about
The ectodomain of a novel member of the immunoglobulin subfamily related to the poliovirus receptor has the attributes of a bona fide receptor for herpes simplex virus types 1 and 2 in human cellsCell-to-cell spread of wild-type herpes simplex virus type 1, but not of syncytial strains, is mediated by the immunoglobulin-like receptors that mediate virion entry, nectin1 (PRR1/HveC/HIgR) and nectin2 (PRR2/HveB)Novel, soluble isoform of the herpes simplex virus (HSV) receptor nectin1 (or PRR1-HIgR-HveC) modulates positively and negatively susceptibility to HSV infectionThe V domain of herpesvirus Ig-like receptor (HIgR) contains a major functional region in herpes simplex virus-1 entry into cells and interacts physically with the viral glycoprotein DRetargeting Strategies for Oncolytic Herpes Simplex VirusesInsertion of a ligand to HER2 in gB retargets HSV tropism and obviates the need for activation of the other entry glycoproteins.Trafficking to the plasma membrane of the seven-transmembrane protein encoded by human herpesvirus 6 U51 gene involves a cell-specific function present in T lymphocytes.Human herpesvirus 6: An emerging pathogen.Herpes simplex virus glycoproteins H/L bind to cells independently of {alpha}V{beta}3 integrin and inhibit virus entry, and their constitutive expression restricts infectionGlycoprotein D or J delivered in trans blocks apoptosis in SK-N-SH cells induced by a herpes simplex virus 1 mutant lacking intact genes expressing both glycoproteins.Pityriasis rosea is not associated with human herpesvirus 7.Glycoprotein D of bovine herpesvirus 5 (BoHV-5) confers an extended host range to BoHV-1 but does not contribute to invasion of the brainThe pro-fusion domain of herpes simplex virus glycoprotein D (gD) interacts with the gD N terminus and is displaced by soluble forms of viral receptors.The soluble ectodomain of herpes simplex virus gD contains a membrane-proximal pro-fusion domain and suffices to mediate virus entryDevelopment of recombinant diagnostic reagents based on pp85(U14) and p86(U11) proteins to detect the human immune response to human herpesvirus 7 infection.The novel receptors that mediate the entry of herpes simplex viruses and animal alphaherpesviruses into cells.Herpes simplex virus glycoproteins gH/gL and gB bind Toll-like receptor 2, and soluble gH/gL is sufficient to activate NF-κB{alpha}V{beta}3-integrin routes herpes simplex virus to an entry pathway dependent on cholesterol-rich lipid rafts and dynamin2.Preclinical therapy of disseminated HER-2⁺ ovarian and breast carcinomas with a HER-2-retargeted oncolytic herpesvirus.A herpes simplex virus recombinant that exhibits a single-chain antibody to HER2/neu enters cells through the mammary tumor receptor, independently of the gD receptors.The domains of glycoprotein D required to block apoptosis induced by herpes simplex virus 1 are largely distinct from those involved in cell-cell fusion and binding to nectin1Cross talk among the glycoproteins involved in herpes simplex virus entry and fusion: the interaction between gB and gH/gL does not necessarily require gD.αvβ6- and αvβ8-integrins serve as interchangeable receptors for HSV gH/gL to promote endocytosis and activation of membrane fusion.The herpesvirus glycoproteins B and H.L are sequentially recruited to the receptor-bound gD to effect membrane fusion at virus entry.The epithelial αvβ3-integrin boosts the MYD88-dependent TLR2 signaling in response to viral and bacterial components.The Engineering of a Novel Ligand in gH Confers to HSV an Expanded Tropism Independent of gD Activation by Its ReceptorsThe murine homolog of human Nectin1delta serves as a species nonspecific mediator for entry of human and animal alpha herpesviruses in a pathway independent of a detectable binding to gDRedistribution of microtubules and Golgi apparatus in herpes simplex virus-infected cells and their role in viral exocytosis.Dissociation of HSV gL from gH by αvβ6- or αvβ8-integrin promotes gH activation and virus entry.Replication-competent herpes simplex virus retargeted to HER2 as therapy for high-grade gliomaαvβ3-integrin is a major sensor and activator of innate immunity to herpes simplex virus-1.Systemic delivery of HER2-retargeted oncolytic-HSV by mesenchymal stromal cells protects from lung and brain metastases.Localization and putative function of the UL20 membrane protein in cells infected with herpes simplex virus 1.Herpes simplex virus envelopment and maturation studied by fracture label.The UL20 gene of herpes simplex virus 1 encodes a function necessary for viral egressThe multipartite system that mediates entry of herpes simplex virus into the cell.The 85-kilodalton phosphoprotein (pp85) of human herpesvirus 7 is encoded by open reading frame U14 and localizes to a tegument substructure in virion particles.Inhibition of human tumor growth in mice by an oncolytic herpes simplex virus designed to target solely HER-2-positive cells.Rethinking herpes simplex virus: the way to oncolytic agents.The molecular basis of herpesviruses as oncolytic agents.
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description
hulumtuese
@sq
researcher
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wetenschapper
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հետազոտող
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name
Gabriella Campadelli-Fiume
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Gabriella Campadelli-Fiume
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Gabriella Campadelli-Fiume
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Gabriella Campadelli-Fiume
@nl
Gabriella Campadelli-Fiume
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type
label
Gabriella Campadelli-Fiume
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Gabriella Campadelli-Fiume
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Gabriella Campadelli-Fiume
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Gabriella Campadelli-Fiume
@nl
Gabriella Campadelli-Fiume
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prefLabel
Gabriella Campadelli-Fiume
@ast
Gabriella Campadelli-Fiume
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Gabriella Campadelli-Fiume
@es
Gabriella Campadelli-Fiume
@nl
Gabriella Campadelli-Fiume
@sl
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P21
P31
P496
0000-0002-6012-6081