Molecular characterization of the surface and cyst fluid components of Taenia crassiceps

Parasitology ◽  
1990 ◽  
Vol 101 (1) ◽  
pp. 115-125 ◽  
Author(s):  
S. Lamsam ◽  
D. P. McManus
Keyword(s):  
Serum Proteins ◽  
Cyst Fluid ◽  
Surface Proteins ◽  
Lectin Affinity Chromatography ◽  
Taenia Crassiceps ◽  
Tegumental Surface ◽  
Lectin Affinity ◽  
Terminal Galactose ◽  
Sds Page

SUMMARYInformation relating to the characterization of cestode surface macromolecules is limited. This is especially the case with Taenia crassiceps, a well-recognized model for the study of larval cestodiasis. Here, the protein and glycoprotein composition of the tegumental surface and cyst fluid of the metacestode have been investigated using radio-isotope labelling, immunoprecipitation, SDS–PAGE and lectin affinity chromatography. A restricted number of surface proteins was labelled with the 125I/Iodogen method although the majority were immunogenic; in contrast an array of cyst fluid antigens were labelled. Host serum proteins, including immunoglobulins, were identified on the surface and in the cyst fluid. Some of the 125I-labelled surface proteins, including a 37 kDa molecule, have been shown to be glycoproteins and probably contain-D-mannose and/or D-glucose; there is limited or no N-acetylglucosamine and no terminal galactose present on these components. A 37 kDa surface molecule, possibly the same glycoprotein, was also precipitated by infection sera and this may endorse the theory that highly immunogenic carbohydrates are continuously shed by T. crassiceps as a mechanism for diverting the immune response of the host. Radio-iodinated and biosynthetically labelled T. crassiceps antigens were highly cross-reactive with antibody raised to other cestodes and not one antigen was identified as a possible candidate for use in specific immunodiagnosis of any of the important taeniid infections.

scholarly journals Characterization of Glycoproteins in Pancreatic Cyst Fluid Using a High-Performance Multiple Lectin Affinity Chromatography Platform

2013 ◽  
Vol 13 (1) ◽  
pp. 289-299 ◽  
Author(s):  
Francisca Owusu Gbormittah ◽  
Brian B. Haab ◽  
Katie Partyka ◽  
Carolina Garcia-Ott ◽  
Marina Hancapie ◽  
...  
Keyword(s):  
Affinity Chromatography ◽  
High Performance ◽  
Pancreatic Cyst ◽  
Cyst Fluid ◽  
Lectin Affinity Chromatography ◽  
Lectin Affinity ◽  
Pancreatic Cyst Fluid

scholarly journals Further Characterization of an Interleukin-2-1Ike Cytokine Produced byXenopus LaevisT Lymphocytes

1993 ◽  
Vol 3 (3) ◽  
pp. 231-238 ◽  
Author(s):  
Laura Haynes ◽  
Nicholas Cohen
Keyword(s):  
T Cell ◽  
South African ◽  
Interleukin 2 ◽  
Biological Properties ◽  
Biologically Active ◽  
Lectin Affinity Chromatography ◽  
Sds Page ◽  
Cell Mitogen ◽  
Clawed Frog

A T-cell growth factor (TCGF) is produced by antigen- or mitogen-stimulated T lymphocytes from the South African clawed frogXenopus laevis. This study further defines the physical and biological properties of this cytokine and demonstrates that TCGF is biochemically similar to mammalian interleukin-2 (IL-2). Biologically active TCGF eluted from SDS-PAGE displays a Mrof 16 kD and lectin-affinity chromatography indicates that the three-dimensionmal configuration of carbohydrates on TCGF and human IL-2 is similar. Secretion of TCGF is detectable 1 day after stimulation of splenocytes with the T-cell mitogen phytohemagglutinin (PHA) and peaks following 2 to 3 days of stimulation. Finally, despite the biological and physical similarities betweenXenopusTCGF and mammalian IL-2, anti-human IL-2 monoclonal antibodies do not recognizeXenopusTCGF.

scholarly journals Isolation and Partial Characterization of an Antiviral Proteolytic Fraction from the Venom of Echis Carinatus Sochureki

2008 ◽  
Vol 1 (1) ◽  
pp. 21-26 ◽  
Author(s):  
G. Borkow ◽  
D. Marco ◽  
M. Ovadia
Keyword(s):  
Molecular Weight ◽  
Hemolytic Activity ◽  
Sendai Virus ◽  
Surface Proteins ◽  
Gelatinase Activity ◽  
Sds Page ◽  
Virion Envelope ◽  
Echis Carinatus ◽  
Viral Surface

The venom of the viper Echis carinatus sochureki suppresses the hemolytic activity of Sendai virus on human erythrocytes, when pre-incubated with the virions prior to their binding to cells. A fraction (C1), with an IC50 of 1.25 􀀁g/ml, was isolated from the venom. Fraction C1 possesses strong azocollase, azocaseinase and gelatinase activity. The proteolytic and anti-hemolytic potency of C1 depends on the period and temperature of incubation. Its antiviral activity is inhibited by Sodium-EDTA but not by PMSF. SDS PAGE of Sendai virus incubated with fraction C1 shows disappearance of several of the virion high molecular weight bands. We suggest that inhibition of the hemolytic activity of the virions is probably a result of the cleavage of viral surface proteins, such as the hemagglutinin-neuraminidase glycoprotein found on the virion envelope that mediates the absorption of the virus to cells.

scholarly journals Characterization of the Phytophagous Nematode Surface Coat to Provide New Strategies for Biocontrol

1995 ◽  
Author(s):  
Yitzhak Spiegel ◽  
Michael McClure ◽  
Itzhak Kahane ◽  
B.M. Zuckerman
Keyword(s):  
Surface Proteins ◽  
Surface Coat ◽  
Pasteuria Penetrans ◽  
Human Red Blood Cells ◽  
Sds Page ◽  
Meloidogyne Spp ◽  
Spore Attachment ◽  
New Strategies

Chemical composition and biological role of the surface coat (SC) of the root-knot nematodes, Meloidogyne spp. are described. SC proteins of M. incognita race 3 infective juveniles (J2) were characterized by electrophoresis and western blotting of extracts from radioiodine and biotin-labelled nematodes. J2 labelled with radioiodine and biotin released 125I and biotin-labelled molecules into water after 20 hours incubation, indicating that SC proteins may be loosely attached to the nematode. Antiserum to the principal protein reacted with the surface of live J2 and with surface proteins previously separated by electrophoresis. Human red blood cells (HRBC) adhered to J2 of several tylenchid nematodes over the entire nematode body. HRBC adhered also to nylon fibers coated with SC extracted from M. javanica J2; binding was Ca++/Mg++ dependent, and decreased when the nylon fibers were coated with bovine serum albumin, or pre-incubated with fucose and mannose. These experiments support a working hypothesis that RBC adhesion involves carbohydrate moieties of HRBC and carbohydrate-recognition domain(s) (CRD) distributed on the nematode surface. To our knowledge, this is the first report of a surface CRD i the phylum Nematoda. Gold-conjugated lectins and neoglycoproteins combined with silver enhancement have been used for the detection of carbohydrates and CRD, respectively, on the SC of M. javanica J2. Biotin reagents were used to trace surface proteins, specifically, on live J2. The labile and transitory nature of the SC was demonstrated by the dynamics of HRBC adherence to detergent-treated J2, J2 at different ages or fresh-hatched J2 held at various temperatures. SC recovery was demonstrated also by a SDS-PAGE profile. Monoclonal antibodies developed to a cuticular protein of M. incognita J2 gave a slight, but significant reduction in attachment of Pasteuria penetrans spores. Spore attachment as affected by several enzymes was inconsistent: alcian blue, which specifically blocks sulfyl groups, had no afffect on spore attachment. Treatment with cationized ferritin alone or catonized ferritin following monoclonal antibody caused significant decreases in spore attachment. Those results suggest a role in attachment by negatively charged groups.

Characterization of parasite antigens from human hydatid cyst fluid by SDS-PAGE and IEF

1985 ◽  
Vol 174 (1) ◽  
pp. 43-50 ◽  
Author(s):  
R. d'Amelio ◽  
O. Pontesilli ◽  
R. Dayal ◽  
F. de Rosa ◽  
M. Barnet ◽  
...  
Keyword(s):  
Hydatid Cyst ◽  
Cyst Fluid ◽  
Sds Page ◽  
Hydatid Cyst Fluid

Isolation, fractionation and partial characterization of the tegumental surface from protoscoleces of the hydatid organism, Echinococcus granulosus

Parasitology ◽  
1985 ◽  
Vol 90 (1) ◽  
pp. 111-129 ◽  
Author(s):  
D. P. McManus ◽  
N. J. Barrett
Keyword(s):  
Echinococcus Granulosus ◽  
Surface Membrane ◽  
Qualitative And Quantitative ◽  
Tegumental Surface ◽  
Sds Page ◽  
Pas Staining ◽  
Approximate Molecular Weight ◽  
Membrane Bound ◽  
Triton X

Several approaches were adopted for the disruption and removal of the tegumental surface from protoscoleces of the horse strain of the hydatid organism, Echinococcus granulosus. The effectiveness of each method and the purity of subsequent microthrix-enriched fractions obtained by differential centrifugation were evaluated by electron microscopy, by the amount of protein released and by the degree of enrichment of surface plasma membrane marker enzymes. Incubation in saponin for 10 min produced the purest microtriche preparation, but in low yield; freeze/thawing, incubation in Triton X-100 for 10 mm or in saponin for 20 min produced fractions containing significant amounts of relatively pure microtriches, but mild homogenization was a poor method for surface disruption and subsequent isolation of microtriches. Phosphodiesterase, adenosine triphosphatase (total and ouabain-inhibited), leucine aminopeptidase and glutamyltransferase were active in the protoscoleces but none were enriched in any of the microthrix fractions. In contrast, alkaline phosphatase, acid phosphatase, 5′ nucleotidase and maltase were enriched significantly in all of the isolated microtriche preparations, which suggests that these enzymes are predominantly surface membrane bound. The protein profiles of the microthrix-enriched fractions, following SDS—PAGE, were basically similar, although there were some qualitative and quantitative differences in the proteins released by each isolation procedure. Three major PAS-staining components were present in all the preparations and these probably originated from the glycocalyx. One of these PAS-positive components, with an approximate molecular weight of 110 kDa, may be a glycoprotein specific to the horse strain of E. granulosus.

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