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Australian bat lyssavirus

Species of virus

  • 9 min read
  • 5 chapters

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Through Australia

Virology

Molecular structure

The Australian bat lyssavirus (ABLV) shares many structural characteristics with the other Lyssaviruses, despite being genetically and serologically distinct from the others. Visually, ABLV is a bullet shaped virus. Molecularly, ABLV is an enveloped, negative-sense, single-stranded RNA virus. The (-)ssRNA genome is relatively small, containing 12 kilobases of genetic material and encoding five viral proteins. The five viral proteins, their symbol, and their functional roles are:

Viral entry mechanism and intracellular trafficking

ABLV has a similar entry mechanism to other rabies viruses, utilizing receptor-mediated endocytosis by the host cells. The glycoprotein (G) is a trimeric spike protein that extends through the virus's envelope and can interact with surface receptors of host cells. While the specific receptors remain mostly unknown at this time, it is thought that ABLV enters the nervous system of host through the neuromuscular junction of the peripheral nervous system. Additionally, it is believed that the spike protein either binds to a highly specific host receptor or uses a co-receptor in lipid rafts. Some of the proposed receptors include nicotinic acetylcholine receptor (nAchR), p75 neurotrophin receptor (p75NTR), and neuronal cell adhesion molecule (NCAM).

After attaching to the host cell surface, ABLV uses a clathrin-dynamin-dependent pathway to invaginate the host membrane and pinch off a vesicle. Actin polymerization at the site of invagination is also required for successful viral entry. The virus is endocytosed fully, unenveloped. The vesicle fuses with a lysosome, causing the pH within the infected vesicle to drop. The lowering of pH in the early-endosome causes a conformational change in the spike protein G. This allows the viral envelope to fuse with the endosome, releasing the nucleocapsid into the cytoplasm of the host cell.

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