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At least 19 recordsLinked to original sources
PubMed1981

Monoclonal antibodies to stage-specific, species-specific, and cross-reactive antigens of the rodent malarial parasite, Plasmodium yoelii.

Eighteen hybridoma cell lines were used to study species-specific, stage-specific, and serological cross-reactive antigens of the rodent malarial parasite, Plasmodium yoelii. Specificity and location of plasmodial antigens were determined by indirect fluorescent-antibody analysis. Results showed that a minimum of 12 distinct plasmodial antigens could be distinguished by the 18 hybridomas. Antigens were found on the surface or within the cytoplasm of the parasite, but not on the surface of erythrocytes from infected animals. The majority (11 of 12) of antigens were present in all erythrocytic stages of the parasite, but one was stage-specific for merozoites. Additional studies showed that 6 of 18 of the monoclonal antibodies identified species-specific antigens, 2 of 18 recognized antigens confined to related rodent malarial parasites (Plasmodium berghei, Plasmodium vinckei, and Plasmodium chabaudi), whereas 8 of 18 detected cross-reactive antigens common to rodent, primate (Plasmodium knowlesi, Plasmodium falciparum), and avian (Plasmodium gallinaceum) malarias.

Animals↗
PubMed1980

The liver specific protein: evidence for species-specific and non-species-specific determinants.

Liver specific protein (LSP) is known to be a macrolipoprotein of complete organ-specificity but without complete species-specificity. This membrane antigen is believed to play an important role in the pathogenesis of human and experimental chronic active hepatitis (CAH). In the present study, we investigated the species-crossreactivity of LSP by crossed immunoelectrophoresis, tandem crossed immunoelectrophoresis and fused rocket immunoelectrophoresis. With a sheep anti human LSP serum, two determinants of human LSP could be detected--one was found to be species-specific, the other crossreacted with rabbit, rat, swine and mouse LSP; no reaction was found with bovine and sheep LSP. A rabbit anti human LSP serum, after short term immunization, reacted only with a species-specific determinant of human LSP, no species-crossreactivity was observed. In contrast, rabbits with experimentally induced CAH, after longterm immunization with human LSP, had developed an autoantibody to rabbit LSP in addition to antibodies to the species-specific determinant of human LSP. Antibodies to the liver membrane antigen (LM-Ag) could not be detected. In conclusion human LSP contains a species-specific and a non-species-specific determinant. CAH in rabbits is induced by the loss of tolerance to the non-species-specific determinant.

Animals↗
PubMed1992

Monoclonal antibodies define genus-specific, species-specific, and cross-reactive epitopes of the chlamydial 60-kilodalton heat shock protein (hsp60): specific immunodetection and purification of chlamydial hsp60.

Ocular and urogenital tract infections with Chlamydia trachomatis can progress to chronic inflammatory diseases that produce blindness and tubal infertility. The pathophysiology of these chronic disease conditions is thought to be immunologically mediated, and the chlamydial 60-kDa heat shock protein (hsp60) has been implicated as a major target antigen that stimulates the immunopathological response. The lack of chlamydial hsp60 antibodies and purified hsp60 has severely restricted studies to define more thoroughly the role of this protein in the immunopathogenesis of chlamydial disease. We produced a panel of antichlamydial hsp60 monoclonal antibodies (MAbs) and defined their specificities by immunoblotting against lysates of C. trachomatis, C. psittaci, and six other genera of bacteria. Three patterns of anti-hsp60 immunoreactivity were observed: chlamydial species specific, chlamydial genus specific, and cross-reactive. The epitopes recognized by these MAbs were localized within the primary amino acid sequence of hsp60 by immunoblotting against recombinant amino-terminal truncated hsp60 fusion polypeptides and then precisely mapped by use of overlapping synthetic peptides. The majority of the MAbs mapped to either the amino or the carboxyl termini of hsp60. Epitopes defining all three MAb reactivities mapped within amino-terminal residues 6 to 16. Genus-specific hsp60 MAbs mapped to epitopes located within this region and to residues 17 to 28 and 177 to 189. Antichlamydial hsp60 MAbs stained inclusions as effectively as MAbs specific for the major outer membrane protein. Homogeneous preparations of full-length recombinant chlamydial hsp60 and amino-terminal truncated recombinant hsp60 polypeptides were obtained by immunoabsorption chromatography with an hsp60 MAb reactive to the carboxyl terminus of the protein. Thus, the antichlamydial MAbs described here should be extremely useful for the specific immunodetection of hsp60 in tissues from individuals having different disease manifestations and for the purification of hsp60 or truncated hsp60 polypeptides for use in serologic and lymphocyte proliferation assays. The availability of these MAbs will facilitate studies to define more precisely the role of hsp60 in the immunopathogenesis of chlamydial disease.

Amino Acid Sequence↗
PubMed1986

Tissue-specific and species-specific distribution of -SH groups in cytochrome c oxidase subunits.

Cytochrome c oxidase was isolated from pig, bovine, rat and human tissues including liver, heart, diaphragm and kidney. The native and the sodium-dodecyl-sulfate (SDS)-dissociated enzymes were labelled under optimal conditions with N-ethyl-[2,3-14C]maleimide before and after reduction with dithiothreitol, separated into 13 subunits by SDS gel electrophoresis and the radioactive bands were visualized by fluorography. In some cases the radioactive bands were cut out and counted. All isozymes were labelled in subunits I, III, Va and VIIb, and in subunit II after reduction. Labelling of subunit Vb was equivocal, and in no case were subunits IV and VIc labelled. All other subunits were labelled tissue-specifically and/or species-specifically. No differences were found between labelling of the native and SDS-dissociated enzyme. By relating the molar amount of bound N-ethylmaleimide to the known amount of cysteines in subunits of bovine heart cytochrome c oxidase, the percentage of -SH group reactivity was calculated. Only the cysteine of subunit Va was found to be 100% reactive. The distinct and different reactivity of subunit VIIb as compared to subunits VIIa and VIIc clearly establishes this polypeptide as an independent subunit of mammalian cytochrome c oxidase.

Animals↗
PubMed1982

Tissue-specific and species-specific monoclonal antibodies to avian red cell nuclear proteins.

In order to identify potential red cell-specific regulatory proteins and to define additional red cell-specific markers, we have isolated a series of hybridomas that produce monoclonal antibodies that react with nuclear preparations from avian red blood cells. Several antibodies have been well characterized for their tissue- and species-specific reactions by using solid-phase and protein-transfer radioimmunoassays as well as immunofluorescence. These antibodies should allow isolation and characterization of individual nuclear proteins that are tissue and species specific and may prove useful for the study of gene expression in the erythropoietic system. The majority of the well-characterized antibodies appear to have tissue-specific properties. However, three antibodies react with all tested chicken tissues; one of these reacts with multiple peptides in a pattern that varies qualitatively and quantitatively between the tissues. This may reflect a common protein domain or modification that is used in several different tissues for similar functions but is nevertheless present in an overall protein framework that is tissue specific. Because the major fraction of the hybridomas initially produced is tissue specific, we presume that the immune system selects for tissue-specific determinants. This property of the immune system may prove to be a useful general feature of this type of analysis.

Animals↗
PubMed1986

On the origin of species specificity of fibronectin. Immunological identification of a species-specific domain of human fibronectin.

We have investigated whether species-specific epitopes of human fibronectin are localized at a specific domain of fibronectin using rabbit polyclonal antibodies. Tryptic fragments of human fibronectin were tested for reactivity with anti-human fibronectin antibody, which had been previously absorbed with other animal fibronectin to establish species specificity. Human-specific epitopes were found to be present on 75,000, 65,000, and 42,000 dalton fragments. The 42,000-dalton fragment shares almost all the epitopes with the 75,000 and 65,000 dalton fragments. It does not promote BHK cell spreading, whereas the 75,000 and 65,000 dalton fragments do. The amino acid sequence from the amino terminus of the 42,000-dalton fragment is Asp/Gly-Gln/Val-?-Ile-Val-, which is almost identical to the sequence Asp-Gln-Cys-Ile-Val- located in the carboxyl terminal 1/3 of the collagen-binding domain of human fibronectin (Kornblihtt et al. (1985) EMBO J. 4, 1755-1759). These results suggest that human fibronectin bears human-specific epitopes mainly on the amino-terminal half of domain 4 (Hayashi & Yamada (1983) J. Biol. Chem. 258, 3332-3340) located between the collagen and cell binding domains almost at the center of the fibronectin polypeptide. The domain specific for human fibronectin may be a general species-specific domain of animal fibronectins.

Amino Acid Sequence↗
PubMed2002

Application of proteomics for fast identification of species-specific peptides from marine species.

In this work, a novel approach based on proteomics is applied for the analysis of the three European marine mussel species: Mytilus edulis (ME), Mytilus galloprovincialis (MG) and Mytilus trossulus (MT), which are of interest in biotechnology and food industry. The proteomes of these species are poorly described in databases, are difficult to diagnose, and have a controversial taxonomy, To characterise species-specific peptides, we compared 51 matrix-assisted laser desorption/ioization-time of flight peptide mass maps generated from 6 random selected prominent spots derived from the two-dimensional electrophoresis analysis of foot protein extracts from several individuals. Minor species-specific differences in the peptide maps were detected in only one of the spots, corresponding to tropomyosin. Two peptides were unique to ME and MG individuals, whereas another peptide was present only in MT individuals. The sequence of these peptides was characterised by, nanoelectrospray ionization-ion trap (nanoESI-IT) tandem mass spectrometry (MS/MS) analysis followed by database searching and de novo sequence interpretation. We detected a single T to D amino acid substitution in MT tropomyosin. Unambiguous and highly-specific species identification was then demonstrated by analysing peptide extracts from tropomyosin spots by micro high-performande liquid chromatography (microHPL) ESI-IT mass spectrometry using the selected ion monitoring configuration, focused on these peptides, in continuous MS/MS operation. Our results suggest that proteomics may be successfully applied for the identification of species whose proteome is not present in databases.

Amino Acid Sequence↗
PubMed1986

Stage-specific and species-specific antigens of Plasmodium vivax and Plasmodium ovale defined by monoclonal antibodies.

Monoclonal antibodies (MAbs) were produced against the asexual blood stages of Plasmodium vivax and Plasmodium ovale and used to define antigens of plasmodial parasites in an indirect fluorescent antibody assay. The anti-P. vivax MAbs produced two distinct patterns in the indirect fluorescent antibody assay. Four patterns were found with the anti-P. ovale MAbs. Species-specific epitopes were defined for P. vivax and P. ovale; epitopes shared among all four species of human malaria parasites were also defined. Some of the anti-P. vivax MAbs reacted only with mature stages, and others reacted with all asexual stages. No asexual blood-stage specificity could be found with the anti-P. ovale antibodies. Five of the anti-P. vivax MAbs and three of the anti-P. ovale MAbs also reacted with sporozoites.

Animals↗
PubMed2000

Species-specific variation in glycosylation of IgG: evidence for the species-specific sialylation and branch-specific galactosylation and importance for engineering recombinant glycoprotein therapeutics.

Immunoglobulins (IgG) are soluble serum glycoproteins in which the oligosaccharides play significant roles in the bioactivity and pharmacokinetics. Recombinant immuno-globulins (rIgG) produced in different host cells by recombinant DNA technology are becoming major therapeutic agents to treat life threatening diseases such as cancer. Since glycosylation is cell type specific, rIgGs produced in different host cells contain different patterns of oligosaccharides which could affect the biological functions. In order to determine the extent of this variation N-linked oligosaccharide structures present in the IgGs of different animal species were characterized. IgGs of human, rhesus, dog, cow, guinea pig, sheep, goat, horse, rat, mouse, rabbit, cat, and chicken were treated with peptide-N-glycosidase-F (PNGase F) and the oligosaccharides analyzed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) for neutral and acidic oligosaccharides, in positive and negative ion modes, respectively. The data show that for neutral oligosaccharides, the proportions of terminal Gal, core Fuc and/or bisecting GlcNAc containing oligosaccharides vary from species to species; for sialylated oligosaccharides in the negative mode MALDI-TOF-MS show that human and chicken IgG contain oligosaccharides with N-acetylneuraminic acid (NANA), whereas rhesus, cow, sheep, goat, horse, and mouse IgGs contain oligosaccharides with N-glycolylneuraminic acid (NGNA). In contrast, IgGs from dog, guinea pig, rat, and rabbit contain both NANA and NGNA. Further, the PNGase F released oligosaccharides were derivatized with 9-aminopyrene 1,4,6-trisulfonic acid (APTS) and analyzed by capillary electrophoresis with laser induced fluorescence detection (CE-LIF). The CE-LIF results indicate that the proportion of the two isomers of monogalactosylated, biantennary, complex oligosaccharides vary significantly, suggesting that the branch specificity of beta1, 4-galactosyltransferase might be different in different species. These results show that the glycosylation of IgGs is species-specific, and reveal the necessity for appropriate cell line selection to express rIgGs for human therapy. The results of this study are useful for people working in the transgenic area.

Amidohydrolases↗
PubMed1988

Social specificity: interaction with own species is necessary to foster species-specific maternal preference in ducklings.

Previous studies have shown that if domestic mallard ducklings are allowed social interaction with broodmates after their initial exposure to a stuffed mallard (Anas platyrhynchos) hen, they later show a visual preference for the familiar mallard over an unfamiliar redhead (Aythya americana) hen. Birds kept in social isolation do not make this difficult discrimination. In the present study, we examined whether this social enhancement of imprintability to a natural maternal model is merely the result of social stimulation in its most general sense, or if its effects are specific to social interaction for 30 min (training). This experience resulted in visual preference for the familiar mallard hen over the unfamiliar redhead hen in simultaneous choices tests at 48 hr and 72 hr after hatching only if the birds were allowed social experience with a group of same-age undomesticated mallard hatchings. No visual preference for the familiar mallard hen was found if the ducklings were permitted social experience with a group of same-age chick (Gallus domesticus) hatchlings or muscovy (Cairina moschata) ducklings. Thus, it appears that for ducklings to show a visually imprinted preference for a natural maternal model, they must be allowed social interaction with broodmates of their own species. Social rearing with other precocial bird hatchlings, even other ducklings, is without apparent effect. These results provide further evidence of the importance of nonobvious experimental factors in the development of species-typical behavior. They also suggest that in the evolution of the species-specific learning underlying early species identification, natural selection has operated on the entire (organism-environment) developmental manifold and not merely on genetic, organic, or organismic aspects of that system.

Animals↗
PubMed1996

Characterization of species-specifically amplified SINEs in three salmonid species--chum salmon, pink salmon, and kokanee: the local environment of the genome may be important for the generation of a dominant source gene at a newly retroposed locus.

Short interspersed repetitive elements (SINEs), known as the HpaI family, are present in the genomes of all salmonid species (Kido et al., Proc. Natl. Acad. Sci. USA 1991, 88: 2326-2330). Recently, we showed that the retropositional efficiency of the SINE family in the lineage of chum salmon is extraordinarily high in comparison with that in other salmonid lineages. (Takasaki et al., Proc. Natl. Acad. Sci. USA 1994, 91: 10153-10157). To investigate the reason for this high efficiency, we searched for members of the HpaI SINE family that have been amplified species-specifically in pink salmon. Since the efficiency of the species-specific amplification in pink salmon is not high and since other members of the same subfamily of SINEs were also amplified species-specifically in pink salmon, the actual sequence of this subfamily might not be the cause of the high retropositional efficiency of SINEs in chum salmon. Rather, it appears that a highly dominant source gene for the subfamily may have been newly created by retroposition, and some aspect of the local environment around the site of retroposition may have been responsible for the creation of this dominant source gene in chum salmon. Furthermore, a total of 11 sequences of HpaI SINEs that have been amplified species-specifically in three salmon lineages was compiled and characterized. Judging from the distribution of members of the same-sequence subfamily of SINEs in different lineages and from the distribution of the different-sequence subfamilies in the same lineage, we have concluded that multiple dispersed loci are responsible for the amplification of SINEs. We also discuss the additional possibility of horizontal transmission of SINEs between species. The availability of the sets of primers used for the detection of the species-specific amplifications of the SINEs provides a convenient and reliable method for identification of these salmonid species.

Animals↗
PubMed1982

Tissue-specificity overrides species-specificity in cytoplasmic cytochrome c oxidase polypeptides.

With a high-resolving dodecyl sulfate electrophoretic system rat liver cytochrome c oxidase was separated into 13 different polypeptides. An antiserum against rat liver holocytochrome c oxidase immunoreacted with all 13 polypeptides, as demonstrated by immunofluorescence after transfer of the separated Coomassie blue-stained bands on nitrocellulose and coupling with FITC-protein A ("western blot"). Polypeptide-specific antisera reacted only with their corresponding polypeptides indicating that the various protein bands are represented by individual polypeptides. From total proteins of rat liver, kidney, heart, spleen and skeletal muscle mitochondria, only the cytochrome c oxidase polypeptides showed immunofluorescence with an antiserum against the rat liver holoenzyme. In contrast to the polypeptide from liver, polypeptide VIa from heart and skeletal muscle showed little or no reactivity, indicating a tissue-specificity of this polypeptide. Mitochondrial proteins from pig, bovine and blackbird heart were incubated with an antiserum against the rat liver holoenzyme. Immunoreaction was found with most cytochrome c oxidase polypeptides but not with polypeptide VIa. This result demonstrates less immunological relationship between tissue-specific polypeptides (VIa, VIIa and VIII) of the same species than between tissue-unspecific polypeptides of different species.

Animals↗