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1.G.23.  The African Swine Fever Virus (ASFV) Fusion Protein pE199L (ASFV-FP) Family 

African Swine Fever Virus protein pE199L mediates virus entry by enabling membrane fusion and core penetration (Matamoros et al. 2020). ASFV is a complex nucleocytoplasmic large DNA virus (NCLDV) causing a lethal hemorrhagic disease that currently threatens the global pig industry. Despite its relevance in the infectious cycle, very little is known about the internalization of ASFV in the host cell. Matamoros et al. 2020 reported the characterization of ASFV protein pE199L, a cysteine-rich structural polypeptide with similarity to proteins A16, G9, and J5 of the entry fusion complex (EFC) of poxviruses. Like the corresponding poxviral proteins, pE199L localizes to the inner viral envelope and behaves as an integral transmembrane polypeptide with cytosolic intramolecular disulfide bonds. Using an ASFV recombinant that inducibly expresses the E199L gene, they found that pE199L is not required for virus assembly and egress or for virus-cell binding and endocytosis but is required for membrane fusion and core penetration. Similar results had been reported for ASFV protein pE248R, an inner membrane virion component related to the poxviral L1 and F9 EFC proteins. Thus, ASFV entry relies on a form of fusion machinery comprising proteins pE248R and pE199L that displays some similarities to the unconventional fusion apparatus of poxviruses (Matamoros et al. 2020).

References associated with 1.G.23 family:

Matamoros, T., A. Alejo, J.M. Rodríguez, B. Hernáez, M. Guerra, A. Fraile-Ramos, and G. Andrés. (2020). African Swine Fever Virus Protein pE199L Mediates Virus Entry by Enabling Membrane Fusion and Core Penetration. mBio 11:. 32788374