Search results for "Heparinase"
showing 3 items of 3 documents
Characterisation of disaccharide fragments from the enzymatic digestion of heparin by liquid secondary ion mass spectrometry
1988
Disaccharide fragments resulting from the enzymatic digestion of heparins with heparinase have been purified by gel filtration chromatography and directly analyzed by positive and negative ion liquid secondary ion mass spectrometry (LSIMS). Following the chromatographic purification from excess sodium salt, the mass spectra of di- and tetrasaccharide fragment mixtures enabled the identification of up to three covalently bound sulfate moieties per glycosaminoglycan-disaccharide unit, by means of their molecular ions, containing the corresponding alkali-counterions.
Human papillomavirus infection requires cell surface heparan sulfate.
2001
ABSTRACT Using pseudoinfection of cell lines, we demonstrate that cell surface heparan sulfate is required for infection by human papillomavirus type 16 (HPV-16) and HPV-33 pseudovirions. Pseudoinfection was inhibited by heparin but not dermatan or chondroitin sulfate, reduced by reducing the level of surface sulfation, and abolished by heparinase treatment. Carboxy-terminally deleted HPV-33 virus-like particles still bound efficiently to heparin. The kinetics of postattachment neutralization by antiserum or heparin indicated that pseudovirions were shifted on the cell surface from a heparin-sensitive into a heparin-resistant mode of binding, possibly involving a secondary receptor. Alpha-6…
Inhibition of Transfer to Secondary Receptors by Heparan Sulfate-Binding Drug or Antibody Induces Noninfectious Uptake of Human Papillomavirus
2007
ABSTRACT Infection with various human papillomaviruses (HPVs) induces cervical cancers. Cell surface heparan sulfates (HS) have been shown to serve as primary attachment receptors, and molecules with structural similarity to cell surface HS, like heparin, function as competitive inhibitors of HPV infection. Here we demonstrate that the N , N ′-bisheteryl derivative of dispirotripiperazine, DSTP27, efficiently blocks papillomavirus infection by binding to HS moieties, with 50% inhibitory doses of up to 0.4 μg/ml. In contrast to short-term inhibitory effects of heparin, pretreatment of cells with DSTP27 significantly reduced HPV infection for more than 30 h. Using DSTP27 and heparinase, we fu…