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At least 973 records · Page 54Linked to original sources
PubMed2002

Species-specific cell adhesion of enteropathogenic Escherichia coli is mediated by type IV bundle-forming pili.

Enteropathogenic Escherichia coli (EPEC) is a causative agent of diarrhoea in humans. Localized adherence of EPEC onto intestinal mucosa was reproduced in an in vitro adherence assay with cultured human epithelial cells. We found that the efficiency of EPEC adherence to a mouse-derived colonic epithelial cell line, CMT-93, was remarkably lower than its adherence to human-derived intestinal cell lines, such as Intestine-407 or Caco-2. Although EPEC did adhere to some cell lines derived from non-human species, fixing the cells with formalin to inactivate one or more formalin-sensitive factors allowed us to observe species-specific differences in EPEC adherence. In contrast to these results, an EPEC mutant that is defective in bundle-forming pili (BFP) production adhered as efficiently to CMT-93 cells as to Caco-2 cells. Furthermore, Citrobacter rodentium expressing BFP adhered to Caco-2 cells much more efficiently than to CMT-93 cells. Finally, a purified BfpA-His6 fusion protein showed higher affinity for Caco-2 cells than for CMT-93 cells, and inhibited EPEC adherence. Following BFP-mediated adherence, secretion of EspB from adherent bacteria and reorganization of F-actin in the host cells was observed. EPEC adhering to CMT-93 cells induced far less secretion of EspB, or reorganization of F-actin in the host CMT-93 cells, than did EPEC adhering to Caco-2 cells. These results indicated that BFP plays an important role in the cell-type-dependent adherence of EPEC and in the progression to the later steps in EPEC adherence.

Actins↗
PubMed1988

Exact definition of species-specific and cross-reactive epitopes of the 65-kilodalton protein of Mycobacterium leprae using synthetic peptides.

With the use of solid phase synthesis of peptides corresponding to major and minor peaks in a Hopp-Woods hydrophilicity plot, the epitopes for 10 of 14 known different mAb to the Mycobacterium leprae 65-kDa protein, a prominent T and B cell Ag of this bacillus, have been located in the primary structure. Five epitopes have been precisely mapped by using the synthetic peptides in inhibition ELISA experiments, and five others have been located on peptides of 22 amino acids or less in length. The epitope of an important species-specific antibody, IIIE9, which may be useful for seriodiagnosis of leprosy, appears to be distinguished from the epitope of the antibody IVD2, widely cross-reactive among mycobacteria, not by its sequence, but only by its critical residues. All epitopes studied appear continuous insofar as can be determined by this approach.

Amino Acid Sequence↗
PubMed2003

Infection of macaques with simian immunodeficiency virus induces a species-specific antibody response to major histocompatibility complex class I and class II molecules.

Envelopes of retroviruses, including human immunodeficiency virus and simian immunodeficiency virus (SIV), contain host cell proteins that potentially represent novel targets for vaccine development. We show here that sera from rhesus macaques recognized simian major histocompatibility complex (MHC) molecules in response to infection with SIV. Antibodies from these animals did not cross-react with human MHC antigens on mitogen-activated peripheral blood mononuclear cells. The development of antibodies to MHC class I alpha-chain did not correlate with anti-SIV envelope antibody responses, suggesting that these antibodies did not arise through molecular mimicry. In contrast to the species-specific response in infected animals, sera from animals vaccinated with inactivated human cell-grown SIV reacted to both human and rhesus MHC class I and class II molecules.

Animals↗
PubMed2000

Evidence for the involvement of a species-specific embryonic protease in zona escape of hamster blastocysts.

The source and nature of zona lytic factors during zona escape of hamster blastocyts were investigated. When cultured in hamster embryo culture medium (HECM)-2h, all 8-cell embryos (n = 135) developed to zona escaped-blastocysts with complete zona lysis. In addition, 2-cell embryos, when co-cultured with zona escaping-blastocysts (at a ratio of 1:10), exhibited zona lysis. Various other embryos at the 1-8-cell stages also showed zona lysis when cultured with zona-escaping blastocysts. However, zonae from mice, rats, sheep and humans were resistant to lysis under these conditions. Pronase treatment resulted in rapid zona lysis in hamsters (7 +/- 1 s), whereas in other species zona lysis was much slower: mouse (662 +/- 27 s), rat (532 +/- 16 s), sheep (120 +/- 12 s) and human (104 +/- 8 s). When cysteine protease inhibitors (antipain, leupeptin, E-64 and p-hydromercuricbenzoate) were tested, they completely inhibited zona escape, while trypsin inhibitors (TLCK and SBTI) did not. Uterine zona lysin contribution in zona escape was discounted since: (i) uterine luminal flushing and endometrial extract from day 4 (the time of zona escape in vivo) pregnant females failed to lyse zonae and (ii) endogenous oocytes and transferred 2-cell embryos (to day 3 pseudopregnant recipients) were all zona-intact, while 71% of transferred blastocysts exhibited zona escape, following their recovery after 24 h. These observations suggest that a species-specific, embryonic proteolytic factor, with a cysteine protease-like activity, is involved in the zona escape of blastocysts in hamsters.

Animals↗
PubMed1992

Construction and functional analysis of hybrid interleukin-6 variants. Characterization of the role of the C-terminus for species specificity.

We have constructed several hybrid human interleukin-6 (IL-6) variants in which the carboxyl-terminus, which includes a receptor binding site of IL-6 has been replaced with the C-terminus of various proteins homologous to human IL-6. IL-6 hybrids with the C-terminus of human growth hormone and human granulocyte-colony stimulating factor maintain part of the biological activity of human IL-6. Replacing the C-terminus of human IL-6 with the C-terminus of mouse and rat IL-6 resulted in a normal or increased activity on a mouse cell line; however, this gave a low (to 200-fold less) activity on a human cell line compared to wild-type human IL-6. We therefore conclude that the C-terminus of IL-6 plays an important role in the species specificity of IL-6.

Amino Acid Sequence↗
PubMed1979

No evidence for the existence of a species-specific renin substrate in plasma from normal and bilaterally nephrectomized rats.

Renin substrate in plasma from normal and biolaterally nephrectomized rats was measured using an excess of rat or rabbit renin which had the same pressor activity when directly assayed in the rat. The amounts of angiotensin I generated with an excess of rat renin were similar to those generated with an excess of rabbit renin in plasma from normal and bilaterally nephrectomized rats. Further addition of an excess of homologous renin to the incubation mixture did not generate more angiotensin I from normal and bilaterally nephrectomized rat plasma which had been incubated before with an excess of rabbit renin. The isoelectric focusing profiles of plasma renin substrate from normal and bilaterally nephrectomized rats were almost identical using an excess of either rat or rabbit renin. It is concluded that there is no species-specific renin substrate for homologous renin in normal or bilaterally nephrectomized rats.

Angiotensin I↗
PubMed1987

The low-molecular-mass, cysteine-rich outer membrane protein of Chlamydia trachomatis possesses both biovar- and species-specific epitopes.

We isolated, by hydroxylapatite high-performance liquid chromatography, 14- and 15-kilodalton (kDa), cysteine-rich outer membrane proteins from Chlamydia trachomatis TW-5/OT (serovar B) and LGV-434 (serovar L2), respectively. Monoclonal antibodies (MAbs) were generated against the purified proteins, and their specificities were determined by immunoblotting. MAb B-14k recognized an epitope located on the 14-kDa cysteine-rich protein of the TW-5/OT strain and was immunoreactive with a comigrating 14-kDa protein that was common to all trachoma biovar strains, but it did not react with the 15-kDa, cysteine-rich protein of LGV biovar strains. In contrast, MAb L2-15k, which recognized an epitope located on the 15-kDa protein of the LGV-434 strain, reacted with the 15- and 14-kDa, cysteine-rich proteins of both LGV and trachoma biovar strains, but did not react with related proteins of two Chlamydia psittaci strains. Thus, the low-molecular-mass, cysteine-rich outer membrane proteins of C. trachomatis possess antigenic determinants that are both biovar and species specific. Neither MAbB-14k nor MAb L2-15k was reactive by dot-blot assay when viable chlamydiae were used as test antigens, indicating that the cysteine-rich proteins are not accessible to antibody on the native chlamydial cell surface.

Antibodies, Bacterial↗
PubMed2006

The N-terminus of rodent and human MAD1 confers species-specific stringency to spindle assembly checkpoint.

The spindle assembly checkpoint (SAC) guards against chromosomal mis-segregation and the emergence of aneuploidy. SAC in higher eukaryotes includes at least 10 proteins including MAD1-3, BUB1-3, and Msp1. A long-standing observation has been that rodent cells are more tolerant of microtubule toxins than primate cells indicating that SAC function is more relaxed in the former than the latter. Here, we report on an unexpected functional difference between the rodent and human MAD1 component of the respective SAC. Ectopic expression of human MAD1 in mouse and hamster cells corrected a relaxed SAC to a more stringent form. Our findings posit MAD1 as a species-specific determinant which influences the stringency of cellular response to microtubule depolymerization and spindle damage.

Amino Acid Sequence↗
PubMed1997

Species-specific alteration of hepatic glucose 6-phosphate dehydrogenase activity with coplanar polychlorinated biphenyl: evidence for an Ah-receptor-linked mechanism.

We examined the in vivo effect of a highly toxic coplanar polychlorinated biphenyl (PCB) on the hepatic activity of glucose 6-phosphate dehydrogenase (G6PDH) in aryl hydrocarbon (Ah)-responsive (C57/BL) and -less-responsive (DBA) strains of mice. The activity in the C57BL strain was moderately increased by 3,3',4,4',5-pentachlorobiphenyl (PCB 126) in a dose dependent manner. However, this was not observed in DBA mice although greater doses were injected. 2,2',5,5'-Tetrachlorobiphenyl (PCB 52) with a non-planar structure did not increase G6PDH activity. The increase in G6PDH activity with PCB 126 was also seen in rats, but not in guinea pigs. The activity in the latter species was decreased rather than increased. These results suggest that the induction of hepatic G6PDH by coplanar PCB is mediated by a mechanism involving the Ah receptor, and the response was highly species-specific.

Animals↗
PubMed2006

Assembly factor Omp85 recognizes its outer membrane protein substrates by a species-specific C-terminal motif.

Integral beta-barrel proteins are found in the outer membranes of Gram-negative bacteria, mitochondria, and chloroplasts. The assembly of these proteins requires a proteinaceous apparatus of which Omp85 is an evolutionary conserved central component. To study its molecular mechanism, we have produced Omp85 from Escherichia coli in inclusion bodies and refolded it in vitro. The interaction of Omp85 with its substrate proteins was studied in lipid-bilayer experiments, where it formed channels. The properties of these channels were affected upon addition of unfolded outer-membrane proteins (OMPs) or synthetic peptides corresponding to their C-terminal signature sequences. The interaction exhibited species specificity, explaining the inefficient assembly of OMPs from Neisseria in E. coli. Accordingly, the in vivo assembly of the neisserial porin PorA into the E. coli outer membrane was accomplished after adapting its signature sequence. These results demonstrate that the Omp85 assembly machinery recognizes OMPs by virtue of their C-terminal signature sequence.

Amino Acid Motifs↗
PubMed2006

Species specificity of mammalian connexin-26 to form open voltage-gated hemichannels.

Mutations of connexin-26 (Cx26) cause nonsyndromic hearing loss and other syndromes affecting ectoderm-derived tissues. While the exact mechanisms underlying these diseases remain elusive, Cx's are generally considered to mediate cell-to-cell communication by forming gap junction channels. We show here that unlike rat Cx26, human and sheep Cx26 form voltage-gated hemichannels when expressed in oocytes and Neuro2A cells. A single evolutionary amino acidic change at position 159 of the rodent protein, the replacement of aspartic acid with asparagine in the human and sheep proteins, accounts for this species specificity. At the resting potential and in normal millimolar extracellular calcium, open human Cx26 hemichannels can be detected both electrophysiologically and by dye uptake, although they did not affect cell viability. These hemichannels opened at approximately -50 mV and their activation increased by depolarization until they inactivate at positive membrane potentials. Single-channel analysis revealed that activation and inactivation involved two distinct voltage gating mechanisms and that the fully open hemichannel displays a conductance twice that of the intercellular channel. The existence of a hemichannel that opens under physiological control of the membrane potential may have important implications for the normal and pathological activity of Cx26 in humans, particularly with respect to hearing and the epidermis.

Animals↗
PubMed1998

Hemopexin from four species inhibits the association of heme with cultured hepatoma cells or primary rat hepatocytes exhibiting a small number of species specific hemopexin receptors.

Hemopexin (Hx) binds heme with a very high affinity (Kd<0.1 pmol/L). It has been implicated as a major vehicle for the transport of heme into liver cells, involving a receptor-mediated recycling mechanism. However, previous studies indicated that heme is not taken up by cultured embryonic chick or adult rat hepatocytes by such a mechanism, because heme added as heme hemopexin failed to affect heme-responsive activities of 5-aminolevulinic acid synthase and heme oxygenase. Here, we investigated the importance of hemopexin in hepatic heme uptake in cultured rat hepatocytes and human HepG2 hepatoma cells, and determined the number and species specificity of hemopexin receptors on the rat hepatocytes. We also tested whether there is a difference between heterologous and homologous hemopexins. We found the following: 1) heme is inhibited from associating with hepatocytes by apo hemopexins from rat, human, rabbit, and chicken; 2) heme readily associates with hepatocytes when heme hemopexin preparations are added in which the ratio of heme to hemopexin exceeds 1.0; 3) heme induces heme oxygenase mRNA in rat hepatocytes and this induction is prevented by excess hemopexin; and 4) rat hepatocytes exhibit only about 2,000 hemopexin receptors per cell when using rat hemopexin, and none when using hemopexin of rabbit and human. We conclude that hemopexin plays a limited role in heme uptake by cultured hepatocytes and hepatoma cells, and that heme which exceeds the hemopexin binding capacity is taken up directly from heme-albumin.

Animals↗
PubMed1990

Tissue- and species-specific expression of cytochrome c oxidase isozymes in vertebrates.

Cytochrome c oxidase was isolated from brown fat tissue of the rat and compared with the isozymes from rat liver and heart, which differ at least in subunits VIa and VIII. ELISA titrations of COX from the three tissues with monospecific antisera to all 13 subunits of the rat liver enzyme showed differences between the three enzymes. The N-terminal amino-acid sequence analysis of subunits VIa and VIII from SDS-PAGE gel bands of the three enzymes indicates the occurrence of three different isozymes in the rat. N-terminal amino-acid sequence analysis of subunits VIa and VIII from cytochrome c oxidase of bovine and human heart demonstrates also species-specific differences in the expression of the 'liver-type' and 'heart-type' of subunits VIa and VIII.

Adipose Tissue, Brown↗
PubMed1998

Seroreactive species-specific lipooligosaccharides of Mycobacterium mucogenicum sp. nov. (formerly Mycobacterium chelonae-like organisms): identification and chemical characterization.

Strains of the new species Mycobacterium mucogenicum exhibit physiological and biochemical features very similar to those of the other species of the Mycobacterium fortuitum complex. To define taxonomic criteria for easy identification of M. mucogenicum, the glycolipid patterns of the reference strains and of 32 environmental and clinical isolates were examined by TLC. It was concluded that all M. mucogenicum strains of smooth colony morphology contained species-specific alkali-labile glycoconjugates. Three different patterns were observed among the strains of the smooth colony type. Fractionation followed by conventional chemical analyses of the purified glycolipids showed the specific glycolipids to be lipooligosaccharides (LOS). The three LOS showed a similar fatty acid composition consisting of straight chain (dodeca-, tetradeca-, hexadecanoyl and hexadecenoyl) and methylbranched (2,4-dimethyleicosanoyl and 2,4-dimethyleicosenoyl) fatty acyl substituents. The most commonly encountered LOS (present in 76% of the smooth strains) contained a tetraacylated pentasaccharide composed of four moles of glucose and one mole of a 2,4-di-O-methylhexose. A LOS composed of arabinose, glucose and mannose was present in 20% of the smooth strains, whereas the newly proposed type strain of M. mucogenicum (ATCC 49650) was the only strain that contained a LOS composed of glucose and galactose. Serological studies clearly differentiated most of the strains of M. mucogenicum from those of the other members of the M. fortuitum complex, and demonstrated the existence of serovars within the former species. Altogether, these data confirm the validity of the new species but show ATCC 49651 to be the most representative strain.

Animals↗
PubMed1987

Use of species-specific DNA probes for detection and identification of trypanosome infection in tsetse flies.

Species- and subspecies-specific trypanosome DNA hybridization probes have been employed in the detection and identification of trypanosome infections in Glossina morsitans centralis. Several ways of sample preparation including the use of tsetse organ suspensions, proboscides and dissected midguts, as well as tsetse abdominal content touch-blots were explored. The results of hybridization of radio-isotope-labelled species-specific DNA probes to tsetse samples indicated that it was possible to detect trypanosomes in the organs where parasite development is known to characteristically occur for each subgenus. Duplicate slot-blots of samples prepared from midguts of tsetse infected with 2 strains of T. congolense and from non-infected fly controls show that it is not only possible to detect infection in tsetse but also to identify the strain of parasite present in a sample after hybridization with the DNA probes specific for each strain. The results, obtained after hybridization of sequential abdominal touch-blots from the same fly with the DNA probe specific for one strain of T. congolense, indicated that at least 8 positive signals can be observed after an overnight exposure. Because of their simplicity and potentially low cost, the techniques described here would be appealing for screening large numbers of tsetse samples from the field for the presence of any trypanosome residing in the guts or proboscis of the vector. In addition, the possibility of doing multiple touch-blots from the same fly gives the opportunity of detecting mixed trypanosome infections in the vector.

Animals↗
PubMed1987

Immunoblotting of Creutzfeldt-Jakob disease prion proteins: host species-specific epitopes.

Creutzfeldt-Jakob disease (CJD) is a rare dementia that is generally found in older people and is caused by unusual infectious pathogens or prions. Using rabbit antisera raised against hamster scrapie prion proteins (HaPrPSc), we identified by immunoblotting human CJD prion proteins (HuPrPCJD) in the brains of 14 patients dying of CJD. Extracts from 6 of the patients were transmitted to mice after prolonged incubation. The rabbit antisera raised against HaPrPSc also reacted with the mouse CJD prion proteins (MoPrPCJD) found in the brains of these experimentally infected mice. When mice were immunized with HuPrPCJD, they produced antibodies that reacted with HuPrPCJD but not with MoPrPCJD. Mice immunized with MoPrPCJD produced antibodies to neither murine nor human prion proteins. Our results provide evidence for host species-specific epitopes on prion proteins. The existence of such epitopes is consistent with the apparent lack of an immune response during prion infections and the finding that prion protein molecules are encoded by host genes.

Brain↗
PubMed2001

Species-specific differences in the operational RNA code for aminoacylation of tRNA(Trp).

Identity elements play essential roles in the recognition of tRNAs by their cognate aminoacyl-tRNA synthetase. An operational RNA code relates amino acids to specific sequences and structural features of tRNA acceptor stems. In this study, a series of tRNA(Trp) variants was prepared by in vitro transcription and their efficiencies of aminoacylation by tryptophan (k(cat)/K(m)) were measured with the aid of Bacillus subtilis and human tryptophanyl-tRNA synthetases (TrpRS). The identity elements in the operational RNA code of human tRNA(Trp) were found to be: major element, discriminator base A73; minor elements, G1/C72 and U5/G68. From the cross-species aminoacylation assays, we conclude that the identity elements in tRNA(Trp) from B.subtilis and human all contribute to species-specific aminoacylation by TrpRS. Analyses of 22 TrpRS sequences covering three taxonomic domains (bacteria, eukarya and archaea) reveal that the sequences are divided into two evolutionarily distant groups. The same partition is also observed in the analyses of tRNA(Trp) acceptor stem sequences. Our data suggest that the two TrpRS groups may reflect co-adaptations needed to accommodate changes in the operational RNA code for tryptophan.

Acylation↗
PubMed1981

Tissue and species-specific effects of small molecular weight nuclear RNA's on transcription in isolated mammalian nuclei.

Small molecular weight nuclear RNA's (SnRNA's) purified from the 0.35 M NaCl extract of chromatin from human and monkey tissues have been found to stimulate transcription of chromatin in isolated nuclei in a tissue- and species-specific manner. While SnRNA from normal human cells (WI38 fibroblasts and placenta) stimulates homologous transcription to some extent, it has a greater activity on transcription of heterologous tissue of the same species and no activity on heterologous tissue of a different species (monkey kidney cells). Likewise SnRNA from monkey cells stimulates transcription of homologous chromatin but has no effect on human cells. Fractionation of the RNA's in polyacrylamide gradient slab gels revealed that in all cases the active RNA was 160-175 nucleotides in length. Our results are compatible with the hypothesis that the active RNA's are involved in the determination and maintenance of tissue differentiation by recognizing promoter or regulator sequences in the DNA and act at the level of the nucleosome to induce tissue-specific genes.

Animals↗