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Volumn 21, Issue , 2016, Pages 93-101

Retargeting of herpes simplex virus (HSV) vectors

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; CELL SURFACE RECEPTOR; COAT PROTEIN; GLYCOPROTEIN D; HEPARAN SULFATE; HERPES SIMPLEX VIRUS VECTOR; HERPESVIRUS ENTRY MEDIATOR; LIGAND; NECTIN 1; NECTIN 1ALPHA; NECTIN 2; NECTIN 2ALPHA; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY; UNCLASSIFIED DRUG; VIRUS GLYCOPROTEIN; VIRUS RECEPTOR; VIRUS VECTOR; DRUG CARRIER;

EID: 84985987046     PISSN: 18796257     EISSN: 18796265     Source Type: Journal    
DOI: 10.1016/j.coviro.2016.08.007     Document Type: Review
Times cited : (27)

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    • Displacement of the C terminus of herpes simplex virus gD is sufficient to expose the fusion-activating interfaces on gD
    • This paper details the overall change in gD structure post receptor binding to the gD amino terminus that leads to the displacement of the C-terminus as a way of communicating the fusion signal to the gB–gH/gL complex.
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    • Induction of conformational changes at the N-terminus of herpes simplex virus glycoprotein D upon binding to HVEM and nectin-1
    • This paper details a comparison of the mutational analyses of the HVEM and Nectin-1 binding domains of gD with the actual crystal structure of receptor-bound and free gD. It provides a greater understanding of the conformational change in gD upon engaging the two different cellular gD receptors.
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    • Bimolecular complementation defines functional regions of herpes simplex virus gB that are involved with gH/gL as a necessary step leading to cell fusion
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    • 45• Zeev-Ben-Mordehai, T., Vasishtan, D., Hernandez Duran, A., Vollmer, B., White, P., Prasad Pandurangan, A., Siebert, C.A., Topf, M., Grunewald, K., Two distinct trimeric conformations of natively membrane-anchored full-length herpes simplex virus 1 glycoprotein B. Proc Natl Acad Sci U S A 113 (2016), 4176–4181 This work employs electron cryotomography to examine the differences in pre-fusion and post-fusion crystallographic forms of gB helping to detail the conformational change in gB enabling fusion of the viral envelop with the host cell or endosomal membrane.
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