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Viruses. 2019 Aug 14;11(8). pii: E750. doi: 10.3390/v11080750.

Proteomics Computational Analyses Suggest that the Antennavirus Glycoprotein Complex Includes a Class I Viral Fusion Protein (α-Penetrene) with an Internal Zinc-Binding Domain and a Stable Signal Peptide.

Author information

1
School of Nursing, Johns Hopkins University, Baltimore, MD 21205, USA.
2
Department of Microbiology and Immunology, Tulane University School of Medicine, New Orleans, LA 70112, USA. rfgarry@tulane.edu.
3
Zalgen Labs, Germantown, MD 20876, USA. rfgarry@tulane.edu.

Abstract

A metatranscriptomic study of RNA viruses in cold-blooded vertebrates identified two related viruses from frogfish (Antennarius striatus) that represent a new genus Antennavirus in the family Arenaviridae (Order: Bunyavirales). Computational analyses were used to identify features common to class I viral fusion proteins (VFPs) in antennavirus glycoproteins, including an N-terminal fusion peptide, two extended alpha-helices, an intrahelical loop, and a carboxyl terminal transmembrane domain. Like mammarenavirus and hartmanivirus glycoproteins, the antennavirus glycoproteins have an intracellular zinc-binding domain and a long virion-associated stable signal peptide (SSP). The glycoproteins of reptarenaviruses are also class I VFPs, but do not contain zinc-binding domains nor do they encode SSPs. Divergent evolution from a common progenitor potentially explains similarities of antennavirus, mammarenavirus, and hartmanivirus glycoproteins, with an ancient recombination event resulting in a divergent reptarenavirus glycoprotein.

KEYWORDS:

antennavirus; arenavirus glycoproteins; class I viral fusion protein; hartmanivirus; internal zinc-binding domain; mammarenavirus; reptarenavirus; stable signal peptide

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