Interaction of herpes simplex virus glycoprotein gC with mammalian cell surface molecules (Q35841977)

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scientific article published in July 1995

Language	Label	Description	Also known as
English	Interaction of herpes simplex virus glycoprotein gC with mammalian cell surface molecules	scientific article published in July 1995

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scholarly article

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7769707%20AND%20SRC:MED&resulttype=core&format=json

25 October 2019

Interaction of herpes simplex virus glycoprotein gC with mammalian cell surface molecules (English)

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25 October 2019

author name string

R Tal-Singer

1

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25 October 2019

C Peng

2

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25 October 2019

M Ponce De Leon

3

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25 October 2019

W R Abrams

4

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25 October 2019

B W Banfield

5

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25 October 2019

F Tufaro

6

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25 October 2019

G H Cohen

7

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25 October 2019

R J Eisenberg

8

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25 October 2019

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publication date

1 July 1995

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25 October 2019

Journal of Virology

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25 October 2019

69

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25 October 2019

7

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25 October 2019

4471-4483

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25 October 2019

Glycoproteins gIII and gp50 play dominant roles in the biphasic attachment of pseudorabies virus.

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The amino-terminal one-third of pseudorabies virus glycoprotein gIII contains a functional attachment domain, but this domain is not required for the efficient penetration of Vero cells.

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A mutant herpes simplex virus type 1 unable to express glycoprotein L cannot enter cells, and its particles lack glycoprotein H

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Herpes simplex virus infection and propagation in a mouse L cell mutant lacking heparan sulfate proteoglycans

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Cell-specific kinetics and efficiency of herpes simplex virus type 1 entry are determined by two distinct phases of attachment

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High-level expression and purification of secreted forms of herpes simplex virus type 1 glycoprotein gD synthesized by baculovirus-infected insect cells.

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Glycoprotein gB (gII) of pseudorabies virus can functionally substitute for glycoprotein gB in herpes simplex virus type 1.

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Virus receptors: binding, adhesion strengthening, and changes in viral structure.

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A peptide-model for the heparin-binding property of pseudorabies virus glycoprotein III.

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The interaction of glycoprotein C of herpes simplex virus types 1 and 2 with the alternative complement pathway

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Neomycin inhibits glycoprotein C (gC)-dependent binding of herpes simplex virus type 1 to cells and also inhibits postbinding events in entry

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Herpes simplex virus glycoprotein D acquires mannose 6-phosphate residues and binds to mannose 6-phosphate receptors.

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Analysis of the contributions of herpes simplex virus type 1 membrane proteins to the induction of cell-cell fusion

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11 July 2018

Identification of structural features of heparin required for inhibition of herpes simplex virus type 1 binding

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11 July 2018

A heterologous heparin-binding domain can promote functional attachment of a pseudorabies virus gC mutant to cell surfaces.

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11 July 2018

Sequential isolation of proteoglycan synthesis mutants by using herpes simplex virus as a selective agent: evidence for a proteoglycan-independent virus entry pathway.

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Localization of a functional site on herpes simplex virus type 1 glycoprotein C involved in binding to cell surface heparan sulphate

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11 July 2018

Identification of functional regions of herpes simplex virus glycoprotein gD by using linker-insertion mutagenesis

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Fc and C3 receptors induced by herpes simplex virus on cultured human endothelial cells

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11 July 2018

Mapping of the structural gene for the herpes simplex virus type 2 counterpart of herpes simplex virus type 1 glycoprotein C and identification of a type 2 mutant which does not express this glycoprotein

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Virus-specific glycoproteins associated with the nuclear fraction of herpes simplex virus type 1-infected cells

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Glycoprotein C of herpes simplex virus type 1: characterization of O-linked oligosaccharides

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Detailed analysis of the portion of the herpes simplex virus type 1 genome encoding glycoprotein C

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Interaction of viruses with cell surface receptors.

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Localization and synthesis of an antigenic determinant of herpes simplex virus glycoprotein D that stimulates the production of neutralizing antibody

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Antigenic variants of herpes simplex virus selected with glycoprotein-specific monoclonal antibodies

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Herpes simplex virus type 1 glycoprotein C-negative mutants exhibit multiple phenotypes, including secretion of truncated glycoproteins

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Molecular basis of the glycoprotein-C-negative phenotype of herpes simplex virus type 1 macroplaque strain

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Inhibitory effect of heparin on herpes simplex virus

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Proteins specified by herpes simplex virus. V. Purification and structural proteins of the herpesvirion

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Herpes simplex virus glycoproteins associated with different morphological entities projecting from the virion envelope

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Putative glycoprotein gene of varicella-zoster virus with variable copy numbers of a 42-base-pair repeat sequence has homology to herpes simplex virus glycoprotein C

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C3b receptor activity on transfected cells expressing glycoprotein C of herpes simplex virus types 1 and 2.

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Demonstration and mapping of highly carbohydrate-dependent epitopes in the herpes simplex virus type 1-specified glycoprotein C.

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Effect of polylysine on the early stages of infection of wild type pseudorabies virus and of mutants defective in gIII.

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Glycoprotein C-dependent attachment of herpes simplex virus to susceptible cells leading to productive infection

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Soluble forms of herpes simplex virus glycoprotein D bind to a limited number of cell surface receptors and inhibit virus entry into cells

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Identification of herpes simplex virus type 1 glycoproteins interacting with the cell surface

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Identification of C3b-binding regions on herpes simplex virus type 2 glycoprotein C

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Antigenic and functional analysis of a neutralization site of HSV-1 glycoprotein D.

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Interaction of glycoprotein gIII with a cellular heparinlike substance mediates adsorption of pseudorabies virus

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Structure of O-glycosidically linked oligosaccharides synthesized by the insect cell line Sf9.

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Enhanced secretion from insect cells of a foreign protein fused to the honeybee melittin signal peptide

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BHV-1 adsorption is mediated by the interaction of glycoprotein gIII with heparinlike moiety on the cell surface

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Bovine herpesvirus 1 attachment to permissive cells is mediated by its major glycoproteins gI, gIII, and gIV

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Glycoprotein C of herpes simplex virus type 1 plays a principal role in the adsorption of virus to cells and in infectivity

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Activity of herpes simplex virus type 1-specified glycoprotein C antigenic site II epitopes reversibly modulated by peripheral fucose or galactose units of glycoprotein oligosaccharides

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Involvement of glycoprotein C (gC) in adsorption of herpes simplex virus type 1 (HSV-1) to the cell

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Herpes simplex virus glycoprotein C is a receptor for complement component iC3b

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Characterization of a recombinant herpes simplex virus which expresses a glycoprotein D lacking asparagine-linked oligosaccharides

1 reference

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Absence of asparagine-linked oligosaccharides from glycoprotein D of herpes simplex virus type 1 results in a structurally altered but biologically active protein

1 reference

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Infection of polarized MDCK cells with herpes simplex virus 1: two asymmetrically distributed cell receptors interact with different viral proteins

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Penetration of cells by herpes simplex virus does not require a low pH-dependent endocytic pathway

1 reference

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Structural basis of C3b binding by glycoprotein C of herpes simplex virus

1 reference

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Genetic analysis of type-specific antigenic determinants of herpes simplex virus glycoprotein C.

1 reference

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Carbohydrates in herpesvirus infections

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=189189

11 July 2018

The different interactions of a gIII mutant of pseudorabies virus with several different cell types

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=189189

11 July 2018

Herpes simplex virus type 1 entry through a cascade of virus-cell interactions requires different roles of gD and gH in penetration

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=189189

11 July 2018

Association of ICP0 but not ICP27 with purified virions of herpes simplex virus type 1

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=189189

11 July 2018

A novel herpes simplex virus glycoprotein, gL, forms a complex with glycoprotein H (gH) and affects normal folding and surface expression of gH

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=189189

11 July 2018

Cell surface receptors for herpes simplex virus are heparan sulfate proteoglycans

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=189189

11 July 2018

Construction and properties of a mutant of herpes simplex virus type 1 with glycoprotein H coding sequences deleted

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=189189

11 July 2018

Membrane proteins specified by herpes simplex viruses. III. Role of glycoprotein VP7(B2) in virion infectivity

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=189189

11 July 2018

Glycoprotein C-independent binding of herpes simplex virus to cells requires cell surface heparan sulphate and glycoprotein B.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=189189

24 September 2018

Mapping of Heparin-Binding Structures on Bovine Herpesvirus 1 and Pseudorabies Virus gIII Glycoproteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=189189

24 September 2018

Glycoprotein C of herpes simplex virus 1 acts as a receptor for the C3b complement component on infected cells

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=189189

24 September 2018

A virion-associated glycoprotein essential for infectivity of herpes simplex virus type 1

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=189189

24 September 2018

Virus Infection of Endothelial Cells

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=189189

24 September 2018

Phylogeny of the third component of complement, C3: Analysis of the conservation of human CR1, CR2, H, and B binding sites, concanavalin A binding sites, and thiolester bond in the C3 from different species

1 reference

https://pubmed.ncbi.nlm.nih.gov/7769707

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Evidence for multiple sites of interaction in C3 for complement receptor type 2 (C3d/EBV receptor, CD21)

1 reference

https://pubmed.ncbi.nlm.nih.gov/7769707

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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