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herpes simplex/carbohydrate
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Inhibition of herpes simplex virus infection by negatively charged and neutral carbohydrate polymers.
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Different natural and semisynthetic polysaccharides were evaluated for their inhibitory effect on in vitro replication of herpes simplex virus (HSV) types 1 and 2. Some neutral and negatively charged carbohydrates were able to inhibit viral infection by interfering mainly with the adsorption process
Demonstration and mapping of highly carbohydrate-dependent epitopes in the herpes simplex virus type 1-specified glycoprotein C.
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The carbohydrate dependence of epitopes in the herpes simplex virus type 1-specified glycoprotein C (gC) was studied using a new solid-phase assay procedure. Glycoprotein C, coated on 96-well microtitre plates, was treated with sialidase and increasing concentrations of periodate. A sequential
Host cell-induced differences in O-glycosylation of herpes simplex virus gC-1. I. Structures of nonsialylated HPA- and PNA-binding carbohydrates.
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Lectins with narrow oligosaccharide specificities were established as probes to study the host cell influence on the biosynthesis of O-linked oligosaccharides of the herpes simplex virus type 1 (HSV-1)-specified glycoprotein C (gC-1). We found that only gC-1 and no other glycoprotein bound to the
Removal of N-linked carbohydrates decreases the infectivity of herpes simplex virus type 1.
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Purified preparations of herpes simplex virus type 1 Angelotti were digested with the exoglycosidases sialidase, beta-galactosidase, N-acetyl-beta-D-glucosaminidase and alpha-mannosidase, and with the endoglycosidases Endo-H and Endo-F. It was found that treatment of virions with Endo-F specifically
Binding of surfactant protein A (SP-A) to herpes simplex virus type 1-infected cells is mediated by the carbohydrate moiety of SP-A.
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Pulmonary surfactant protein A (SP-A) has been shown to act as an opsonin in the phagocytosis of viruses by alveolar macrophages. To determine whether SP-A binds to viral proteins and which part of the SP-A molecule is involved in this interaction, binding studies were undertaken. SP-A was labeled
O-glycosidic carbohydrate-peptide linkages of Herpes simplex virus glycoproteins.
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Electrophoretically purified HSV-specified glycoproteins with radiolabelled carbohydrates were subjected to mild alkaline borohydride treatment (0.5 M NaOH and 0.5 M NaBH4). The treatment liberated significant amounts of the labelled oligosaccharides. The latter demonstrated molecular weights of
Different populations of herpes simplex virus glycoprotein C discriminated by the carbohydrate-binding characteristics of N-acetylgalactosamine specific lectins (soybean and Helix pomatia). Brief report.
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From the herpes simplex virus specified glycoprotein C two fractions were isolated with affinity either for Helix pomatia lectin (HPA) or soybean lectin (SBA). The data indicated that HPA and SBA, despite their mutual main specificity for N-acetylgalactosamine, recognize structurally different gC
Herpes simplex virus type 1 infection increases the carbohydrate binding activity and the secretion of cellular galectin-3.
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Galectin-3 binds beta-galactoside-containing sugars and is a chemoattractant for monocytes, macrophages, and neutrophils. Galectin-3 was identified by mass spectrometry from an anti-gI affinity column; however, we determined that galectin-3 did not bind gI, but rather that HSV-1 infection increased
C3b receptor activity on transfected cells expressing glycoprotein C of herpes simplex virus types 1 and 2.
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Glycoprotein C from herpes simplex virus type 1 (gC-1 from HSV-1) acts as a receptor for the C3b fragment of the third component of complement on HSV-1-infected cell surfaces. Direct binding assays with purified gC-1 and C3b demonstrate that other viral and cellular proteins are not required for
Expression of herpes simplex virus type 1 glycoprotein D deletion mutants in mammalian cells.
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Glycoprotein D (gD) is a viron envelope component of herpes simplex virus types 1 and 2. We have previously defined seven monoclonal antibody (MAb) groups which recognize distinct epitopes on the mature gD-1 protein of 369 amino acids. MAb groups VII, II, and V recognize continuous epitopes at
Mannan-binding protein and bovine conglutinin mediate enhancement of herpes simplex virus type 2 infection in mice.
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A broad range of plant lectins have recently been shown to inhibit the infectivity of herpes simplex virus type 1 (HSV-1) in vitro. We decided to investigate the role of mammalian lectins in infection with herpes simplex virus. Two lectins, conglutinin and mannan-binding protein (also called
An effector phenotype of CD8+ T cells at the junction epithelium during clinical quiescence of herpes simplex virus 2 infection.
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Herpes simplex virus 2 infection is characterized by cycles of viral quiescence and reactivation. CD8(+) T cells persist at the site of viral reactivation, at the genital dermal-epidermal junction contiguous to neuronal endings of sensory neurons, for several months after herpes lesion resolution.
HLA class I molecules are not transported to the cell surface in cells infected with herpes simplex virus types 1 and 2.
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To assess the effect of herpes simplex virus (HSV) on assembly and transport of class I MHC molecules, we compared class I MHC immunoprecipitated from metabolically labeled infected and uninfected human dermal fibroblasts. The immunoprecipitates were analyzed by isoelectric focusing, allowing
The single base pair substitution responsible for the Syn phenotype of herpes simplex virus type 1, strain MP.
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Nucleotide sequences were determined for portions of the genomes of the syncytial (Syn) mutant of herpes simplex virus type 1, strain MP, and the related wild-type strain mP. Comparisons of the nucleotide sequences showed only 1 bp difference between the DNAs of strains MP and mP in the region to
Antiviral effect of a polysaccharide from Sclerotium glucanicum towards herpes simplex virus type 1 infection.
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Among different neutral polysaccharides from natural sources, scleroglucan from Sclerotium glucanicum significantly inhibits the replication of herpes simplex virus type 1 on Vero cells. Scleroglucan belongs to a class of exopolymers, expressed by members of genus Sclerotium and consists of a linear
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