Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P43026 (lipopolysaccharide)
 62,215 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

To characterize and clarify the function of CD34 antigen experimentally, we isolated two types of CD34 mRNA from a cDNA library of murine stromal cell line, PA-6 stimulated with lipopolysaccharide (LPS) and 12-o-tetra-decanoylphorbol 13-acetate (TPA) using a human CD34 probe. In addition to the clone (open reading frame [ORF]:1149bp) reported by Brown et al, a novel clone (ORF:978 bp) was obtained. The difference between the two clones was in the cytoplasmic portion of CD34; the former has 73 amino acids, while the latter has 16. We investigated the genomic sequence of cytoplasmic portion and found conserved nucleotide sequences at the exon-intron junction (GT ... AG). Thus, it was concluded that alternative splicing gave two types of CD34 mRNA. A novel clone contains the longer cDNA, including a insert of 156 bp, but results in a shorter predicted coding sequence because of the introduction of an inframe stop codon. Northern blot analysis using a murine cDNA probe (HindIII fragment, 900 bp) showed that CD34 was highly expressed in the brain and testis, and moderately in the thymus, spleen, and bone marrow, but not in adult liver. However, day 12 to 14 fetal liver cells showed significant expression of CD34. Quantitative reverse transcription polymerase chain reaction showed that spleen, thymus, bone marrow, and testis RNA gave two bands of almost equal intensity, but in the brain a novel clone was expressed three times more than the other clone. Furthermore, Northern blot analysis using a probe (156 bp) specific for the spliced intracellular region confirmed the significant mRNA expression of a novel clone. Although the biologic significance of alternative splicing remains to be elucidated, it is suggested that a different carboxyterminal tail causes a change in signal transduction.
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PMID:Two types of murine CD34 mRNA generated by alternative splicing. 137 70

Previous work from this laboratory has shown that a 26-kb insert in cosmid clone pFV100, isolated from a Pseudomonas aeruginosa gene library, contained genes that could restore serotype-specific B-band lipopolysaccharide (LPS) expression in rough mutant ge6. In this study, subclones from pFV100 were made to identify genes responsible for B-band LPS synthesis. Transformation of Escherichia coli HB101 with cosmid clone pFV100 resulted in expression of P. aeruginosa serotype O5 B-band LPS, indicating the presence of an rfb cluster in pFV100. Expression of P. aeruginosa LPS could not be achieved in E. coli HB101 transformed with any of the subclones. Complementation studies of well-characterized rough mutants of P. aeruginosa PAO1 deficient in B-band LPS biosynthesis were performed with the various subclones. Subclone pFV110, containing a 1.4-kb XbaI-HindIII insert, restored B-band LPS biosynthesis in mutant AK44 (A+B-; complete core). Probing chromosomal DNA from the 20 International Antigenic Typing Scheme serotypes with the 1.4-kb insert from pFV110 in Southern hybridizations revealed a positive reaction to restriction fragments in serotypes O2, O5, O16, O20, and O18. LPS of serotypes O2, O5, O16, and O20 were shown earlier to have a similar backbone structure in their O antigen. The insert in pFV110 was sequenced, and the deduced amino acid sequence was compared with sequences of protein databases. No significant homology could be detected with any sequences in the database. Open reading frame analysis identified one region, ORF303, which could encode a 33-kDa protein. Using E. coli maxicells for protein expression, orf303 mediated the expression of a unique polypeptide with an apparent molecular mass of 32.5 kDa. The deficiency in the synthesis of B-band LPS biosynthesis in mutant AK44 is apparently complemented by the 33-kDa protein encoded by orf303. We have designated this ORF rfbA. This investigation is the first report on cloning and sequencing of an rfb gene involved specifically in O-antigen biosynthesis in P. aeruginosa PAO1.
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PMID:Identification of rfbA, involved in B-band lipopolysaccharide biosynthesis in Pseudomonas aeruginosa serotype O5. 759 Nov 68

Campylobacter fetus cells may exist as either of two defined serogroups (type A or B) based on their lipopolysaccharide (LPS) composition. Wild-type strains contain surface array proteins (S-layer proteins) that have partial antigenic cross-reactivity but bind exclusively to LPS from homologous (type A or B) cells. Type A cells possess 8 homologs of sapA, which encodes a 97-kDa S-layer protein; the gene products of these homologs have a conserved N terminus of 184 amino acids. To further explore the structural relationships between the C. fetus S-layer proteins and their encoding genes, we sought to clone and express an S-layer protein from type B strain 84-91. The cloned type B gene (sapB) was similar in structure to the previously cloned type A gene (sapA) and encoded a full-length 936-amino acid (97-kDa) S-layer protein. Sequence analysis of sapB indicated that the conserved N-terminal encoding region in sapA was absent but that the remainder of the ORF (encoding 751 amino acids) was identical to that of sapA in spite of the nonconserved nature of this region among sapA homologs. Noncoding sequences both 300 base pairs 5' and 1000 base pairs 3' to the sapB and sapA ORFs, including the sapA promoter and transcriptional terminator sequences, were essentially identical. Southern analyses revealed that the sapB N-terminal encoding region was conserved in multiple copies in type B strains but was absent in type A strains. Recombinant sapA and sapB products bound to a substantially greater degree to cells of the homologous LPS type compared with the heterologous LPS type, indicating that the conserved sapA- and sapB-encoded N termini are critical for LPS binding specificity. The parallel genetic organization and identity at the nucleotide level in both coding and noncoding regions for sap homologs in types A and B cells indicates the necessity of both homolog conservation and high fidelity DNA replication in the biology of sap diversity.
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PMID:Segmental conservation of sapA sequences in type B Campylobacter fetus cells. 779 93

A region encoding ORFs with homology to known lipopolysaccharide (LPS) biosynthesis genes was isolated from two strains of Campylobacter jejuni. One of the strains produces LPS, but the second strain is reported to produce only lipooligosaccharide (LOS) and therefore lacks the O-chain. The two strains shared six predicted ORFs, but an additional ORF, orfE, of unknown function was identified in the LOS-producing strain. Mutation of the shared wbeE (rfbE) homologue (orfF) or deletion of five of the seven genes reduced core reactivity with specific antiserum without affecting O-chain production. Mutation of either the capD homologue (orfG) or the unique orfE had no detectable effect on LOS or LPS production. The presence or absence of orfE in 36 isolates of C. jejuni did not correlate with LOS/LPS phenotype or serotype. However, after insertion of orfE into a LPS-producing orfE-negative strain the O-chain ladder was no longer detectable on Western blots. We were not able to disrupt the wbaP (rfbP) homologue (orfC) in C jejuni.
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PMID:Cloning, mutation and distribution of a putative lipopolysaccharide biosynthesis locus in Campylobacter jejuni. 1007 20

The suppressor of cytokine signaling 3 (SOCS-3) is a member of a newly discovered protein family, which have been shown to regulate the responses of many immune cytokines, such as interferon (IFN), interleukin-2 (IL-2) and IL-6, etc., by inhibiting Janus kinase (JAK)-signal transducers and activators of transcription (STAT) signaling in a negative auto-regulatory manner. Although SOCS-3 was well characterized in several mammal species, there was still no report in fish. In present study, we initially identified and characterized the SOCS-3 genes from three fishes, the Tetraodon nigroviridis, the Danio rerio and the Fugu rubripes. The results showed that Tetraodon SOCS-3 gene located within a 2666 bp genomic fragment of chromosome 3, transcribed into a 1445 bp mRNA including 273 bp 5' UTR (untranslated region), 606 bp ORF (open reading frame) and 566 bp 3' UTR. Tetraodon SOCS-3 with 201aa (amino acid) has a calculated molecular mass of 22.76 kDa and a theoretical pI of 8.99. Danio SOCS-3 gene located within a 3617 bp genomic fragment of chromosome 3, transcribed into a 1927 bp mRNA including 178 bp 5' UTR, 624 bp ORF and 1125 bp 3' UTR. Danio SOCS-3 with 207aa has a calculated molecular mass of 23.68 kDa and a theoretical pI of 9.19. Fugu SOCS-3 gene located within a 2842 bp genomic fragment of Scaffold_1118, transcribed into a 1528 bp mRNA including 209 bp 5' UTR, 606 bp ORF and 713 bp 3' UTR. Fugu SOCS-3 with 201aa has a calculated molecular mass of 22.76 kDa and a theoretical pI of 8.18. The fish SOCS-3-encoding genes with the same organization as the mammalians consist of two exons and a single intron that lies in the 5' UTR of the transcript. The deduced amino acid sequences of the fish SOCS-3s showed: 60.7-61.7% sequence identity to mammalian SOCS-3s; 62.3-63.2% sequence identity to bird SOCS-3s; and 55.3-57.8% sequence identity to amphibian SOCS-3s. Phylogenetic analysis separates the fish SOCS-3s into an exclusive group. Expression study of Tetraodon SOCS-3 mRNA in ten selected tissues showed that it was constitutively expressed and induced by lipopolysaccharide (LPS) strikingly. These results indicated that SOCS-3s in fish may be involved in inflammatory responses. This is the first report of cloning and characterization of SOCS-3 cDNAs and genes in fish.
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PMID:Identification and characterization of suppressor of cytokine signaling 3 (SOCS-3) homologues in teleost fish. 1662 Sep 88

Macrophage migration inhibitory factor (MIF) is one of the first cytokines to be identified, which have been emerged to be an important mediator of the innate and adaptive immune system. Although MIF was well characterized in several mammal species, there was still little report in fish. In present study, we cloned the MIF gene from Tetraodon nigroviridis, and identified other six MIF genes from other teleost fishes, Fundulus heteroclitu, Oncorhynchus mykiss, Ictalurus punctatus, Danio rerio, Salmo salar and Haplochromis chilotes. The results showed that the fish MIF genes with the same organization as the mammalians consist of three exons and two introns. Tetraodon MIF gene located within a 1091bp genomic fragment of chromosome 1, transcribed into a 500bp mRNA including 14bp 5' untranslated region (UTR), 348bp ORF and 138bp 3'-UTR. Tetraodon MIF with 115aa has a calculated molecular mass of 12.5kDa and a theoretical pI of 6.81. The deduced amino-acid sequences of the teleost fish MIFs showed 64.1-73.5% sequence identity to mammalian MIFs, 61.5-70.1% to avian MIFs, 55.6-62.4% to amphibian MIFs, 74.4-97.4% among the teleost fishes. Phylogenetic analysis separates the teleost fish MIFs into an exclusive group. Genomic Southern blotting analyses suggest that Tetraodon has one copy of the MIF gene. RT-PCR and real-time PCR analyses reveal that Tetraodon MIF (TnMIF) mRNA was constitutively expressed in 10 selected tissues and induced by lipopolysaccharide (LPS) strikingly in head kidney and spleen. The bioactivity of recombinant TnMIF was tested by macrophage migration inhibition (MMI) assay. The result of MMI assay showed that the recombinant TnMIF inhibited the macrophage cells migration at rate of 35% (P<0.04). These results indicated that MIFs in fish may be involved in immune responses.
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PMID:Molecular cloning and identification of macrophage migration inhibitory factor (MIF) in teleost fish. 1744 92

An interleukin-7 (IL-7) gene has been cloned and sequenced within the Japanese pufferfish, Takifugu rubripes (Fugu), providing the first conclusive evidence for the existence of IL-7 in teleosts. The IL-7 cDNA was composed of 1438 bp, with a 117 bp 5'-UTR, an 826 bp 3'-UTR containing two mRNA instability motifs, and a 498 bp ORF which translates into a peptide of 166 amino acid residues. The Fugu IL-7 peptide contained a predicted signal peptide of 19 amino acid residues and the IL-7/9 family signature (Arg140-Val149). Homology analysis of Fugu IL-7 with other known IL-2 family members showed some similarity to the known mammalian IL-7 and Fugu IL-21 molecules, and phylogenetic tree analysis showed that the Fugu IL-7 clustered with the chicken and mammalian IL-7 and mammalian IL-9, away from other IL-2 family members (IL-2, IL-4, IL-15 and IL-21). The organization of the Fugu IL-7 gene was the same as in mouse, and consisted of five exons and four introns, but differed from the human gene, which is composed of six exons and five introns. Comparison of the Fugu and human genomes showed that some synteny existed around the IL-7 gene, with the presence of both the protein kinase inhibitor-alpha and chromosome 8 ORF 70 (C8orf70) genes, with IL-7 and C8orf70 having the same transcriptional orientation. The Fugu IL-7 gene was expressed within unstimulated tissues, such as the head kidney, spleen, liver, intestine, gill and muscle. Stimulation of head kidney cells with lipopolysaccharide, polyinosinic polycytidylic acid or phytohaemagglutinin increased this expression. This discovery of IL-7 in Fugu will allow a more complete analysis of fish immune responses in the future.
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PMID:Characterization and expression analysis of an interleukin-7 homologue in the Japanese pufferfish, Takifugu rubripes. 1826 67

The outer core region of Helicobacter pylori lipopolysaccharide of the majority of isolates contains an alpha-1,6-glucan polymer synthesized by the product of the HP0159 ORF. Structural studies carried out on HP0159 lipopolysaccharide mutants by a combination of chemical methods, mass spectrometry and nuclear magnetic resonance spectroscopy confirmed that insertional inactivation of HP0159 gene in H. pylori strains 26695 and SS1 resulted in formation of a truncated lipopolysaccharide molecule characterized by the presence of a terminal dd-heptose residue in the side-chain outer core fragment and maintaining an inner core backbone structure compared with the wild-type Lewis antigen-expressing strains. Colonization studies with HP0159 mutants of two mouse-colonizing strains, SS1 and M6, confirmed their inability to successfully colonize the murine stomach.
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PMID:Effect of the HP0159 ORF mutation on the lipopolysaccharide structure and colonizing ability of Helicobacter pylori. 1843 2

Rickettsia helvetica is an obligate intracellular Gram-negative microorganism found in Ixodes ricinus ticks. When R. helvetica was first discovered in 1979, little was known about its physiology and it fell into oblivion until it recently was suspected of being pathogenic to humans. However, all efforts to isolate R. helvetica from patients have been unsuccessful, although serological responses against R. helvetica can be demonstrated. The aim of our study was to investigate the protein profile of R. helvetica and study the antigenicity of its proteins using two-dimensional (2D) immunoblot in order to characterize the immunological response against R. helvetica infection. Our results show that in addition to the known PS120 and OmpB antigenic R. helvetica proteins, three other antigens exist: a 60 kDa GroEL protein, a 10 kDa GroES protein and a hitherto unknown 35 kDa hypothetical protein that has similarities with ORF-RC0799 of Rickettsia conorii. Furthermore, the lipopolysaccharide showed strong antigenicity. In this study, we present the first proteome map and the first 2D immunoblot profile of R. helvetica and finally we present the 35 kDa R. helvetica as an additional antigen to the previously known rickettsial antigens.
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PMID:A study of the antigenicity of Rickettsia helvetica proteins using two-dimensional gel electrophoresis. 1933 13

The present study was undertaken to investigate the possible role of a 10-kDa, secretory antigenic protein of Mtb (MTSA-10) in regulating macrophase response to lipopolysacchride (LPS). MTSA-10 inhibited the lipopolysaccharide (LPS)-induced oxidant species generation in the macrophage. Treatment of macrophages with MTSA-10 activated their protein tyrosine phosphatases (PTPs) in a redox-regulated fashion. These activated phosphatases then interfered with the early events of LPS signaling and lower the strength and magnitude of the signal generated, thereby preventing macrophages from making an effective immune response. Mycobacterium tuberculosis Region of Deletion-1 (RD-1)-specific secretory antigen MTSA-10 (encoded by ORF Rv3874 of Mtb genome) modulated the macrophage signaling machinery and prevented it from responding to further activation by LPS.
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PMID:Mycobacterium tuberculosis secreted antigen (MTSA-10) inhibits macrophage response to lipopolysaccharide by redox regulation of phosphatases. 1963 17


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