• CoV E

    Selected traces at various holding potentials in DPhPC bilayers measured on the Port-a-Patch

    Li et al. (2014)

CoV E - Coronavirus Envelop Protein E

Viral Fusion Pores

Three distinct classes of viral membrane fusion proteins have been identified based on structural criteria. Viral fusion proteins also contain different types of fusion peptides and vary in their reliance on accessory proteins. Despite the rich diversity of existent fusion proteins, all characterized viral fusion proteins convert from a fusion-competent state (dimers or trimers) to a membrane-embedded homotrimeric prehairpin, to a trimer-of-hairpins that brings the fusion peptide, attached to the target membrane, and the transmembrane domain, attached to the viral membrane, into close proximity, thereby facilitating the union of viral and target membranes. During these conformational conversions, the fusion proteins induce membranes to progress through stages of close apposition, hemifusion, and then the formation of small, and finally large, fusion pores.

CoV E Background Information


Coronaviruses are large, often spherical, enveloped, single-stranded positive-sense RNA viruses, ranging in size from 80-220 nm. Of the four structural proteins encoded in the viral genome, the RNA winds around the highly basic nucleocapsid (N) protein. The three other structural proteins, envelope (E), membrane (M) and spike (S), are transmembrane proteins. The E protein is a small (9-12 kDa) single transmembrane domain protein, which enables virus assembly with the M protein, a larger (23-35 kDa) 3TM protein.

The channel activity 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.

Data Sheet:

Viral Protein:
UniProt: P0DTC4 (Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2))

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.

Channel Function:
Plays a central role in virus morphogenesis and assembly. Acts as a viroporin and self-assembles in host membranes forming pentameric protein-lipid pores that allow ion transport. Also plays a role in the induction of apoptosis


Bilayer Recordings on the Orbit Product family or on the Port-a-Patch

Reviews and Links


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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