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PubMed1995

A species-specific nucleotide sequence of Mycobacterium tuberculosis encodes a protein that exhibits hemolytic activity when expressed in Escherichia coli.

Species-specific proteins may be implicated in the unique pathogenic mechanisms characteristic of Mycobacterium tuberculosis. In previous studies, a 3.0-kb species-specific DNA fragment of M. tuberculosis was identified (C. A. Parra, L. P. Londoño, P. del Portillo, and M. E. Patarroyo, Immun. 59:3411-3417, 1991). The nucleotide sequence of this 3.0-kb fragment has been obtained. This sequence was shown to contain two open reading frames (ORFs) whose putative gene products share 68.9% identity between each other. The major ORF shows 57.8% similarity with PLC-N and 53.2% similarity with PLC-H, two phospholipase C enzymes from Pseudomonas aeruginosa. The major ORF was amplified by PCR and cloned into the pGEX-5T expression vector. Cell extracts of Escherichia coli overexpressing this glutathione S-transferase fusion protein were shown to produce beta-hemolysis suggestive of phospholipase activity. Since phospholipase C enzymes have been reported as virulence factors of P. aeruginosa and also of the intracellular pathogen Listeria monocytogenes, it is possible that the proteins identified in this study could also play a role in sustaining tuberculosis infection in humans.

Amino Acid Sequence↗
PubMed2006

Lessons from comparative analysis of species-specific imprinted genes.

Genomic imprinting is generally believed to be conserved in all mammals except for egg-laying monotremes, suggesting that it is closely related to placental and fetal growth. As expected, the imprinting status of most imprinted genes is conserved between mouse and human, and some are imprinted even in marsupials. On the other hand, a small number of genes were reported to exhibit species-specific imprinting that is not necessarily accounted for by either the placenta or conflict hypotheses. Since mouse and human represent a single, phylogenetically restricted clade in the mammalian class, a much broader comparison including mammals diverged earlier than rodents is necessary to fully understand the species-specificity and variation in evolution of genomic imprinting. Indeed, comparative analysis of a species-specific imprinted gene Impact using a broader range of mammals led us to propose an alternative dosage control hypothesis for the evolution of genomic imprinting.

Animals↗
PubMed1993

Identification of species-specific, non-cross-reactive proteins of Borrelia burgdorferi.

The low specificity of diagnostic tests for Lyme disease is due to the fact that Borrelia burgdorferi possesses many antigenic proteins that are cross-reactive with other spirochetes and bacteria. The low sensitivity is a result of high (> or = 1:100) dilutions used for patient sera during testing to eliminate non-specific cross-reactivity. The present study was conducted to identify species-specific non-cross-reactive protein(s) of B. burgdorferi that might be used as antigen(s) in serologic tests. Whole-cell sonicates of B. burgdorferi were tested against pooled sera from patients with symptoms, signs, and serologic features diagnostic of Lyme disease (LD), rheumatoid arthritis, infectious mononucleosis, systemic lupus erythematosus, Rocky Mountain spotted fever, secondary syphilis, and from healthy individuals. Different LD pools were also tested against whole-cell sonicates of Treponema pallidum, Treponema phagedenis, Leptospira interrogans, and Escherichia coli. Comparison among patterns obtained by each serum pool revealed that IgM antibodies to species-specific 39-, 23-, and 22-kD proteins and IgG antibodies to 34- and 31-kD proteins were present only in the patients with LD and absent from patients with rheumatoid arthritis, infectious mononucleosis, systemic lupus erythematosus, Rocky Mountain spotted fever, secondary syphilis, and healthy individuals pools. These results suggest that 39-, 23-, and 22-kD proteins may be used in an IgM immunoassay for diagnosis of LD.

Antibodies, Anti-Idiotypic↗
PubMed2002

Species-specific protein sequence and fold optimizations.

BACKGROUND: An organism's ability to adapt to its particular environmental niche is of fundamental importance to its survival and proliferation. In the largest study of its kind, we sought to identify and exploit the amino-acid signatures that make species-specific protein adaptation possible across 100 complete genomes. RESULTS: Environmental niche was determined to be a significant factor in variability from correspondence analysis using the amino acid composition of over 360,000 predicted open reading frames (ORFs) from 17 archaea, 76 bacteria and 7 eukaryote complete genomes. Additionally, we found clusters of phylogenetically unrelated archaea and bacteria that share similar environments by amino acid composition clustering. Composition analyses of conservative, domain-based homology modeling suggested an enrichment of small hydrophobic residues Ala, Gly, Val and charged residues Asp, Glu, His and Arg across all genomes. However, larger aromatic residues Phe, Trp and Tyr are reduced in folds, and these results were not affected by low complexity biases. We derived two simple log-odds scoring functions from ORFs (CG) and folds (CF) for each of the complete genomes. CF achieved an average cross-validation success rate of 85 +/- 8% whereas the CG detected 73 +/- 9% species-specific sequences when competing against all other non-redundant CG. Continuously updated results are available at http://genome.mshri.on.ca. CONCLUSION: Our analysis of amino acid compositions from the complete genomes provides stronger evidence for species-specific and environmental residue preferences in genomic sequences as well as in folds. Scoring functions derived from this work will be useful in future protein engineering experiments and possibly in identifying horizontal transfer events.

Adaptation, Physiological↗
PubMed1986

Species specificity of human and murine tumor necrosis factor. A comparative study of tumor necrosis factor receptors.

Recombinant murine and human tumor necrosis factor (mTNF and hTNF, respectively) were radioiodinated to high specific activity using a solid-phase lactoperoxidase method. A single class of high affinity receptors for 125I-TNF was identified on TNF-sensitive murine L cells and human HeLa S2 cells. Competitive radioligand binding assays were used to study the species specificity of TNF preparations. Unlabeled hTNF competed 30-fold less effectively than mTNF for binding to L cell receptors, whereas mTNF competed to approximately the same extent as hTNF for binding to HeLa cell receptors. A similar species specificity was observed in cytotoxicity assays; hTNF was more cytotoxic for HeLa cells than mTNF. Conversely, mTNF was more growth inhibitory and cytotoxic for L cells than hTNF. mTNF. and hTNF.receptor complexes were compared by gel filtration chromatography and polyacrylamide gel electrophoresis before and after cross-linking with bis[2-(succinimidooxycarbonyloxy)ethyl]sulfone (BSOCOES). These complexes eluted in gel filtration at a position corresponding to a globular protein of 350,000 Mr. Gel autoradiographs of the fractions containing cross-linked complexes showed bands of 95,000 and 75,000 Mr as well as small amounts of higher Mr bands. mTNF and hTNF treated with BSOCOES formed cross-linked dimers and trimers. Therefore, we were unable to determine whether the 95,000 and 75,000 Mr bands represented two distinct subunits of receptors or one subunit to which either a dimer or a monomer of TNF was cross-linked. These results demonstrate species specificity in the TNF-receptor interaction. In addition, the affinity labeling studies in two species give an identical pattern for the TNF X receptor complexes, suggesting that the receptors have similar subunit composition.

Animals↗
PubMed1998

From absolute to exquisite specificity. Reflections on the fuzzy nature of species, specificity and antigenic sites.

The term specificity is derived from the word species and shares with it an inherent fuzziness based on the absence of sharp boundaries between closely related entities. Antibody specificity is a ternary relational property which refers to the antibody's capacity to discriminate between two or more epitopes. There are no sharp boundaries between the individual overlapping epitopes that constitute an antigenic site and there is also no clear-cut minimum difference in binding affinity or in atomic positions at the epitope-paratope interface that can serve as a yardstick for deciding that two epitopes or two paratopes are the same or not. Immunology shares with the whole of empirical science the need to handle fuzzy sets and concepts and this poses no threat to the unabated further development of immunochemical analysis.

Antibody Specificity↗
PubMed1996

Detection of species specific epitopes of mouse and hamster prion proteins (PrPs) by anti-peptide antibodies.

Antisera to four synthetic peptides containing the substitutions between mouse and hamster prion proteins (PrPs) were produced in rabbits. The synthetic peptides used represent two mouse (Mo-I: residues 100-115 and Mo-V: residues 199-208) and two hamster PrP subregion sequences (Ha-I: 101-116 and Ha-V: 200-209). All antisera reacted strongly with homologous peptides but either not at all or poorly with heterologous peptides in enzymelinked immunosorbent assay (ELISA). Antisera to Mo-I and Mo-V recognized mouse PrPSc but not hamster PrpSc in western blot analysis (WB) and ELISA. Antisera to Ha-I contain antibodies specific to hamster PrPSc. The results indicate that these regions of PrPSc constitute species-specific epitopes. In contrast to these antisera, the antiserum to Ha-V recognized neither hamster nor mouse PrPSc. In this study, we identified mouse subregion-V as a species-specific epitope.

Amino Acid Sequence↗
PubMed1988

Production of murine monoclonal antibodies against a liver-specific, species cross-reactive antigen in the liver-specific lipoprotein (LSP) preparation.

Previous attempts in several laboratories have failed to produce murine monoclonal antibodies (MAbs) against liver-specific, species-cross-reactive, cell surface-expressed antigens in the normal liver preparation known as liver-specific membrane lipoprotein (LSP). In the present study, BALB/c mice were pretreated with a single dose of cyclophosphamide (20 mg/kg), hyperimmunized with human LSP and hybridomas produced by fusion of spleen cells from these mice with murine myeloma (P3-NS1-Ag4-1) cells. To bias selection in favour of MAbs reacting with species cross-reactive epitopes, hybridoma supernatants were screened by ELISA against rabbit LSP. From 70 stable hybridomas, four MAbs were obtained that react with rabbit LSP. One is an IgM antibody and the other three are of IgG2a class. All four react with the hepatic asialo-glycoprotein receptor (HL), a liver-specific, species-cross-reactive component that is normally expressed on the surfaces of hepatocytes. Using a rapid screening technique (an 'additive' ELISA), preliminary evidence was obtained indicating that these four MAbs between them recognise three different epitopes on the HL molecule. The results suggest that this is a viable approach for the production of MAbs against autoantigens to which autoreactivity may normally be suppressed.

Animals↗
PubMed2004

Sensitive and specific detection of Xanthomonas campestris pv campestris by PCR using species-specific primers based on hrpF gene sequences.

A sensitive and specific assay was developed to detect bacterial black rot of crucifers caused by Xanthomonas campestris pv. campestris (X. c. pv. campestris), in cabbage seed and plant. Primers XCF and XCR from hrpF homologous to nolX, host recognition protein, were used to amplify a 525 bp DNA fragment. PCR technique was applied to detect the pathogen in naturally infected seed and plant of cabbage. The PCR product was only produced from X. c. pv. campestris among 40 isolates of Xanthomonas strains, Escherichia coli (O157:H7), Pectobacterium carotovorum subsp. carotovorum, and other reference bacteria.

Bacterial Proteins↗
PubMed1993

EIA with species-specific monoclonal antibodies: a novel seroepidemiologic tool for determination of the etiologic agent of spotted fever rickettsiosis.

All currently available assays for antibodies to the etiologic agents of spotted fever group rickettsioses detect reactivity with antigens of lipopolysaccharides and the major cell wall proteins, which contain epitopes that are shared among many spotted fever group rickettsiae. The hypothesis of this study was that a monoclonal antibody to a species-specific epitope of Rickettsia rickettsii would be blocked from binding to the rickettsial surface if the rickettsiae were incubated previously with serum containing species-specific antibodies to the epitope. In an EIA, binding of monoclonal antibody 5C10-F3 to R. rickettsii was blocked by convalescent sera from patients with Rocky Mountain spotted fever but not from those with Mediterranean spotted fever, endemic typhus, or Q fever or normal subjects. This assay should be useful in determining the origin of the high seroprevalence of spotted fever rickettsial antibodies in certain geographic regions and establishing a species-specific diagnosis in patients with undetermined rickettsial exposure.

Antibodies, Bacterial↗
PubMed2003

Species-specific effects of single sensillum ablation on mating position in Drosophila.

Dipteran insects show a wide range of species-specific mating positions. Interspecific transitions from one position to another may reflect sexual or natural selection, or be pleiotropic consequences of other genetic changes. Like many cyclorrhaphan flies, Drosophila species mate with the male on the back of the female, positioned centrally. Mechanosensory sensilla on the male genitalia of three species of the melanogaster species sub-group of Drosophila have species-specific effects on mating position and on courtship success: ablation of a single pair of bristles on the genital claspers of D. melanogaster males halved homotypic mating success, and unilateral ablation produced a contralateral asymmetry in the male's mating posture. Ablation of mechanoreceptors on the male genital lateral plate affected mating posture less radically and had no effect on mating frequency. Surprisingly, ablation of sensilla on the claspers of D. simulans and D. sechellia males showed no effect on homotypic mating. A similar result was found for D. melanogaster x D. simulans hybrid males. The existence of major differences in the sensory bases of mating position and copulation success in closely related species shows how differing mating positions may have evolved and underlines the need for detailed functional studies in studying the evolution of insect genitalia: homologous structures may serve different functions in different species.

Analysis of Variance↗
PubMed1992

Functional characterization of a hybrid human-mouse interferon gamma receptor: evidence for species-specific interaction of the extracellular receptor domain with a putative signal transducer.

The human interferon gamma (IFN-gamma) receptor expressed in mouse cells displays binding properties indistinguishable from those of the resident receptor on human cells. Still, mouse cells expressing the human IFN-gamma receptor remain insensitive to human IFN-gamma. It is widely accepted that at least one species-specific cofactor encoded within human chromosome 21 is required for signal transduction. To define structural domains of the human IFN-gamma receptor responsible for this species-specific interaction, a hybrid between the human and the murine receptor was constructed and expressed in mouse L929 cells or in mouse L cell-derived SCC16-5 cells, which contain human chromosome 21. This hybrid receptor, which consisted of the extracellular domain of the human IFN-gamma receptor and the transmembrane and cytoplasmic domains of the murine IFN-gamma receptor, was found to bind human IFN-gamma with high affinity. However, only SCC16-5 cells expressing the human/mouse hybrid receptor were responsive to human IFN-gamma as revealed by enhanced expression of major histocompatibility complex class I antigens, induction of the transcription factor IRF-1, and induction of a partial antiviral state. These findings strongly suggest that IFN-gamma-mediated signal transduction requires a species-specific interaction of the extracellular portion of the known ligand-binding IFN-gamma receptor chain with an additional, presumably membrane-anchored receptor subunit.

Animals↗
PubMed2001

Episodic evolution of growth hormone in primates and emergence of the species specificity of human growth hormone receptor.

Growth hormone (GH) evolution is very conservative among mammals, except for primates and ruminant artiodactyls. In fact, most known mammalian GH sequences differ from the inferred ancestral mammalian sequence by only a few amino acids. In contrast, the human GH sequence differs from the inferred ancestral sequence by 59 amino acids. However, it is not known when this rapid evolution of GH occurred during primate evolution or whether it was due to positive selection. Also, human growth hormone receptor (GHR) displays species specificity; i.e., it can interact only with human (or rhesus monkey) GH, not with nonprimate GHS: The species specificity of human GHR is largely due to the Leu-->Arg change at position 43, and it has been hypothesized that this change must have been preceded by the His-->Asp change at position 171 of GH. Is this hypothesis true? And when did these changes occur? To address the above issues, we sequenced GH and GHR genes in prosimians and simians. Our data supported the above hypothesis and revealed that the species specificity of human GHR actually emerged in the common ancestor of Old World primates, but the transitional phase still persists in New World monkeys. Our data showed that the rapid evolution of primate GH occurred during a relatively short period (in the common ancestor of higher primates) and that the rate of change was especially high at functionally important sites, suggesting positive selection. However, the nonsynonymous rate/synonymous rate ratio at these sites was <1, so relaxation of purifying selection might have played a role in the rapid evolution of the GH gene in simians, possibly as a result of multiple gene duplications. Similar to GH, GHR displayed an accelerated rate of evolution in primates. Our data revealed proportionally more amino acid replacements at the functionally important sites in both GH and GHR in simians but, surprisingly, showed few coincidental replacements of amino acids forming the same intermolecular contacts between the two proteins.

Amino Acids↗
PubMed1994

Species-specific expression of CYP4B1 in rabbit and human gastrointestinal tissues.

CYP4B1 is a P450 enzyme displaying tissue and species specific regulation. The rabbit CYP4B1 enzyme exhibits activity towards procarcinogenic aromatic amines. In the present study, CYP4B1 expression has been characterized in rabbit tissues using histological techniques, Northern blotting and Western blotting. Similar analyses were attempted using available human tissues. CYP4B1 mRNA and protein was demonstrated throughout the rabbit small intestine and colon. A unique 1.8 kb transcript, that is smaller than the transcript found in other tissues, was detected in rabbit stomach with a CYP4B1 specific RNA probe. No CYP4B1 protein was detected in this tissue. In rabbit liver, CYP4B1 was induced by phenobarbital primarily in zone 1 hepatocytes (periportal). In humans, CYP4B1 expression was demonstrated at low levels in human colon using in situ hybridization but not in liver or the small intestine. All rabbit gastrointestinal tissues other than stomach possess a high capacity for the activation of 2-aminofluorene compatible with CYP4B1 expression. In contrast, no activity was observed in human gastrointestinal microsomes. The present study therefore shows that CYP4B1 is an abundant P450 in the rabbit gastrointestinal tract and identifies species-specific differences in CYP4B1 expression and function.

Animals↗
PubMed2001

Species-specific differences in amino acid editing by class II prolyl-tRNA synthetase.

Aminoacyl-tRNA synthetases are a family of enzymes responsible for ensuring the accuracy of the genetic code by specifically attaching a particular amino acid to their cognate tRNA substrates. Through primary sequence alignments, prolyl-tRNA synthetases (ProRSs) have been divided into two phylogenetically divergent groups. We have been interested in understanding whether the unusual evolutionary pattern of ProRSs corresponds to functional differences as well. Previously, we showed that some features of tRNA recognition and aminoacylation are indeed group-specific. Here, we examine the species-specific differences in another enzymatic activity, namely amino acid editing. Proofreading or editing provides a mechanism by which incorrectly activated amino acids are hydrolyzed and thus prevented from misincorporation into proteins. "Prokaryotic-like" Escherichia coli ProRS has recently been shown to be capable of misactivating alanine and possesses both pretransfer and post-transfer hydrolytic editing activity against this noncognate amino acid. We now find that two ProRSs belonging to the "eukaryotic-like" group exhibit differences in their hydrolytic editing activity. Whereas ProRS from Methanococcus jannaschii is similar to E. coli in its ability to hydrolyze misactivated alanine via both pretransfer and post-transfer editing pathways, human ProRS lacks these activities. These results have implications for the selection or design of antibiotics that specifically target the editing active site of the prokaryotic-like group of ProRSs.

Alanine↗
PubMedDate not supplied

[The development of species-specific test systems for the rapid diagnosis of staphylococcal infections].

Highly purified teichoic acids (TA) were isolated from Staphylococcus aureus and S. epidermidis and characterized. The preparations of TA were highly species-specific. For the first time monospecific sera to S. aureus and S. epidermidis were obtained. From these monospecific sera immunoglobulins were isolated and used for the preparation of reagents for the passive hemagglutination (PHA) test and the enzyme immunoassay (EIA). The sensitivity of the PHA test and EIA was 15 micrograms/ml when S. aureus and S. epidermidis were used and 10(6)-10(7) cells/ml when whole microbial cells were used. The diagnostic preparations proved to be highly specific and did not react with other preparations isolated from S. aureus and S. epidermidis, as well as from bacteria belonging to other taxa. Experiments on rabbits, carried out with the use of newly developed test systems, demonstrated that staphylococci could be detected in the blood as early as 10 minutes after the intravenous infection of the animals and until day 12.

Animals↗
PubMedDate not supplied

Monoclonal antibodies species-specific to Mycoplasma gallisepticum and M. synoviae.

Two species-specific monoclonal antibodies (MAbs) were produced against Mycoplasma gallisepticum and M. synoviae. The MAb against M. synoviae recognizes an antigen of 90,000 molecular weight present in strain WVU 1853 and in two Brazilian field isolates. The MAb produced against M. gallisepticum recognizes a surface antigen in strains S6 and R and in three Brazilian field isolates of different molecular weights. The MAbs do not recognize antigens in M. gallinarum and M. iowae.

Animals↗
PubMed2004

Species-specific allozyme markers for Appalachian wood-feeding cockroaches (Dictyoptera: Cryptocercidae).

Members of the genus Cryptocercus are wood-feeding cockroaches that live in the temperate forests. Nine species are recognized in the genus worldwide: two in eastern Eurasia, two in China, and five in the United States. Within the United States, one species occurs in the Pacific Northwest and four occur in the Appalachian Mountains. Previous studies have revealed the presence of potential zones of overlap in distribution among the Appalachian species, raising the possibility of hybridization among them. Differences in mitochondrial DNA have previously been identified for the Appalachian species. However, to identify hybrid individuals one or more species-specific, codominant nuclear markers are required. Therefore, our objective was to undertake allozyme analysis of enzymatic loci to identify fixed, species-specific alleles for the four Appalachian species. We assayed a mean of 42 individuals each from 16 sites for allozyme variation for the four species. At 6 of the 33 loci examined, fixed alternate alleles were identified; a combination of 2 loci enabled the identification of all four species. To identify hybrids in the field, we examined 42 individuals each from 13 sites in which two or more of the above species occur in close proximity for presence of heterozygous individuals at one or more of the six fixed loci. No heterozygous individuals were found suggesting the lack of hybridization among the Appalachian species.

Alleles↗