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PubMed1996

Regulation of the Serratia marcescens extracellular nuclease: positive control by a homolog of P2 Ogr encoded by a cryptic prophage.

The Serratia marcescens extracellular nuclease is a secreted protein that is subject to growth phase and SOS control. Regulatory mutants affecting nuclease expression have been isolated that define a new locus, nucC, essential for transcription of the nuclease gene nucA. The cloned nucC gene is able to activate efficient expression from the nucA promoter in Escherichia coli, where it normally is poorly expressed. NucC is very similar to the bacteriophage P2 Ogr protein, a transcriptional activator essential for P2 late gene expression. NucC is able to replace P2 Ogr to support the growth of P2 ogr- mutants in E. coli. Ogr is a poor activator of the nuclease promoter in E. coli, but the related delta gene product from satellite phage P4 is highly effective. The presence of genes encoding a lysozyme and a putative porin or holin in the nucC operon suggests that nucC may be part of a cryptic prophage genome. The putative holin-like membrane protein is required in E. coli for extracellular secretion of the S. marcescens nuclease.

Amino Acid Sequence↗
PubMed1997

Biological relationship between F18ab and F18ac fimbriae of enterotoxigenic and verotoxigenic Escherichia coli from weaned pigs with oedema disease or diarrhoea.

Comparative fimbrial expression and adhesion studies were made on enterotoxigenic and verotoxigenic E. coli (ETEC and VTEC) strains isolated from cases of porcine postweaning diarrhoea or oedema disease. F107(F18ab) fimbriae--monitored by polyclonal and monoclonal antibodies and by electron microscopy--were poorly expressed on most VTEC strains. In contrast, 2134P(F18ac) fimbriae were more readily detected on most ETEC strains. The F18ac strains adhered in vivo to ligated intestinal loops in weaned pigs while the F18ab strains did not adhere or adhered weakly. Similarly, the F18ac strains adhered to isolated intestinal brush borders in weaned pigs but the F18ab strains (except for the F107 reference E. coli) did not adhere or adhered weakly in vitro. Neither the F18ab nor F18ac strains adhered to brush borders from newborn pigs. In vitro adhesion of F18ab and F18ac strains was mannose resistant and receptors for F18 seemed to differ from receptors for K88(F4). It is concluded that the antigenic variants of F18 fimbriae (F18ab and F18ac) are biologically distinct. F18ab fimbriae are expressed poorly both in vitro and in vivo and are frequently linked with the production of SLT-IIv and serogroup O139, while F18ac are more efficiently expressed in vitro and in vivo and most often are linked with enterotoxin (STa, STb) production, and serogroups O141, O157.

Animals↗
PubMed1992

High expression vectors for the production of recombinant single-chain urinary plasminogen activator from Escherichia coli.

An expression cassette containing a synonymous gene for human single-chain urokinase-type plasminogen activator (Rscu-PA) 5'-flanked by a trp promoter and the Shine-Dalgarno sequence of the xyl A operon of Bacillus subtilis and terminated by the terminators trp A and Tn10 was constructed and inserted into a pBR322 derivative to yield pBF160. When compared to pUK54 trp 207-1 containing the natural scu-PA gene without the Shine-Dalgarno sequence and terminator, the expression efficiency of pBF160 in Escherichia coli strains was improved by one order of magnitude. Replacement of the trp by the tac promoter (pBF171) did not affect expression. Inserting the Shine-Dalgarno sequence and Tn10 terminator into pUK54 trp 207-1 (pWH1320) slightly increased the expression level, whereas elimination of the Shine-Dalgarno sequence and the terminators from pBF160 with almost complete conservation of the synonymous structural gene (pBF191) significantly reduced the expression. Variation of the distance between the Shine-Dalgarno sequence and the start codon between 8 and 10 bp (pBF163) proved irrelevant. In conclusion, poor expression of mammalian genes in E. coli may result from both improperly designed regulatory elements and structural features of the coding region and therefore de-novo synthesis of the gene may be required to obtain satisfactory expression.

Amino Acid Sequence↗
PubMed2000

Expression and characterization of nonmammalian selenoprotein P in the zebrafish, Danio rerio.

BACKGROUND: Selenoprotein P is a protein of considerable intrigue, due to its unusual composition and requirements for its biosynthesis. Whereas most selenoproteins contain a single selenocysteine residue, the human, bovine and rodent selenoprotein P genes encode proteins containing 10-12 selenocysteines. Selenoprotein P genes have, to date, only been reported in mammals, and the function of the protein remains elusive. RESULTS: Herein, we report the identification and characterization of nonmammalian selenoprotein P in the zebrafish Danio rerio. Sequencing of the cDNA revealed the presence of 17 selenocysteine codons, the highest number reported in any protein. Two histidine-rich regions present in the mammalian selenoprotein P sequences are conserved in the zebrafish protein, and two SECIS elements are present in the 3' untranslated region. Whole-mount in situ hybridization of zebrafish embryos revealed high levels of expression of selenoprotein P mRNA in fertilized eggs and in the yolk sac of developing embryos. Transient transfection of the cDNA in mammalian cells resulted in efficient expression of the full-length secreted selenoprotein. A single N-glycosylation site is predicted, and shown to be utilized. CONCLUSIONS: Discovery of selenoprotein P in the zebrafish opens a previously unavailable avenue for genetic investigation of the functions of this unusual protein.

Amino Acid Sequence↗
PubMed1999

MHC class II alpha/beta heterodimeric cell surface molecules expressed from a single proviral genome.

Transplantation tolerance to renal allografts can be induced in large animal preclinical models if the donor and recipient have identical major histocompatibility complex (MHC) class II loci. Such class II matching is, however, not clinically achievable owing to the extreme diversity of class II sequences. With the ultimate goal of creating a somatic class II match in the bone marrow of an allograft recipient, the aim of the study is to develop a double-copy retrovirus construct to express both chains of the MHC class II DQ glycoprotein on a single transduced cell. Analysis of the expression patterns of the retroviral DQ transgenes in both virus producer and transduced fibroblasts revealed correct transcription and stable surface expression of the DQ heterodimers. In addition, we demonstrate that both the DQA and DQB sequences are functional within the same proviral copy, a prerequisite for efficient induction of transplantation tolerance following transduction of bone marrow precursor cells. The DQ double-copy retrovirus vector showed efficient expression of the transferred class II cDNA in murine colony-forming units for the granulocyte-monocyte lineage (CFU-GM), indicating that it is suitable for gene therapy of multimeric proteins in hematopoietic cells.

3T3 Cells↗
PubMed1997

Overexpression in Escherichia coli of chemically synthesized gene for active 0.19 alpha-amylase inhibitor from wheat kernel.

A synthetic gene encoding 0.19 alpha-amylase inhibitor (alpha-AI) from wheat kernel was obtained by enzymatic assembly of 18 oligodeoxynucleotides which were chemically synthesized. The synthetic gene was introduced into vector pET15b for expression in Escherichia coli BL21(DE3) under the control of T7 promoter. However, in SDS-PAGE and Western blotting analyses of the E. coli cell lysate, the expression product could not be detected. Expression analysis for various partially deleted gene fragments suggested that the putative hairpin-like structure of mRNA in the 5'-terminal coding region might interrupt efficient expression. When the hairpin structure was eliminated by using degenerate codons, the resulting gene could be overexpressed in E. coli. Although the gene product was accumulated in an insoluble fraction as inclusion bodies, its inhibitory activity could be recovered by solubilization with 8 M urea, followed by refolding through two successive steps of dialysis at alkaline pH. After purification, the recombinant 0.19 alpha-AI showed the same characteristics as the authentic inhibitor in terms of N-terminal amino acid sequence, peptide mapping on reverse-phase HPLC, far-UV circular dichroism (CD) spectrum and have inhibition of human salivary alpha-amylase. Thus, we have established an overexpression system in E. coli for active recombinant 0.19 alpha-AI.

Amino Acid Sequence↗
PubMed1995

Molecular cloning, expression, and characterization of a human intestinal 15-kDa protein.

We have isolated a cDNA encoding a human intestinal 15-kDa protein (I-15P) from a human ileal lambda gt 11 cDNA library, using a full-length rat I-15P cDNA. One clone encompassed 571 nucleotides and encoded a 128-amino-acid protein with a calculated molecular mass of 14355 Da. The deduced amino acid sequence of human I-15P showed high similarity to the rat counterpart (78%), mouse ileal lipid-binding protein (80%) and porcine gastrotropin (75%). It also exhibited 36% similarity to human liver fatty-acid-binding protein (L-FABP). Northern blot analysis of human I-15P revealed a single transcript only in ileum, however, the reverse-transcription/PCR demonstrated expression in ovary and placenta, but it was much lower than in ileum. Transformation of Escherichia coli with the I-15P cDNA resulted in the efficient expression of a protein that was identical to the ileal cytosolic I-15P. In vitro binding studies revealed that the bacterially expressed recombinant I-15P showed much lower affinities for palmitate and oleate than L-FABP. However, it showed similar affinity for taurocholate, compared with a control, BSA. Comparison of the structural features of human I-15P and human L-FABP suggested that loss of a long alpha-helix region and hydrophobic profile of I-15P may be attributable to a unique ligand-binding specificity of I-15P.

Aged↗
PubMed1997

Expression of gp19K increases the persistence of transgene expression from an adenovirus vector in the mouse lung and liver.

Activation of the cellular immune system and subsequent lysis of vector-transduced cells by adenovirus- or transgene-specific cytotoxic T lymphocytes have been shown to limit transgene expression in animal models. The adenovirus gp19K gene product associates with major histocompatibility complex class I proteins and prevents their maturation by sequestering them in the endoplasmic reticulum. gp19K has been shown to block the ability of adenovirus-specific cytotoxic T lymphocytes to recognize virus-infected cells in vitro. To determine if gp19K expression in an adenovirus vector would increase transgene persistence, a vector that replaces the E1 region of adenovirus with an expression cassette encoding both gp19K and beta-glucuronidase was constructed. This vector produced high levels of functional gp19K in infected cells. RNase protection analysis revealed efficient expression of the gp19K gene in the mouse lung. Enhanced persistence and increased beta-glucuronidase activity were observed in the lung and liver following delivery of the gp19K-expressing adenovirus vector in B10.HTG mice but not in BALB/c mice. Since gp19K binds to both class I alleles on B10.HTG mice but only one allele on BALB/c mice, these results suggest that the major histocompatibility complex class I haplotype of mice is important in determining the effectiveness of gp19K in vivo. Since gp19K has previously been shown to interact with every human major histocompatibility complex class I allele tested, the inclusion of gp19K in gene therapy vectors may increase vector persistence in human gene therapy trials.

Adenoviridae↗
PubMed2006

Phenotypic correction of von Willebrand disease type 3 blood-derived endothelial cells with lentiviral vectors expressing von Willebrand factor.

Von Willebrand disease (VWD) is an inherited bleeding disorder, caused by quantitative (type 1 and 3) or qualitative (type 2) defects in von Willebrand factor (VWF). Gene therapy is an appealing strategy for treatment of VWD because it is caused by a single gene defect and because VWF is secreted into the circulation, obviating the need for targeting specific organs or tissues. However, development of gene therapy for VWD has been hampered by the considerable length of the VWF cDNA (8.4 kb [kilobase]) and the inherent complexity of the VWF protein that requires extensive posttranslational processing. In this study, a gene-based approach for VWD was developed using lentiviral transduction of blood-outgrowth endothelial cells (BOECs) to express functional VWF. A lentiviral vector encoding complete human VWF was used to transduce BOECs isolated from type 3 VWD dogs resulting in high-transduction efficiencies (95.6% +/- 2.2%). Transduced VWD BOECs efficiently expressed functional vector-encoded VWF (4.6 +/- 0.4 U/24 hour per 10(6) cells), with normal binding to GPIbalpha and collagen and synthesis of a broad range of multimers resulting in phenotypic correction of these cells. These results indicate for the first time that gene therapy of type 3 VWD is feasible and that BOECs are attractive target cells for this purpose.

Animals↗
PubMed1992

The transmembrane and flanking sequences of beta 1,2-N-acetylglucosaminyltransferase I specify medial-Golgi localization.

UDP-GlcNAc:alpha 3-D-mannoside beta 1,2-N-acetylglucosaminyltransferase I (GnTI) is an N(in)/C(out) (type II) membrane protein, localized in the medial-Golgi, that initiates the conversion of high mannose N-glycans to complex N-glycans. Anti-rabbit GnTI antibodies were generated using a purified, enzymatically active, bacterial recombinant fusion protein as immunogen. Rabbit GnTI was effectively retained in the Golgi complex of transfected COS-1 cells and murine L cells, as assessed by indirect immunofluorescence using the species-specific anti-GnTI antibodies; no surface expression of rabbit GnTI could be detected in the transfected cells. Rabbit GnTI, stably expressed in murine L cells, was localized by immunoperoxidase electron microscopy to the medial-cisternae of the Golgi stack. The role of the transmembrane domain of GnTI in Golgi localization was examined by generation of a hybrid construct containing the amino-terminal 31 amino acids of GnTI, corresponding to the 25-residue transmembrane (signal/anchor) domain and flanking hydrophilic sequences, fused with ovalbumin; this ovalbumin/GnTI hybrid molecule was retained in the Golgi complex of transfected COS cells and stably transfected murine L cells. No surface expression of ovalbumin/GnTI was detected. In contrast, ovalbumin fused to the equivalent domains of the human transferrin receptor, a type II cell-surface protein, was efficiently expressed on the cell surface of transfected cells. The ovalbumin/GnTI hybrid molecules in the transfected L cells were N-glycosylated, indicating an N(in)/C(out) membrane orientation, and were localized by immunoperoxidase electron microscopy to one or two cisternae of the medial-Golgi (90% of stained Golgi profiles showed medial-cisternae staining). These results show that a signal contained within the transmembrane domain and flanking residues of GnTI specifies medial-Golgi localization.

Amino Acid Sequence↗
PubMed2005

[Modification of the sunflower defensin SD2 gene sequence and its expression in bacterial and yeast cells].

To achieve broader range of the defensin antimicrobial activity, based on the sd2 gene sequence, the modified gene, sd2mod, was constructed. Hybrid genes, sd2-licBM2, licBM2-sd2, licBM2-sd2mod, and sd2mod-licBM2, in which the wild-type and modified gene sequences were fused in frame with the reporter gene encoding thermostable lichenase, were constructed. Expression of the wild-type, modified, and hybrid genes was examined in the cells of pro- and eukaryotes. It was demonstrated that these genes were efficiently expressed in the cells of lower eukaryotes, the yeast. Inhibiting effect of the SD2 and SDmod proteins as the components of the hybrid proteins, SD2-LicBM2 and SD2mod-LicBM2, on the growth of the Fusarium culmorum hyphae was similar to that of the wild-type and modified proteins. It was shown that the presence of lichenase in the hybrid proteins facilitated selection and analysis of the hybrid proteins expression in transgenic organisms.

Amino Acid Sequence↗
PubMed2005

[Expression of HBV S and preS1 fusion gene in Pichia pastoris expression system].

BACKGROUND: To clone and express the ss1 recombinant gene containing S gene and preS1 (10-50 AA) gene in P. pastoris expression system. METHODS: The fusion gene ss1 containing the S (1-222 AA) gene and preS1 (10-50 AA) gene was constructed with PCR method. The fusion ss1 gene was cloned into the expression vector of pPIC3.5k. The linear vector DNA was transformed into the host cell of GS115 with electroporation method. After screening with G418, the product was induced to express with methanol and its antigenicity was analyzed. RESULTS: The molecular weight of expressed ss1 protein was about 30,000 dalton. The product was reactive to anti-HBs and anti-preS1 mAb. CONCLUSION: The fusion gene was efficiently expressed in P. pastoris expression system.The expressed products have the antigenicity of both S and preS1 protein.

Blotting, Western↗
PubMed1989

Thyroid hormone regulates the mouse thyrotropin beta-subunit gene promoter in transfected primary thyrotropes.

In TtT 97 cells, a thyrotropin-producing mouse pituitary tumor, thyroid hormone rapidly inhibits the transcription rate of both the thyrotropin alpha- and beta-subunit (TSH beta) genes, and this closely parallels the increase in nuclear thyroid hormone receptor occupancy. In this study, we have identified regions of the mouse TSH beta gene which are involved in mediating tissue-specific and thyroid hormone-regulated expression. Transient expression studies were performed using a series of chimeric plasmids in which 5'-flanking DNA was ligated to the firefly luciferase gene. Following transfection by electroporation, efficient expression of TSH beta 5'-flanking luciferase constructs occurred only in cells derived from TtT 97 tumors which express the endogenous TSH beta gene. Deletion analysis demonstrated that the region of the 5'-flanking DNA between positions -271 and -80 relative to the major transcriptional start site is important for TSH beta promoter activity in thyrotropes. No expression was measurable in mouse L cells, a fibroblast line, whereas a low level of expression was seen in MGH 101A cells derived from a thyrotropic tumor which no longer expresses the TSH beta gene. Reduced expression of TSH beta constructs was also found in GH3 and GH4 pituitary tumor lines. Addition of thyroid hormone effectively inhibited the level of transient TSH beta promoter activity in TtT 97 cells in a dose-dependent manner. The inhibitory effect was more pronounced and more accurately reflected the transcription rate data when transfected cells were derived from tumors treated with thyroid hormone for 5 days prior to transfection. Deletion of all but 46 base pairs of TSH beta gene 5'-flanking DNA and 3 base pairs of the first exon had no effect on thyroid hormone inhibition. This indicates that signals sufficient for transcriptional regulation of the TSH beta gene by thyroid hormone reside in the vicinity of the proximal promoter and may act by interfering with basal transcriptional factors.

Animals↗
PubMed1994

Transcriptional repression of apolipoprotein AI gene expression by orphan receptor ARP-1.

Expression of the apolipoprotein AI (apoAI) gene in the liver is controlled by a liver-specific enhancer. The function of this enhancer depends on synergistic interactions between transcription factors bound to at least three sites (designated A, B, and C) located within this enhancer. We have previously shown that an apoAI gene reporter construct containing the entire enhancer is expressed efficiently in a hepatoma cell line and that its activity is repressed by the orphan receptor ARP-1. Moreover, repression by ARP-1 is overcome by the retinoid X receptor RXR alpha in the presence of retinoic acid. In this study, we show that ARP-1 represses the apoAI promoter by binding to site A of the apoAI liver-specific enhancer, the repression being a promoter context-specific event. Mapping analysis of ARP-1 indicated that its DNA binding domain is essential but not sufficient for repression. Two separate repression domains located at the amino- and carboxyl-terminal halves of ARP-1 were found to individually complement the DNA binding domain for efficient repression. We also demonstrate the reversibility of ARP-1 repression by transcription factors C/EBP and Egr-1, which might also be involved in apoAI gene expression. Significantly, repression by ARP-1 was found to be a prerequisite for C/EBP-mediated transactivation. We interpret our results in terms of a model in which ARP-1 repression via its interaction with site A is an obligatory intermediate step in switching from one activated state of the apoAI gene to another.

Animals↗
PubMed1994

Human adenovirus encodes two proteins which have opposite effects on accumulation of alternatively spliced mRNAs.

All mRNAs expressed from the adenovirus major late transcription unit have a common, 201-nucleotide-long 5' leader sequence, which consists of three short exons (the tripartite leader). This leader has two variants, either with or without the i-leader exon, which, when present, is spliced between the second and the third exons of the tripartite leader. Previous studies have shown that adenovirus early region 4 (E4) encodes two proteins, E4 open reading frame 3 (E4-ORF3) and E4-ORF6, which are required for efficient expression of mRNAs from the major late transcription unit. These two E4 proteins appear to have redundant activities, and expression of one has been shown to be sufficient for efficient major late mRNA accumulation during a lytic virus infection. In this report, we provide evidence that E4-ORF3 and E4-ORF6 both regulate major late mRNA accumulation by stimulating constitutive splicing. Moreover, we show that the two proteins have different effects on accumulation of alternatively spliced tripartite leader exons. In a DNA transfection assay, E4-ORF3 was shown to facilitate i-leader exon inclusion, while E4-ORF6 preferentially favored i-leader exon skipping. In addition, E4-ORF3 and E4-ORF6 had the same effects on accumulation of alternatively spliced chimeric beta-globin transcripts. This finding suggests that the activities of the two proteins may be of more general relevance and not restricted to splicing of major late tripartite leader-containing pre-mRNAs. Interestingly, E4-ORF6 expression was also shown to stimulate i-leader exon skipping during a lytic virus infection.

Adenoviruses, Human↗
PubMed1994

A negative regulatory element of the macrophage-specific human mannose receptor gene represses its expression in nonmyeloid cells.

We have cloned the putative promoter of the human mannose receptor gene using the ligation-mediated polymerase chain reaction. This modified polymerase chain reaction method depends upon the ligation of restricted genomic DNA fragments to a sequence of DNA containing a generic primer site. Approximately 400 bp of genomic DNA sequence immediately upstream from the 5' end of the lectin gene was amplified with this strategy. Primer-extended reverse transcription identified several 5' ends of the mannose receptor mRNA corresponding to differential use of initiation transcription sites. DNA sequence analysis of the 5' flanking sequence of the mannose receptor gene indicated the presence of a TATA box and various putative binding sites for several transcription activators. The insertion of the sequence into a plasmid containing a promoterless luciferase reporter gene reveals a promoter activity with a high cell type specificity, efficient expression upon transfection into macrophage type cells, and lack of efficiency upon transfection into nonmyeloid cells. A series of deletion mutants reveals that this cell-type-specific promoter activity is mediated by a negative regulatory element located at the 5' end of the isolated promoter.

Base Sequence↗
PubMed1994

Expression of human liver fatty acid-binding protein in Escherichia coli and comparative analysis of its binding characteristics with muscle fatty acid-binding protein.

Human liver fatty acid-binding protein (L-FABP) has been efficiently expressed in Escherichia coli. The cDNA encoding human liver FABP was under the control of T7 RNA polymerase promoter in the expression vector pET-3b. Expression required overnight induction with isopropyl beta-D-thiogalactopyranoside in the presence of the bacterial RNA polymerase inhibitor, rifampicin. The protein could be purified by (NH4)2SO4 fractionation, anion-exchange and gel filtration chromatography, and was recognized by anti-(human L-FABP) antiserum. The binding characteristics of delipidated recombinant human L-FABP and muscle FABP (M-FABP) for fatty acids of different chain length and saturation grade, and for various hydrophobic ligands, were determined by radiochemical analysis and also by fluorescence for L-FABP. The apparent binding affinity of the ligands was calculated by using displacement curves of oleic acid and dansylamino-undecanoic acid (DAUDA). L-FABP showed a preference for the binding of long-chain saturated and unsaturated fatty acids up to C24:1, whereas the M-FABP has a preference for unsaturated fatty acids, especially those with 18 C atoms. L-FABP also binds palmitoyl derivatives and many other hydrophobic ligands--however, generally with a lower affinity than fatty acids. M-FABP binds--besides with fatty acids--only with oestradiol and testosterone with high affinity. Fatty acids with fluorescent reporter groups are also more tightly bound by L-FABP. A direct assay and displacement study of oleic acid gave the same Kd value of DAUDA for L-FABP. Fluorescence enhancement and displacement studies indicate that the binding of fluorescent fatty acids is determined by both the fluorescent reporter group and the acyl carbon chain.

Base Sequence↗
PubMed2001

Roles of phytanoyl-CoA alpha-hydroxylase in mediating the expression of human coagulation factor VIII.

The coagulation factor VIII (FVIII) is the coagulation factor deficient in the X-chromosome-linked bleeding disorder hemophilia A. Previous transfection studies demonstrated that factor VIII was 10-100-fold less efficiently expressed than the homologous coagulation factor, factor V. To investigate the regulatory mechanisms of FVIII synthesis and secretion, we used the yeast two-hybrid system as an approach to search for proteins that associated with FVIII. The A2 domain (337-740 amino acids) of factor VIII (FVIII-A2) was used as a bait and phytanoyl-CoA alpha-hydroxylase (PAHX) was identified as a binding protein of FVIII-A2. PAHX had potential to interact with the residues 373-508 within the A2 domain, but not with A1 and A3 (the homologous domains of A2). The interaction between the A2 domain and PAHX was independent of the type 2 peroxisomal targeting signal (PTS2) of PAHX. Overexpression of PAHX in FVIII-produced cells decreased the expression of FVIII by about 70%. The elevated expression of von Willebrand factor had no effect on the suppression of FVIII secretion by PAHX. Expression of the green fluorescent PAHX fusion protein in SMMC-7721 cells affected the intracellular trafficking of FVIII-A2. These results suggested that the interaction between PAHX and FVIII-A2 was in part responsible for the low-level expression of factor VIII.

Animals↗