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PubMedDate not supplied

[Species-specific detection of Proteus vulgaris and Proteus mirabilis by the polymerase chain reaction].

Sets of primers for the species-specific detection of P. mirabilis and P. vulgaris by the polymerase chain reaction (PCR) were developed. As targets for these primers beta-lactamase and 16S rRNA gene fragments were chosen on the basis of the multiple leveling of the sequences of the DNA of all known P. mirabilis and P. vulgaris isolates. For differential detection oligonucleotides were selected in such a way that primers, specific for P. vulgaris, contained the non-paired nucleotide for P. mirabilis isolate at the 3'-end, and all other nucleotides were complementary to the beta-lactamase gene fragment. Primers, specific for gene 16S rRNA of P. mirabilis, contained the non-paired nucleotide for P. vulgaris isolates at the 3'-end. Standard PCR was carried out for 6 P. mirabilis and P. vulgaris strains. The use of PCR species-specific primers to P. vulgaris DNA made it possible to amplify the DNA fragment of the expected length only for P. vulgaris isolates, while the result of PCR for P. mirabilis was negative. PCR with primers specific to P. mirabilis permitted the detection of amplicon sized 101 nucleotides pairs only for P. mirabilis strains. These primers were optimized so as to use them in the specific differentiation of closely related P. mirabilis and P. vulgaris species by multiplex PCR. Genus-specific primers permitted the detection of bacterial gyrB gene of the genus Proteus were developed also.

Bacteriological Techniques↗

PubMed1984

Monoclonal antibodies to rabbit and pig zonae pellucidae distinguish species-specific and shared antigenic determinants.

Monoclonal antibodies against rabbit or porcine zonae pellucidae (ZP) demonstrate species-specific and shared antigenic determinants. In addition, these antibodies are used to characterize the biochemical nature of these determinants. All of six monoclonal antibodies developed against porcine ZP react with porcine but not with rabbit ZP. Only one of seven monoclonal antibodies developed against rabbit ZP cross-reacts with porcine ZP. None of these antibodies recognized antigens associated with other tissues tested. High-resolution, two-dimensional polyacrylamide gel electrophoresis (2D-PAGE) followed by immunoblotting was used to demonstrate that the cross-reactive antibody recognizes an antigenic determinant which is associated with the major low molecular weight glycoprotein of both the pig and rabbit ZP. Since this antibody recognizes all charge species of this glycoprotein, it is apparent that the antigenic determinant recognized by this antibody involves protein. Further studies demonstrate that proteolytic digestion of ZP will destroy the antigenic determinant while glycosidic digestion of ZP has no effect on antibody binding. Although polyclonal antibodies to this glycoprotein inhibit sperm from binding to the zona pellucida, this monoclonal antibody does not affect sperm binding. None of the species-specific antibodies recognize ZP glycoproteins following 2D-PAGE. This is a property typical of antibodies directed against conformational antigenic determinants. The presence of common as well as unique zona antigenic determinants could explain why ZP proteins induce heteroantibodies which result in infertility while alloimmunization has no effect on fertility.

Animals↗

PubMed1996

Species-specific detection of Legionella using polymerase chain reaction and reverse dot-blotting.

Legionella pneumophila and some other Legionella species are capable of causing Legionnaire's disease, a potentially fatal pneumonia. The identification of legionellae by standard laboratory techniques such as culture is difficult and time consuming. In the present work, the DNA sequence of the 23S-5S spacer region was determined for 43 Legionella isolates, and the sequence information was used to develop a species-specific detection system using PCR and reverse dot-blotting which employs just one PCR amplicon to perform genus- and species-specific detection. L. pneumophila serogroups 1-16 as well as 21 non-pneumophila isolates could be identified and differentiated at the species level using this system.

Base Sequence↗

PubMed1999

Species-specific responses to metals in organically enriched river water, with emphasis on effects of humic acids.

Invertebrate communities in polluted rivers are often exposed to a wide variety of compounds. Due to complex interactions, 'pollution tolerant' species are not necessarily the most tolerant species to toxicants tested under standard laboratory conditions. It was hypothesized that the distribution of species in polluted rivers is not only dependent on the tolerance of species to toxicants, but also on species-specific capacities to modify or compensate for negative effects of toxicants. To test this hypothesis, species-specific responses to metals in organically enriched river water were studied under controlled conditions. The zebra mussel Dreissena polymorpha and the midge Chironomus riparius were exposed to metal-polluted water from the River Dommel. Additionally, the (interactive) effects of metals and humic acids (HA) on both species were evaluated. In spite of a lower tolerance of Chironomus riparius to metals in laboratory studies, the midge was the most tolerant of the two test species to metal-polluted site water. The results indicated that the sensitivities of the two test species determined in laboratory tests were inversely related to their sensitivities to polluted river water. In accordance with these results, midge larvae were protected from copper (Cu) toxicity by HA, while metal toxicity was not reduced (Cu) or even amplified (cadmium) by HA for the zebra mussel. Thus, the presence of (naturally occurring) HA in site water may partly account for discrepancies between responses of species to bioassays and toxicity tests. It is suggested that these differences in responses to metals in site water are strongly influenced by species-specific preferences for organic compounds (like HA). It is concluded that the response to organic compounds present in site water largely determines whether a species is classified as 'pollution tolerant' or 'pollution sensitive'.

Journal Article↗

PubMed1997

Detection of Plasmodium ovale malaria parasites by species-specific 18S rRNA gene amplification.

A polymerase chain reaction (PCR) assay was developed for the specific detection of Plasmodium ovale, one of the four malaria parasites that infect humans. On the basis of sequence variation of the Plasmodium 18S ribosomal RNA (rRNA) gene, oligonucleotide primers for PCR were designed to amplify various fragments of the P. ovale gene. Using a recombinant plasmid with the complete P. ovale 18S rRNA gene as target, 59 primer combinations were tested so that at least one of the pairs was species-specific while the other primer was either genus conserved or P. ovale species-specific. Three primer pairs yielding DNA fragments at stringent conditions were further tested against genomic DNA of four human malaria species. This approach yielded P. ovale species-specific primer pairs that may be useful for further field testing.

Animals↗

PubMed1983

Species-specific binding of purified pili (AF/R1) from the Escherichia coli RDEC-1 to rabbit intestinal mucosa.

Species-specific colonization of rabbit intestine by RDEC-1 Escherichia coli is an accepted animal model for bacterial mucosal adherence. To determine whether RDEC-1 pili are functional as adherence factors for this organism, we grew the organism under conditions that promoted pilus expression; we isolated the pili, documented their purity, and compared their mucosal adherence properties with those of whole organisms using an indirect immunofluorescence technique. Frozen sections of rabbit, rat, guinea pig, and human small intestine were incubated with either piliated or nonpiliated RDEC-1 organisms or purified RDEC-1 pili and observed for the distribution and intensity (0-4+) of fluorescence. Piliated RDEC-1 organisms fluoresced brightly (4+) and were distributed along the entire mucosal surface of the rabbit ileum. Only a few nonpiliated RDEC-1 attached to rabbit ileum, and they were randomly scattered across the entire section of tissue. Rabbit ileum overlain with pure RDEC-1 pili showed a specific, D-mannose resistant (2-3+) fluorescence on the mucosal surface from the crypts to the villus tips. No fluorescence was seen on the guinea pig, rat, or human mucosal surface overlain with RDEC-1 pili. Purified RDEC-1 pili adhere to the rabbit intestinal mucosa in a species-specific manner and with the same distribution as whole piliated organisms. The data suggest that RDEC-1 produce pili (distinct from type 1 pili) that determine the specificity of the mucosal adherence of RDEC-1 to rabbit ileum.

Adhesiveness↗

PubMed1992

Species specificity in the interaction of CD8 with the alpha 3 domain of MHC class I molecules.

The alpha 1 and alpha 2 domains of the class I MHC molecule constitute the putative binding site for processed peptides and the TCR, although the alpha 3 domain has been implicated as a binding site for the CD8 molecule. Species specificity in the binding of CD8 to the alpha 3 domain has been suggested as an explanation for the low xenogeneic T cell response to class I molecules, but results on this point have been conflicting and controversial. We have addressed this issue using CTL lines from HLA-A2.1 transgenic mice that specifically recognize and lyse A2.1-expressing cells infected with influenza A/PR/8 or pulsed with influenza matrix peptide M1(57-68). Species specificity was examined using transfectants that expressed hybrid molecules containing the alpha 1 and alpha 2 domains from HLA-A2.1 and the alpha 3 domain from a murine class I molecule. Lower levels of M1(57-68) peptide were required to sensitize L cell transfectants expressing a chimera that contained an H-2Dd alpha 3 domain than targets expressing the intact A2.1 molecule. However, at high doses of peptide, lysis of these two targets was similar. However, no reproducible difference in sensitization was observed using EL4 or Jurkat transfectants expressing A2.1 or A2.1 chimeric molecules that contained an H-2Kb alpha 3 domain. In all cases, however, lysis of peptide-pulsed A2.1 expressing targets was more sensitive to inhibition with anti-CD8 mAb than lysis of cells expressing these chimeric molecules. Thus, under suboptimal conditions such as low Ag density or in the presence of anti-CD8 mAb, these CTL preferentially recognize class I molecules with a murine alpha 3 domain. This suggests that there is some species specificity in the interaction of CD8 with the alpha 3 domain of the class I molecule. However, CTL recognition was inhibited by point mutations in the alpha 3 domain of HLA-A2.1 that have been shown to inhibit binding of human CD8 and recognition by human CTL, suggesting that murine CD8 interacts to some degree with human alpha 3 domains, and that similar alpha 3 domain residues may be important for murine and human CD8 binding. The relevance of these results to an understanding of low xenogeneic responses is discussed.

Animals↗

PubMed2004

A species-specific determinant on beta2-microglobulin required for Ly49A recognition of its MHC class I ligand.

The mouse inhibitory NK cell receptor Ly49A recognizes the mouse MHC class I molecule H-2D(k). The present study focuses on the species specificity of beta(2)-microglobulin (beta(2)m), an invariant component of MHC class I, in the interaction between Ly49A and H-2D(k). Transfection of the beta(2)m-defective mouse cell line R1E/TL8x.1 with human (h) beta(2)m induced cell-surface expression of H-2D(k), but failed to protect the cells from killing by Ly49A(+) NK cells. In contrast, the cells transfected with mouse (m) beta(2)m were protected from killing by Ly49A(+) NK cells. These data indicate that Ly49A distinguishes mbeta(2)m from hbeta(2)m when it recognizes the H-2D(k) complexes. To identify the species-specific determinant of beta(2)m required for Ly49A recognition of H-2D(k), we prepared a panel of mbeta(2)m mutants and tested the H-2D(k) that included each of the beta(2)m mutants for its capacity to engage Ly49A on NK cells. Ly49A failed to functionally recognize the H-2D(k) that included the mbeta(2)m with K3R and Q29G mutations. Moreover, Ly49A was able to recognize the H-2D(k) that included the hbeta(2)m with R3K and G29Q mutations. These data indicate that Lys3 and Gln29 consist of the central part of the species-specific determinant of beta(2)m required for Ly49A recognition of H-2D(k). The two residues are conserved in the mouse and the rat, in which NK cells use Ly49 family molecules as the receptors specific for MHC class I. These results suggest functional importance of beta(2)m in NK cell recognition of target cells.

Amino Acid Sequence↗

PubMed2003

Characterization of species-specific genes using a flexible, web-based querying system.

We describe a query-based web-accessible system (www.neurogadgets.com/bws.php) for facilitating comparative microbial genomics. A variety of query pages are available, each with numerous options, that allow a biologist to pose relevant questions of genomic data. We illustrate with a characterization of species-specific protein-coding genes (so-called "ORFans"), finding that they are on average smaller, faster evolving, and less G+C-rich, and that they encode proteins more basic in their predicted isoelectric point, compared with non-species-specific genes. Using a dual-threshold approach, we conclude that these are characteristics of true species-specific genes, rather than artifacts of mis-annotation.

Base Composition↗

PubMed1998

Predominant recognition of species-specific determinants of the GroES homologues from Mycobacterium leprae and M. tuberculosis.

The Mycobacterium leprae and M. tuberculosis 10,000 MW heat-shock protein homologues of GroES have previously been identified as major immunogens for human T cells. We used synthetic peptides to characterize the determinants recognized by murine T cells. The findings suggest that, despite 90% sequence identity between these two proteins, T cells recognize prominently the species-specific determinants localized within amino acid residues 21-40 and 49-72. Analysis of the molecular determinants of species-specificity for the M. leprae GroES sequence 25-40, using T-cell hybridomas and major histocompatibility complex (MHC)-binding assays, led to the identification of epitope cores and critical residues. Interestingly, closely overlapping epitope cores were found to be restricted by either H-2Ad (24-34) or H-2Ed (28-34). Furthermore, the site recognized by the M. leprae-specific monoclonal antibodies ML06 and ML10 was also localized in the overlapping sequences 25-31 and 25-29. In conclusion, we demonstrated that immunodominant species-specific T- and B-cell epitopes can be found in a mycobacterial heat-shock protein despite its highly conserved amino acid sequence. This finding suggests the feasibility of identifying a sufficient number of M. leprae-specific determinants for a composite T-cell immunodiagnostic reagent for tuberculoid leprosy.

Amino Acid Sequence↗

PubMed2006

Cross-reactive and species-specific immunoglobulin E epitopes of plant profilins: an experimental and structure-based analysis.

BACKGROUND: Profilins are cross-reactive plant allergens responsible for multiple pollen sensitization and pollen-associated food allergy. While it is assumed that profilins from different species are immunologically equivalent, some studies suggest partial or even lacking IgE cross-reactivity between certain profilins. OBJECTIVE: We aimed to obtain a semi-quantitative assessment of the contributions of conserved and species-specific epitopes to IgE binding of plant profilins. METHODS: We compared model structures of profilins from timothy, mugwort, celery and bell pepper with crystal structures of birch and latex profilins. We predicted potential conformational epitopes that consisted of contiguous patches of at least 20% surface-exposed residues. Celery and timothy profilins were purified from their natural sources, and profilins from birch, mugwort, bell pepper and latex were expressed in Escherichia coli. The structural integrity of all purified proteins was confirmed by circular dichroism spectroscopy. IgE ELISAs and ELISA inhibitions using sera from 22 profilin-sensitized allergic patients were carried out. RESULTS: Peptide backbone conformations of all six profilins were highly similar. Nine variable epitopes and two containing high proportions of conserved residues were predicted. IgE from all sera bound to all tested profilins and the amounts were highly correlated. However, IgE inhibition experiments revealed that up to 60% of total IgE binding was mediated by species-specific epitopes. The extent of cross-reactivity among profilins from timothy, birch, latex and celery was greater than cross-reactivity to mugwort and bell pepper profilins. This pattern was mirrored by sequence similarities among one of the predicted variable epitopes. Patients with IgE to cross-reactive epitopes displayed allergic reactions to a greater number of plant foods than patients having IgE directed to species-specific epitopes. CONCLUSION: The large extent of cross-reactivity among plant profilins justifies using a single profilin for diagnosis. However, the fine specificity of IgE directed to variable epitopes may influence the clinical manifestation of profilin sensitization.

Amino Acid Sequence↗

PubMed1995

Using evolutionary changes to achieve species-specific inhibition of enzyme action--studies with triosephosphate isomerase.

BACKGROUND: Many studies that attempt to design species-specific drugs focus on differences in the three-dimensional structures of homologous enzymes. The structures of homologous enzymes are generally well conserved especially at the active site, but the amino-acid sequences are often very different. We reasoned that if a non-conserved amino acid is fundamental to the function or stability of an enzyme from one particular species, one should be able to inhibit only the enzyme from that species by using an inhibitor targeted to that residue. We set out to test this hypothesis in a model system. RESULTS: We first identified a non-conserved amino acid (Cys14) whose integrity is important for catalysis in triosephosphate isomerase (TIM) from Trypanosoma brucei. The equivalent residues in rabbit and yeast TIM are Met and Leu, respectively. A Cys14Leu mutant of trypanosomal TIM had a tendency to aggregate, reduced stability and altered kinetics. To model the effects of a molecule targeted to Cys14, we used methyl methanethiosulfonate (MMTS) to derivatize Cys14 to a methyl sulfide. This treatment dramatically inhibited TIMs with a Cys residue at a position equivalent to Cys14, but not rabbit TIM (20% inhibition) or yeast TIM (negligible inhibition), which lack this residue. CONCLUSIONS: Cys14 of trypanosomal TIM is a non-conserved amino acid whose alteration leads to loss of enzyme structure and function. TIMs that have a cysteine residue at position 14 could be selectively inhibited by MMTS. This approach may offer an alternative route to species-specific enzyme inhibition.

Animals↗

PubMed2003

Role of X chromosomal song genes in the evolution of species-specific courtship songs in Drosophila virilis group species.

In the Drosophila virilis group the males of the virilis phylad species produce courtship song consisting of pulse trains with no pauses between successive sound pulses, whereas the males of the montana phylad species produce songs with clear pauses between the sound pulses. We obtained song data for F1 hybrids between D. virilis (representing the virilis phylad) or D. flavomontana (representing the montana phylad) females and the males of several species of the D. virilis group to study the interaction of X chromosomal and autosomal song genes affecting species differences in song. In crosses with D. virilis females, X chromosomal (or maternal) factors masked variation in pulse length despite variation in heterospecific autosomal song genes. To the contrary, in crosses with D. flavomontana females, X chromosomal genes largely determined the pause length and interacted with autosomal genes to determine the pulse length. In the montana phylad species, pulse length showed dominance toward shorter pulses and pause length toward longer pauses. The first-mentioned trait also indicated the epistatic effects of X chromosomal and autosomal components.

Analysis of Variance↗

PubMed1993

Genus-specific polymerase chain reaction for the mycobacterial dnaJ gene and species-specific oligonucleotide probes.

Identification of tuberculous and nontuberculous mycobacteria by biochemical methods is a long-term process that takes up to 8 weeks for completion and requires expertise to interpret the results. In order to detect and differentiate the major pathogenic mycobacterial species, we developed genus-specific primers that amplify the dnaJ gene from the broad spectrum of mycobacterial species and determined the nucleotide sequences within the dnaJ genes from 19 mycobacterial species (Mycobacterium tuberculosis, M. bovis, M. bovis BCG, M. africanum, M. microti, M. kansasii, M. marinum, M. gastri, M. simiae, M. scrofulaceum, M. szulgai, M. gordonae, M. avium, M. intracellulare, M. xenopi, M. fortuitum, M. chelonei, M. haemophilum, and M. paratuberculosis). On the basis of the dnaJ gene sequences, we developed dot blot hybridization analysis with species-specific oligonucleotide probes for the M. tuberculosis complex. M. avium, M. intracellulare, and M. kansaii, allowing a rapid identification of these species following polymerase chain reaction for the dnaJ gene. We conclude that polymerase chain reaction with the genus-specific primer that amplifies the dnaJ genes and subsequent dot blot analysis with species-specific oligonucleotide probes are most useful for differential diagnosis of tuberculosis and nontuberculous mycobacterial infections.

Base Sequence↗

PubMed1978

Sensitivity of TSTA and species-specific cell membrane antigens of tumor cells to glutaraldehyde treatment.

In vivo immunogenicity and in vitro species-specific membrane antigens in tumor cells treated or untreated with glutaraldehyde (GA) were studied. Two different syngeneic Syrian hamster transplantable tumor cell lines (spontaneous liver cancer and SV40-induced sarcoma) not only lost immunogenicity after GA treatment but were responsible for enhancement of test-tumor growth in immunized animals. In vitro mixed hemadsorption test used for determination of species-specific membrane antigens in Syrian hamster, green monkey and interspecies hybrid cells revealed drastic alteration of antigens on the membrane of cells treated with GA.

Aldehydes↗

PubMed1979

[Hyperacute rejection of renal xenografts after presensitization of the recipients induced by treatment with donor species-specific spleen antigen (author's transl)].

This paper reports about experimental xenografting of kidneys in closely related species (fox/dog) modifying primary graft rejection by pretreatment of the recipients with semisoluble donor species-specific spleen antigen. This kind of pretreatment does not induce immunological enhancement which protects the graft from damage, but causes presensitization of the recipients and subsequently the hyperacute rejection of the transplants. Arteriovenous gradients of platelets and leukocytes as well as those of fibrinogen and clotting factors II, V, VIII, and IX suggest a greater degree of intravascular coagulation within the first minutes after revascularization. Hemagglutinating antibodies induced by pretreatment of the recipients with donor species-specific spleen extract seem to be responsible for the rapidity of rejection and for the reduction of survival time.

Animals↗

PubMedDate not supplied

Species-specific field testing of Entamoeba spp. in an area of high endemicity.

Entamoeba histolytica has been separated in recent years into 2 morphologically identical species: the apathogenic E. dispar and the pathogenic E. histolytica, only the latter being pathogenic. Although various laboratory techniques allow discrimination between the 2 species there is a lack of field data about the suitability of available diagnostic tests for use in epidemiological studies and few epidemiological studies using species-specific diagnosis have been performed at community level in endemic areas, especially in sub-Saharan Africa. We conducted a repeated cross-sectional study of 967 schoolchildren in central Côte d'Ivoire to compare and evaluate light microscopy, 2 different antigen detection assays, and one polymerase chain reaction (PCR) assay. Microscopy and a non-specific antigen capture Entamoeba enzyme-linked immunosorbent assay (ELISA) were used for the primary screening of all children (time t0). The prevalence of the E. histolytica/E. dispar species complex at t0 was 18.8% by single microscopical examination and 31.4% using the non-specific ELISA. Approximately 2 months after the initial screening, fresh stool specimens were collected on 2 consecutive days (t1 and t2) from (i) all the children who were positive by microscopy at t0 (n = 182) and (ii) 155 randomly selected children who were negative at the primary screening. These samples were tested with a second antigen detection ELISA specific for E. histolytica (n = 238) and with a species-specific PCR assay (n = 193). The second and third examinations (t1 and t2) revealed an additional 43 infections with the species complex E. histolytica/E. dispar, so that the cumulative microscopical prevalence for t1 and t2 was 27.7%. The overall prevalence of E. histolytica by species-specific ELISA antigen detection was low (0.83%), while the prevalence of E. dispar was 15%. When analysing only microscopically positive samples by PCR (n = 129), the ratio E. histolytica: E. dispar was very low (1:46), suggesting that the vast majority of Entamoeba infections in this area were apathogenic. Both species-specific tests performed well but the ELISA was easier to use for large-scale field screening.

Adolescent↗

PubMed2002

Response of testicular antioxidant enzymes to hexachlorocyclohexane is species specific.

AIM: To find out whether the response of testicular oxidative stress parameters to hexachlorocyclohexane (HCH) is species specific. METHODS: In rats and mice (n=5 in each group), HCH was administered at a dose of 20 mg/kg/day intraperitoneally for 30 days in 0.1 ml of refined groundnut oil. The control groups received equal volume of the vehicle. Animals were sacrificed 24 hours after the last injection and various oxidative stress parameters were measured immediately. RESULTS: The level of both endogenous as well as FeSO4 and ascorbic acid-stimulated lipid peroxidation was increased significantly in the HCH-treated rats, whereas the pattern was just the reverse in case of mice. Although the level of H2O2 content increased in response to HCH in both groups, a totally different trend was observed for the activity of the principal H2O2-metabolising enzyme, catalase. In case of rats, a significant decline in the activity of catalase was recorded in response to HCH whereas a sharp augmentation in the enzyme activity was noticed in mice. Similarly, the decreased activity of superoxide dismutase observed in rats remained unaltered in mice. CONCLUSION: HCH induces oxidative stress in the testis of both rats and mice. However, the pattern of response of testicular oxidative stress parameters seems to be species specific.

Animals↗