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Query: UMLS:C0024530 (malaria)
 44,886 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Monoclonal antibodies (MAbs) which are reactive with several antigenically distinct variable antigen types were prepared by immunization with Trypanosoma brucei rhodesiense. Certain MAbs were shown to be specific for members of the genus Trypanosoma and not reactive with Leishmania spp. or Plasmodium falciparum by the indirect immunofluorescence assay. These genus-specific MAbs were used to identify the molecular location of these invariant antigen determinants in whole T. brucei rhodesiense antigen preparations. Two monoclonals reacted with a low-molecular-weight doublet of approximately 22,000 relative molecular weight on Western blots of whole trypanosome antigen preparations separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. These determinants did not appear to be on the variable surface glycoprotein molecule and were destroyed by trypsin digestion. Binding studies in which live, DEAE-purified, bloodstream trypanosomes were exposed to invariant antigen-specific MAbs suggested these determinants were accessible on living trypanosomes. Genus-specific MAbs also reacted with determinants present in sera from African trypanosomiasis patients in a dot immunobinding assay but not sera from patients with malaria or leishmaniasis. These results suggest that certain invariant molecules of African trypanosomes are immunogenic, possibly accessible on the trypanosome surface, and may be present as circulating invariant antigen in trypanosomiasis patients.
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PMID:Molecular identity and location of invariant antigens on Trypanosoma brucei rhodesiense defined with monoclonal antibodies reactive with sera from trypanosomiasis patients. 390 17

Previous studies have suggested that malaria induces changes in erythrocytic membrane permeability and susceptibility to osmotic lysis. The present study investigated erythrocytic transport of sodium with cells from Rhesus monkeys infected with Plasmodium knowlesi. Red blood cell sodium concentration was significantly elevated in 37 parasitized animals (21.8+/-1.2 mM; mean +/-SEM), as compared to 23 control animals (10.0+/-0.38 mM). The cellular sodium increased with the density of parasitemia and the cellular potassium decreased in proportion to the elevation of sodium. Nonparasitized as well as parasitized erythrocytes possessed this abnormality of cation metabolism. Effective chloroquine therapy reversed the changes over a period of 4 days. Active sodium outflux rate constants were depressed in animals with malaria (0.202+/-0.012), as compared to controls (0.325+/-0.027). Passive sodium influx rate constants were higher in infected monkeys (0.028+/-0.002) than in control animals (0.019+/-0.002). The cross incubation of malarial plasma with normal red blood cells induced a 22% diminution in active sodium outflux but no changes were observed in sodium influx. It is concluded that malaria alters erythrocytic sodium transport in all erythrocytes. The elevated intracellular sodium concentration is the net result of decreased sodium outflux and increased sodium influx. The plasmodium organism or the affected host may produce a circulating substance that is deleterious to erythrocytic membrane cation transport.
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PMID:Alterations of red blood cell sodium transport during malarial infection. 497 61

Serum samples from Aotus trivirgatus subsp. griseimembra monkeys obtained at different stages of a vaccination experiment were analyzed for total antibody titer to Plasmodium falciparum and were used for identifying protective antigens of the human malaria parasite. Total malarial antibody titers were higher in serum samples from protected monkeys (vaccinated with antigen in an adjuvant) than in those from unprotected monkeys (vaccinated with either antigen or adjuvant only). Parasite proteins were labeled with [3H]isoleucine, solubilized with nonionic detergent, and reacted with immune Aotus sera. Immunoprecipitates obtained were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and fluorography. Thirteen protein antigen bands in the molecular weight range 73,000 to 180,000 were resolved. Serum samples obtained from protected Aotus monkeys reacted more intensely with these proteins than samples from unprotected monkeys did. Evidence is presented that the protective antigen is not a single, normally nonimmunogenic, protein that is recognized only in protected monkeys. Rather, the present data indicate that a heightened immune response to multiple proteins correlated with in vivo protection to P. falciparum in Aotus monkeys. This finding may have a significant bearing on strategies for the development of a human P. falciparum vaccine.
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PMID:Plasmodium falciparum: protein antigens identified by analysis of serum samples from vaccinated Aotus monkeys. 636 Sep 1

The effect of normal human peripheral blood polymorphonuclear leucocytes on in vitro multiplication of Plasmodium falciparum malaria parasites was investigated. It was shown that normal neutrophils were able to phagocytose parasitized erythrocytes and free parasites and thus inhibit in vitro multiplication of the parasite. Stimulation of the neutrophils by phorbol myristate acetate, a potent stimulus of leucocyte oxidative metabolism, resulted in enhanced inhibition of parasite growth. Superoxide dismutase, scavenger of superoxide anion, catalase, inhibitor of hydrogen peroxide, and sodium azide, inhibitor of myeloperoxidase, did not abrogate the inhibitory ability of the neutrophils. The results indicate that polymorphonuclear leucocytes play an important role in the defence against P. falciparum malaria.
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PMID:Enhanced inhibition of in vitro multiplication of Plasmodium falciparum by stimulated human polymorphonuclear leucocytes. 638 Aug 30

The antibody response of mice to Plasmodium chabaudi adami and Plasmodium yoelii has been compared using a solid phase isotype-specific radioimmunoassay and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Serological cross-reactivity between these parasites was substantial. Studies using a radioimmunoassay detecting all classes of malaria-specific antibody demonstrated that during the early part of infection it was not possible to distinguish between homologous and heterologous reactions. Immunoprecipitation and sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed that 50% or more of the protein antigens detected were apparently shared by both parasites although the intensity of bands was always greater with homologous reactions. However, the distribution of isotypes in the antibody (Ab) response differed in the two infections. P. chabaudi infections were characterized by a predominant and persistent IgM response, moderate IgG2 and IgG3 and little significant IgG1 response during a primary infection. By contrast, IgM antibodies were transient in P. yoelii infection, IgG2 was the predominant isotype, and both IgG1 and IgG3 antibodies were present during a primary infection. These differences in isotypes were also detected when sera were tested on the heterologous antigen extracts suggesting that antigens shared by P. chabaudi and P. yoelii do not necessarily induce similar antibody responses in the two infections.
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PMID:Immunoglobulin isotype distribution of malaria-specific antibodies produced during infection with Plasmodium chabaudi adami and Plasmodium yoelii. 646 84

We have determined the N-terminal amino acid sequence of the first 25 amino acids of the histidine-rich protein (HisRP) isolated from granules of the avian malaria parasite Plasmodium lophurae. The protein was purified from cytoplasmic granules and shown to be 65.2 mol % histidine, close to the previously described value of 73 mol % histidine (Kilejian (1974) J. Biol. Chem. 249, 4650-4655). Ten of the first 25 residues were histidine, five of which formed the sequence His-His-His-His-His (positions 14-18). Also notable was the presence of eight acidic residues within the N-terminal 25 residues. HisRP contained no detectable carbohydrate. When the HisRP was biosynthetically labeled in cultured infected erythrocytes, incorporation of [3H]His greatly exceeded [3H]Ile. Labeled HisRP was not solubilized with 1% w/v Triton X-100 but could be solubilized with greater than or equal to 1% w/v sodium dodecyl sulfate. On sodium dodecyl sulfate-polyacrylamide gel electrophoresis the [3H]His labeled protein migrated as a doublet (Mr 53 000 and 50 000). Only one of these bands (Mr 53 000) comigrated with the Coomassie Blue stained protein isolated by the acid-extraction procedure from purified granules. The amino acid composition of HisRP and presence of five contiguous histidine residues in the sequence studied here suggests that other sequences of several contiguous histidine residues must exist in this molecule.
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PMID:N-terminal amino acid sequence of the histidine-rich protein from Plasmodium lophurae. 648 6

Monoclonal antibodies (MAb) against gametes of the chicken malaria Plasmodium gallinaceum have been derived. All reacted with the surface of extracellular gametes of the parasite in immunofluorescent antibody reactions and all agglutinated both male and female gametes. In the absence of active complement one mu isotype MAb, la 1-D5, mediated at least 95% suppression of infectivity of the parasites to Aedes aegypti mosquitoes. Individually, MAb of the gamma 1 or gamma 2a isotypes mediated only slight suppression in the absence of active complement. Certain combinations of these MAb, however, suppressed parasite infectivity by 90 to 95%. Suppression of infectivity by the MAb was shown to be mainly due to their effects on the events leading up to or including fertilization. Certain gamma 2a isotype MAb, which otherwise mediated minimal or no suppressive effect, completely abolished infectivity of the parasites if complement was present. No target antigen could be identified by immunoprecipitation of Triton X-100 extracts of surface radioiodinated zygotes or gametes of P. gallinaceum for the mu isotype MAb. All gamma isotype MAb precipitated the same three proteins of 240,000, 56,000, and 54,000 daltons under reducing conditions on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, from extracts of radioiodinated male and female gametes. These surface proteins on gametes of both sexes of P. gallinaceum thus appear to include target antigens of anti-gamete transmission blocking immunity.
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PMID:Monoclonal antibodies against surface determinants on gametes of Plasmodium gallinaceum block transmission of malaria parasites to mosquitoes. 663 Oct 12

Plasmodium knowlesi malaria-infected erythrocytes were radio-iodinated and several non-ionic, anionic and zwitterionic detergents were compared in their capacity to extract the labelled membrane proteins. The use of these detergents for antigen identification was tested by immunoprecipitation, after addition of Triton X-100 to some detergent extracts, using hyperimmune monkey antiserum and protein A-Sepharose. 125I-labelled antigens were specifically immunoprecipitated with all detergents tested, including the anionic detergents sodium dodecyl sulphate (SDS), deoxycholate and cholate; the zwitterions Zwittergent-312 and -314, CHAPS and Empigen BB, as well as several non-ionic detergents. The SDS-polyacrylamide gel electrophoresis patterns of 125I-labelled antigens varied after extraction with different detergents, there being no consistent pattern for detergents of a particular class. A total of 14 125I-labelled antigens were identified, 11 of them using Triton X-100. Some minor 125I-labelled antigens identified with Triton X-100 were immunoprecipitated in greater amount after extraction in other detergents. Most importantly, two antigens Mr 200 000 and 180 000 were detected only after extraction with deoxycholate or SDS.
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PMID:Solubilization and immunoprecipitation of 125I-labelled antigens from Plasmodium knowlesi schizont-infected erythrocytes using non-ionic, anionic and zwitterionic detergents. 670 93

Mature asexual stages of the malaria parasite Plasmodium Knowlesi synthesize proteins of Mr 180 000-225 000 that are expressed on the outer membrane of infected erythrocytes and which vary antigenically such that different parasite clones are specifically agglutinated with homologous antibody. Other non-agglutinable clones have been prepared which fail to express variant antigen on infected cells. Two agglutinable clones of different variant antigen phenotypes and a non-agglutinable cone were examined to determine the proportion of total malarial proteins represented by variant antigens. Malarial proteins were labelled with various radioactive amino acids and the sodium dodecyl sulphate--polyacrylamide gel patterns for the three clones compared by fluorography. The patterns were indistinguishable, the variant antigens being undetectable in analyses of total malarial proteins. Furthermore, these antigens were not detected by Coomassie Blue-staining of total cellular proteins after electrophoresis. Sodium dodecyl sulphate and Triton X-100 extracts of labelled cells were immunoprecipitated using a panel of sera of defined agglutination specificity. The variant antigens could not be detected in the fluorographic patterns of total malarial antigens immunoprecipitated by these sera. In contrast, after lactoperoxidase catalysed radio-iodination of intact schizont-infected cells, the 125I-variant antigens on the cell surface were identified by demonstrating their accessibility both to antibody and to trypsin with intact cells. Thus, the variant antigens are quantitatively very minor malarial proteins that can only be detected by methods which selectively analyse the subset of proteins on the erythrocyte surface.
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PMID:Protein antigens of Plasmodium knowlesi clones of different variant antigen phenotype. 671 54

Resealed erythrocyte ghosts were prepared under different experimental conditions and were tested in vitro for susceptibility to infection with the human malarial parasite, Plasmodium falciparum. Resealed ghosts, prepared by dialyzing erythrocytes in narrow membrane tubing against low ionic strength buffer that was supplemented with magnesium ATP, were as susceptible to parasite infection as were normal erythrocytes. There was a direct correlation between intraerythrocytic ATP content and susceptibility to parasite infection. Neither MgCl2 nor sodium ATP could be substituted for magnesium ATP in maintaining high intraerythrocytic ATP concentration. When resealed ghosts were loaded with antispectrin IgG, malaria merozoite invasion was inhibited. At an average intracellular antispectrin IgG concentration of 3.5 micrograms/10(8) cells, there was a 35% inhibition of parasite invasion. This inhibition was due to spectrin crosslinking within the resealed ghosts, since the monovalent, Fab' fragments of antispectrin IgG had no inhibitory effect on invasion. These results indicate that the cytoskeleton plays a role in the complex process of merozoite entry into the host erythrocyte.
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PMID:Involvement of spectrin and ATP in infection of resealed erythrocyte ghosts by the human malarial parasite, Plasmodium falciparum. 675 13


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