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#19545528   2009/11/03 Save this To Up

Giardia lamblia: immunogenicity and intracellular distribution of GHSP-115, a member of the Giardia head-stalk family of proteins.

Giardia lamblia, a protozoan causing diarrheal outbreaks, is one of the main pathogens monitored in developed countries. Immunoscreening of G. lamblia expression library using the monoclonal antibodies (mAb) against G. lamblia, identified a subset of antigenic proteins in this protozoan, which are proteins belonging to GHSP (Giardia head-stalk protein), GHSP115, GHSP138, and GHSP180. In order to map the epitope region of GHSP115, the corresponding open reading frame was dissected into three parts and expressed as recombinant proteins with histidine tags. Western blot analysis of these recombinant proteins with mAbs reacting with GHSP115 indicated that one-third of the C-terminus of GHSP115 showed immunoreactivity with the mAb. Intracellular location of GHSP115 was examined both in trophozoites and encysting cells of G. lamblia by an immunofluorescence assay, indicating that location of GHSP115 varies during encystation. These results suggest that GHSP115 is an abundant and antigenic protein, which is differentially localized during life cycle of G. lamblia.

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#18456259   2008/06/02 Save this To Up

Giardia duodenalis: adhesion-deficient clones have reduced ability to establish infection in Mongolian gerbils.

The role of Giardia duodenalis surface molecules in the attachment of trophozoites to epithelial cells has been established through the dual strategies of characterizing G. duodenalis clones with deficient adhesion and blocking experiments with surface-specific monoclonal antibodies. Also, the infectivity of the analyzed clones was tested using Mongolian gerbils as experimental model. Two adhesion-deficient G. duodenalis clones, C6 and C7, were isolated from the wild type C5 clone which in turn was obtained from the WB strain. The adhesion efficiencies of C6 and C7 clones (48.2+/-4.9 and 32.6+/-2.4, respectively) were significantly lower as compared with WB strain or C5 clone (82.8+/-6.4 and 79.9+/-7.9). Analysis of radiolabel surface proteins by 1D and 2D SDS-PAGE revealed prominently labelled 28 and 88 kDa components in C6 and C7 clones and a major 200 kDa protein in the C5 clone and the WB strain. The 88 and 200 kDa components are acidic proteins by two-dimensional electrophoretic analyses. The most striking difference between wild-type and adhesion-deficient Giardia trophozoites was the reduced expression of a 200 kDa surface protein in the latter. Significantly, a mAb (IG3) specific for the 200 kDa protein that reacted with more than 99% of WB and C5 trophozoites and less than 1% of C6 and C7 trophozoites as determined by indirect immunofluorescence inhibited the adhesion of trophozoites from WB and C5 clone to Madin Darby Canine Kidney cells by 52% and 40.9%, respectively, suggesting a participation of this antigen in adherence. Finally, the functional relevance of trophozoite adhesion to epithelial cells was indicated by the reduced capacity of the adhesion-deficient clones to establish the infection in Mongolian gerbils.

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#12641416   2003/03/18 Save this To Up

Detection of Cryptosporidium parvum and Giardia lamblia carried by synanthropic flies by combined fluorescent in situ hybridization and a monoclonal antibody.

Wild-caught synanthropic flies were tested for the presence of Cryptosporidium parvum and Giardia lamblia on their exoskeletons and in their digestive tracks by fluorescent in situ hybridization and fluorescein isothiocyanate (FITC)-conjugated monoclonal antibody (MAb) against Cryptosporidium and Giardia cell wall epitopes. The levels of C. parvum were positively correlated with the levels of G. lamblia, indicating a common source of contamination. The majority of oocysts and cysts were potentially viable (C. parvum = 80% and G. lamblia = 69%). More G. lamblia cysts occurred on the exoskeleton of the flies than within the digestive tracts; the opposite relationship was observed for C. parvum. No genotype other than C. parvum G2 was found to be associated with flies. Because filth flies carry viable C. parvum oocysts and G. lamblia cysts acquired naturally from unhygienic sources, they can be involved in the epidemiology of cryptosporidiosis and giardiasis. Fluorescent oligonucleotide probes used together with FITC-conjugated MAb represent a convenient and cost-effective technique for rapid and specific identification of human-infectious species of Cryptosporidium and Giardia mechanically transported by flies, and for the assessment of the viability of these pathogens.

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#12541282   2003/01/23 Save this To Up

Analysis-only detection of Giardia by combining immunomagnetic separation and two-color flow cytometry.

Giardia is a protozoan parasite of concern to water utilities. Giardia detection relies on cyst isolation and confirmation with the use of fluorescence microscopy. It is of interest to develop a flow cytometric (FCM) method that reliably detects one cyst in 10 L of water. To date all available antibodies have targeted the same epitope on the cyst wall. To achieve a reliable method, two independent probes are required.

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#8801550   1996/10/01 Save this To Up

Electron microscopical investigation of surface alterations on Giardia lamblia trophozoites after exposure to a cytotoxic monoclonal antibody.

The present study describes a transmission electron microscopical investigation of trophozoites from Giardia lamblia clone GS/M-83-H7 after exposure to monoclonal antibody (MAb) G10/4. From previous studies it is known that this antibody immunoreacts with the parasite's major surface antigen VSP (variable surface protein) and exhibits a complement-independent cytotoxic effect on trophozoites of clone GS/M-83-H7. Our investigations revealed that cytotoxicity of MAb G10/4 is associated with shedding of VSP-containing membrane vesicles from the parasite surface and a concomitant partial disruption of the cellular membrane. These morphological alterations depend on the cross-linking capacity of the antibody because the immunoreactivity of respective monovalent F(ab)' has no significant influence on the cell-surface structure. These findings indicate that the membrane-disintegrative activity of MAb G10/4 may be responsible for the parasitocidal function of the antibody.

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#7525336   1994/12/07 Save this To Up

Giardia lamblia: traffic of a trophozoite variant surface protein and a major cyst wall epitope during growth, encystation, and antigenic switching.

Both trophozoites and cysts of Giardia lamblia have unique outer surfaces that protect them from very different hostile environments. However, little is known about the transport of these important molecules to the cell surface. We used monospecific anti-recombinant TSA 417 antibodies and mAb 8C5 in double label immunoelectron microscopy to compare the localization and transport of this major trophozoite surface antigen (TSA) with that of a prominent cyst wall epitope during vegetative growth, encystation, and antigenic switching in vitro. TSA 417 is a marker of the constitutive transport of the major plasma membrane protein, while the 8C5 epitope traces a differentiation-regulated secretory pathway to the cyst wall. Both proteins localized to the nuclear envelope endoplasmic reticulum (ER) cisternae, ER, and cytoplasmic membrane cisternae, reflecting their site of synthesis, but only the differentiation-specific epitope 8C5 localized to the encystation-specific vesicles (ESV). These large secretory vesicles form only during encystation and transport cyst antigens to the nascent wall. In contrast, only TSA 417 was found on the outer surface of the plasmalemma of trophozoites and encysting cells and underlaying the walls of many cysts, while only 8C5 localized to the cyst wall. As encystation progressed, TSA 417 disappeared from the plasmalemma and increased in the lysosome-like PV and other large cytoplasmic vesicles. In contrast to their segregation in the ESV and on the cell surface, both TSA 417 and 8C5 were found in the peripheral vesicles, presumably an endocytic compartment. We propose that this may be the initiation of a stage in differentiation-driven antigenic switching of TSA 417, in which this antigen is no longer synthesized or exported to the plasmalemma, but is taken back inside the cell.

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#8050777   1994/09/06 Save this To Up

Characterization of monoclonal antibodies to conserved antigens of Entamoeba histolytica and E. dispar and development of a stool ELISA.

Eight murine monoclonal antibodies (MAbs) were generated against Entamoeba histolytica NIH:200. All MAbs reacted with three axenic strains of E. histolytica, NIH:200, HM-1: IMMS, and SAW 1734R clAR, but not with enteric bacteria or Giardia lamblia. Five of the MAbs reacted with low-molecular-weight, periodate-sensitive antigens of 14-21 kD, while one (AB31) reacted with high-molecular-weight, 90 to 200-kD protein determinants. MAb PC14 appeared to be specific for antigen in its native state. Another MAb (BB12) agglutinated live trophozoites and caused membrane fluorescence in contrast to the five other MAbs tested. Although BB12 reacted with the same 14 to 21-kD band on Western blot as AC55, the latter reacted with different cytoplasmic epitopes. All the MAbs reacted to five pathogenic (E. histolytica) and six nonpathogenic (E. dispar) clinical isolates. These MAbs may be helpful for studying conserved antigens of E. histolytica and were used to develop a sandwich ELISA for the diagnosis of intestinal amoebiasis. The assay was sensitive to 60 ng of E. histolytica antigen. A comparative study of microscopic examination of stool samples and the sandwich ELISA was conducted on 102 samples from patients with gastrointestinal complaints. The ELISA could detect all microscopically positive samples with a sensitivity of 100% and specificity of 93%. A sandwich ELISA using a monoclonal antibody to conserved antigens of E. histolytica has the potential to be a reliable method for the diagnosis of intestinal amoebiasis.

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#7504633   1994/01/13 Save this To Up

Giardia lamblia: absence of cyst antigens and reduced secretory vesicle formation and bile salt uptake in an encystation-deficient subline.

Encystation of Giardia lamblia entails the appearance of a number of new antigens, as well as formation of a novel class of large encystation-specific secretory vesicles (ESV) that transport stage-specific proteins to the nascent cyst wall. The monoclonal antibody GCSA-1, which was raised against purified cyst walls, recognizes protein species of approximately 26-46 kDa that are regulated by exposure to bile (plus lactic acid) and alkaline pH, the factors that induce encystation. The GCSA-1 epitope is maximally expressed after approximately 14 hr of encystation and localizes to the interior, but not the membrane of the ESV as shown by frozen section immunoelectron microscopy. To further understand the process of encystation, we compared two sublines of strain WB that differ in their ability to encyst in vitro. Water-resistant cysts were not detected in subline A6 under conditions in which subline C6 formed approximately 2 x 10(5) cysts/ml. Moreover, subline A6 did not form ESV efficiently or detectably express antigens recognized by mAb GCSA-1 or by polyclonal anti-cyst sera. Finally, uptake of the bile salt taurocholate by A6 was reduced 4- to 20-fold, compared with that of C6, although transport by both strains was sodium-dependent and regulated by bile salt starvation. The decrease in bile salt uptake by A6 may be related to its defect in encystation.

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#8106183   1994/03/23 Save this To Up

Characterization and biological activities of anti-Brugia pahangi tubulin monoclonal antibodies.

Three monoclonal antibodies (mAb) specific to beta-tubulin were used to investigate the heterogeneity of tubulins from nematodes and mammals. Western blot analysis of one-dimensional SDS-PAGE showed that anti-Brugia pahangi tubulin mAb 1B6 and P3D react with epitope(s) specific to nematode beta-tubulin and recognize tubulin from adults and microfilariae of B. pahangi, adult B. malayi and Dirofilaria immitis, eggs of Haemonchus contortus and adult Ascaris suum. However, the same mAb did not recognize tubulin from trophozoites of Giardia lamblia, pig brain or 3T3 mouse fibroblast cells. In two-dimensional SDS-PAGE, mAb 1B6 recognized one isoform of beta-tubulin and mAb P3D recognized two beta-tubulin isoforms. Limited proteolysis showed that mAb 1B6 reacted with the amino-terminal fragments of beta-tubulin. In contrast, mAb P3D recognized the carboxy-terminal fragments of beta-tubulin. In ELISA, mAb P3D reacted with an 18 amino acid peptide corresponding to residues 430-448 of B. pahangi beta-tubulin. These observations confirm that the epitope of mAb P3D is located on the extreme carboxy-terminal region. Immunogold labelling of adult B. pahangi sections with mAb P3D revealed the presence of beta-tubulin isoforms in the cuticle, hypodermal layer and somatic muscle blocks of B. pahangi. Under in vitro conditions, mAb P3D caused 80% reduction in worm viability, during exposure over 48 h.

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#1937758   1991/11/27 Save this To Up

Variant surface antigens of Giardia lamblia are associated with the presence of a thick cell coat: thin section and label fracture immunocytochemistry survey.

Giardia lamblia undergoes surface antigenic variation. The ultrastructural location of antigens on four different variants was studied by label fracture and immunocytochemistry with four monoclonal antibodies (MAbs), each of which recognized the predominant variant in a particular clone. Each Giardia clone and its reacting MAb showed similar findings. The entire surface of the organism was covered by a surface coat which contained the variant surface protein. The surface coat was densely and uniformly labeled. Unreacting MAbs failed to label the surface. Label-fractured Giardia trophozoites exposed to reactive MAb revealed a planar distribution of reactivity with no discernible relationship to visualized intramembranous particles. Unexpectedly, some Giardia trophozoites lacked a surface coat and consequently failed to react with the appropriate MAb. The biological relevance of coatless Giardia trophozoites is unknown. These findings localize the variant antigens to the surface coat of the parasite and identify a minority of the population which lacks a surface coat.

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