Dextran sulfate can act as an artificial receptor to mediate a type-specific herpes simplex virus infection via glycoprotein B

Dyer, Angela P.; Banfield, Bruce W.; Martindale, Diane; Spannier, D M; Tufaro, Frank

doi:10.1128/jvi.71.1.191-198.1997

Cited by 27 publications

(20 citation statements)

References 44 publications

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“…These polysaccharides include κ and λ carrageenans (Marchetti et al, 1995 ; Carlucci et al, 1997 , 1999a , b ; Zacharopoulos and Phillips, 1997 ), galactan sulfate (Damonte et al, 1996 ; Mazumder et al, 2002 ), galactofucan sulfate (Thompson and Dragar, 2004 ), fucan sulfate (Preeprame et al, 2001 ), spirulan (Hayashi K. et al, 1996 ; Hayashi T. et al, 1996 ), fucoidan (Ponce et al, 2003 ; Lee et al, 2004a ), rhamnan sulfate (Lee et al, 1999 ), chitin sulfate (Ishihara et al, 1993 ), and other uncharacterized polymers (Hasui et al, 1995 ; Witvrouw and De Clercq, 1997 ; Lee et al, 2004b ; Zhu et al, 2004 ). In addition, other polysaccharides investigated as mimics of heparan sulfate include chemically modified heparins (Herold et al, 1995 , 1997 ; Feyzi et al, 1997 ), non-anticoagulated heparin (Herold et al, 1997 ), pentosan polysulfate (Herold et al, 1997 ), and dextran sulfate (Marchetti et al, 1995 ; Neyts et al, 1995 ; Dyer et al, 1997 ; Herold et al, 1997 ).…”

Section: Heparan Sulfate Structures That Interact With Viral Glycopromentioning

confidence: 99%

Sulfotransferase and Heparanase: Remodeling Engines in Promoting Virus Infection and Disease Development

et al. 2018

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An extraordinary binding site generated in heparan sulfate (HS) structures, during its biosynthesis, provides a unique opportunity to interact with multiple protein ligands including viral proteins, and therefore adds tremendous value to this master molecule. An example of such a moiety is the sulfation at the C3 position of glucosamine residues in HS chain via 3-O sulfotransferase (3-OST) enzymes, which generates a unique virus-cell fusion receptor during herpes simplex virus (HSV) entry and spread. Emerging evidence now suggests that the unique patterns in HS sulfation assist multiple viruses in invading host cells at various steps of their life cycles. In addition, sulfated-HS structures are known to assist in invading host defense mechanisms and initiating multiple inflammatory processes; a critical event in the disease development. All these processes are detrimental for the host and therefore raise the question of how HS-sulfation is regulated. Epigenetic modulations have been shown to be implicated in these reactions during HSV infection as well as in HS modifying enzyme sulfotransferases, and therefore pose a critical component in answering it. Interestingly, heparanase (HPSE) activity is shown to be upregulated during virus infection and multiple other diseases assisting in virus replication to promote cell and tissue damage. These phenomena suggest that sulfotransferases and HPSE serve as key players in extracellular matrix remodeling and possibly generating unique signatures in a given disease. Therefore, identifying the epigenetic regulation of OST genes, and HPSE resulting in altered yet specific sulfation patterns in HS chain during virus infection, will be a significant a step toward developing potential diagnostic markers and designing novel therapies.

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Section: Heparan Sulfate Structures That Interact With Viral Glycopromentioning

confidence: 99%

Sulfotransferase and Heparanase: Remodeling Engines in Promoting Virus Infection and Disease Development

et al. 2018

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“…Another mutant cell line, sog9, was further selected from gro2C cells and expresses neither HS nor CS (2). These mutant cells have been useful for studies of binding of herpes simplex virus type 1 (HSV-1) glycoprotein B (gB) and gC proteins to cell surface GAGs (3,9). D8L and A27L proteins were tested with these cells for their binding specificity (Fig.…”

Section: Soluble Vaccinia Virus D8l Protein Bound To Cell Surface Cs mentioning

confidence: 99%

Vaccinia Virus Envelope D8L Protein Binds to Cell Surface Chondroitin Sulfate and Mediates the Adsorption of Intracellular Mature Virions to Cells

Hsiao

Chung

Chang

1999

J Virol

236

106

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We previously showed that an envelope A27L protein of intracellular mature virions (IMV) of vaccinia virus binds to cell surface heparan sulfate during virus infection. In the present study we identified another viral envelope protein, D8L, that binds to chondroitin sulfate on cells. Soluble D8L protein interferes with the adsorption of wild-type vaccinia virions to cells, indicating a role in virus entry. To explore the interaction of cell surface glycosaminoglycans and vaccinia virus, we generated mutant viruses from a control virus, WR32-7/Ind14K (A27L+ D8L+) to be defective in expression of either the A27L or the D8L gene (A27L+D8L− or A27L− D8L+) or both (A27L− D8L−). The A27L+D8L+ and A27L− D8L+ mutants grew well in BSC40 cells, consistent with previous observations. However, the IMV titers of A27L+ D8L− and A27L− D8L− viruses in BSC40 cells were reduced, reaching only 10% of the level for the control virus. The data suggested an important role for D8L protein in WR32-7/Ind14K virus growth in cell cultures. A27L protein, on the other hand, could not complement the functions of D8L protein. The low titers of the A27L+ D8L− and A27L−D8L− mutant viruses were not due to defects in the morphogenesis of IMV, and the mutant virions demonstrated a brick shape similar to that of the control virions. Furthermore, the infectivities of the A27L+ D8L− and A27L−D8L− mutant virions were 6 to 10% of that of the A27L+ D8L+ control virus. Virion binding assays revealed that A27L+ D8L− and A27L− D8L− mutant virions bound less well to BSC40 cells, indicating that binding of viral D8L protein to cell surface chondroitin sulfate could be important for vaccinia virus entry.

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“…The differential activity of HBB(112-147) against HSV-1 and HSV-2 may reflect differences in the glycoprotein sequence and/or composition of both viruses. In fact, both viruses differ in their sensitivity to polyanions (Hutton et al, 1973) and polycations (Langeland et al, 1987(Langeland et al, , 1988, differential binding to heparan sulfate (HS)/heparin chains (Herold et al, 1996;Trybala et al, 2000) and stimulation of viral infection in glycosaminoglycan-deficient cells by dextran sulfate (Dyer et al, 1997). Collectively these data suggest that HBB(112-147) may interact with an HSV-2 specific glycoprotein that is important for viral attachment and/or entry.…”

Section: Discussionmentioning

confidence: 99%

A Placenta Derived C-Terminal Fragment of β-Hemoglobin With Combined Antibacterial and Antiviral Activity

et al. 2020

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The placenta acts as physical and immunological barrier against the transmission of viruses and bacteria from mother to fetus. However, the specific mechanisms by which the placenta protects the developing fetus from viral and bacterial pathogens are poorly understood. To identify placental peptides and small proteins protecting from viral and bacterial infections, we generated a peptide library from 10 kg placenta by chromatographic means. Screening the resulting 250 fractions against Herpes-Simplex-Virus 2 (HSV-2), which is rarely transmitted through the placenta, in a cellbased system identified two adjacent fractions with significant antiviral activity. Further rounds of chromatographic purification and anti-HSV-2 testing allowed to purify the bioactive peptide. Mass spectrometry revealed the presence of a 36-mer derived from the C-terminal region of the hemoglobin β subunit. The purified and corresponding chemically synthesized peptide, termed HBB(112-147), inhibited HSV-2 infection in a dose-dependent manner, with a mean IC 50 in the median µg/ml range. Full-length hemoglobin tetramer had no antiviral activity. HBB(112-147) did not impair infectivity by direct targeting of the virions but prevented HSV-2 infection at the cell entry level. The peptide was inactive against Human Immunodeficiency Virus Type 1, Rubella and Zika virus infection, suggesting a specific anti-HSV-2 mechanism. Notably, HBB(112-147) has previously been identified as broad-spectrum antibacterial agent. It is abundant in placenta, reaching concentrations between 280 and 740 µg/ml, that are well sufficient to

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Dextran sulfate can act as an artificial receptor to mediate a type-specific herpes simplex virus infection via glycoprotein B

Cited by 27 publications

References 44 publications

Sulfotransferase and Heparanase: Remodeling Engines in Promoting Virus Infection and Disease Development

Sulfotransferase and Heparanase: Remodeling Engines in Promoting Virus Infection and Disease Development

Vaccinia Virus Envelope D8L Protein Binds to Cell Surface Chondroitin Sulfate and Mediates the Adsorption of Intracellular Mature Virions to Cells

A Placenta Derived C-Terminal Fragment of β-Hemoglobin With Combined Antibacterial and Antiviral Activity

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