in DPhPC bilayers measured on the Port-a-Patch

    Li et al. (2014)

CoV E - Coronavirus Envelop Protein E

Coronaviruses (CoVs) assemble at endoplasmic reticulum Golgi intermediate compartment membranes and egress from cells in cargo vesicles. Additionally, the E protein has ion channel activity, interacts with host proteins, and may have multiple membrane topologies.

Coronavirus envelope (CoV E) proteins are ~100-residue polypeptides with at least one channel-forming α-helical transmembrane (TM) domain. The extramembrane C terminal tail contains a completely conserved proline, at the center of a predicted β coil β motif.

The channel activity of E was first demonstrated for CoV E in planar lipid bilayers, where it was found that a synthetic peptide corresponding to the protein could permeabilize bilayers to Na+ and K+, with a 10-fold preference for Na+. The role of the CoV E ion channel in infection is not entirely clear. However, studies have linked the putative ion channel activity with virus replication and release.


2014 - Structure of a Conserved Golgi Complex-targeting Signal in Coronavirus Envelope Proteins

icon pap  Port-a-Patch and   icon vpp   Vesicle Prep Pro publication in Journal of Biological Chemistry (2014)

Li Y., Surya W., Claudine S., Torres J.

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