Abstract
Rhabdoviruses enter the cell via the endocytic pathway and subsequently fuse with a cellular membrane within the acidic environment of the endosome. Both receptor recognition and membrane fusion are mediated by a single transmembrane viral glycoprotein (G). Fusion is triggered via a low-pH induced structural rearrangement. G is an atypical fusion protein as there is a pH-dependent equilibrium between its pre- and post-fusion conformations. The elucidation of the atomic structures of these two conformations for the vesicular stomatitis virus (VSV) G has revealed that it is different from the previously characterized class I and class II fusion proteins. In this review, the pre- and post-fusion VSV G structures are presented in detail demonstrating that G combines the features of the class I and class II fusion proteins. In addition to these similarities, these G structures also reveal some particularities that expand our understanding of the working of fusion machineries. Combined with data from recent studies that revealed the cellular aspects of the initial stages of rhabdovirus infection, all these data give an integrated view of the entry pathway of rhabdoviruses into their host cell.
Highlights
The Rhabdoviridae family is grouped in the order Mononegavirales together with the Filoviridae (e.g., Ebola Virus), the Paramyxoviridae and the Bornaviridae (e.g., Borna disease virus)
After incorporation of exogenous gangliosides such as GT1b and GQ1b, the cells recovered their susceptibility to RABV infection [38]. These results indicate that highly sialylated gangliosides are part of the cellular membrane receptor structure for the attachment of fixed RABV strains
The second protein that has been proposed to play the role of a RABV receptor is the neural cell adhesion molecule (NCAM) [45]
Summary
The Rhabdoviridae family is grouped in the order Mononegavirales together with the Filoviridae (e.g., Ebola Virus), the Paramyxoviridae (e.g., measles and respiratory syncytial viruses) and the Bornaviridae (e.g., Borna disease virus). They are widespread among a great diversity of organisms such as plants, insects, fishes, mammals, reptiles and crustaceans [1] This family has a long history and it has been recently shown that the genomes of several arthropods contain numerous integrated elements from Rhabdoviruses with some integration events that are at least 11 million years old [2]. Based on their structural properties, antigenicity and phylogenetic analyses, Rhabdoviruses have been grouped into six genera. It recognizes receptors at the viral surface and after virion endocytosis, it mediates the fusion between the viral and the endosomal membranes
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