Co-assembly of Viral Envelope Glycoproteins Regulates Their Polarized Sorting in Neurons

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Neurons are highly polarized cells exhibiting somatodendritic and axonal domains with distinct protein and lipid compositions. Some enveloped viruses target neurons by binding of the viral envelope glycoproteins to neuronal surface receptors. The ensuing fusion of the viral and neuronal membranes delivers the genetic material of the virus into the neurons. During viral replication in neurons, newly synthesized envelope glycoproteins are sorted to the somatodendritic and/or axonal domains. Although critical for viral propagation, the mechanisms responsible for this sorting are largely unknown. We studied the neuronal sorting of the attachment (NiV-G) and fusion (NiV-F) glycoproteins of Nipah virus, a pathogen that causes fatal human encephalitis. When analyzed individually, NiV-G was delivered to both the axonal and somatodendritic domains. In contrast, NiV-F was exclusively targeted to the somatodendritic domain by virtue of interaction of specific signals in this protein with AP-1, a component of the neuronal protein transport machinery. Assembly with NiV-G, however, abolished somatodendritic sorting of NiV-F due to incorporation of complexes into axon-bound vesicles. Thus, coordinated interactions of viral glycoproteins with the host's sorting machinery and between themselves allow temporal and spatial regulation of their distribution in neurons. We propose that this coordination facilitates viral spread among neurons.

Vyšlo v časopise: Co-assembly of Viral Envelope Glycoproteins Regulates Their Polarized Sorting in Neurons. PLoS Pathog 10(5): e32767. doi:10.1371/journal.ppat.1004107
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.ppat.1004107

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