Recombinant Vesicular stomatitis Indiana virus Glycoprotein G (G), partial

1. Vesicular stomatitis virus G protein complex with two distinct cysteine-rich domains (CR2 and CR3) of LDL-R. PMID: 29531262
2. This work reveals the range of glycoprotein G structural changes and suggests that G monomers can re-associate, through antiparallel interactions between fusion domains, into dimers that play a role at some early stage of the fusion process. PMID: 28188244
3. NSF deficiency in HeLa cells barely affected cell viability, anterograde trafficking of vesicular stomatitis virus glycoprotein G and transferrin endocytosis. PMID: 27995606
4. MARCH8 is highly expressed in terminally differentiated myeloid cells, and that it is a potent antiviral protein that targets viral envelope glycoproteins and reduces their incorporation into virions. PMID: 26523972
5. Pepscan mapping of autophagy-inducing linear determinants of glycoproteins viral hemorrhagic septicemia virus and glycoproteins vesicular stomatitis virus showed that peptides located in their fusion domains induce autophagy PMID: 25046110
6. Overall, these results showed that the HIV Env membrane-proximal external region could functionally substitute for the vesicular stomatitis virus G-stem region implying that both perform similar functions even though they are from unrelated viruses. PMID: 24597516
7. Authors show that D268, located in the segment consisting of residues 264 to 273, which refolds into postfusion helix F during G structural transition, is the major pH sensor while D274, D395, and D393 have additional contributions. PMID: 25210175
8. Recombinant VSV with RABV-G drives strong expression of transgenes and spreads rapidly from neuron to neuron in only a retrograde manner. PMID: 23403489
9. Energetic analyses revealed weakened interaction between Domain IV and the protein core at pH 5, which can be attributed to two pairs of structurally neighboring conserved and differentially protonated residues in the Domain IV-core interface. PMID: 22806964
10. set of recombinant VSV particles bearing lethal mutations in G; study confirms hydrophobic fusion loops are critical for membrane fusion; underscores importance of the sequence elements surrounding the hydrophobic tips of fusion loops in driving fusion PMID: 21680501
11. Data suggest that BMP preferentially affects the ability of VSV G to mediate lipid mixing during membrane fusion. PMID: 21333650
12. adaptation of VSIV-6.8 to pHs 6.6 and 6.4 resulted in additional amino acid substitutions in areas of the glycoprotein that were not previously implicated in attachment or fusion. PMID: 15731252
13. crystal structure; structure of G in its low-pH form shows the classic hairpin conformation observed in all other fusion proteins in their postfusion conformation PMID: 16840692
14. structure of the prefusion form, determined to 3.0 angstrom resolution, shows that the fusogenic transition entails an extensive structural reorganization of G PMID: 17289996
15. We now report that VSV glycoprotein G (gpG) is essential for the induction of a previously unrecognized CD14/TLR4-dependent response PMID: 17292937
16. results suggest a new model of virus assembly in which an interaction of VSV nucleocapsids with G-protein-containing microdomains is a precursor to the formation of viral budding sites PMID: 18367537

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KEGG: vg:1489834