Schistosoma mansoni: Identification and analysis of an mRNA and a gene encoding superoxide dismutase ()

Simurda, Maryanne C.; Keulen, Harry van; Rekosh, David; LoVerde, Philip T.

doi:10.1016/0014-4894(88)90010-0

Cited by 67 publications

(33 citation statements)

References 22 publications

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“…Preliminary results with SodC-p-lactamase gene fusions (8), which confer ampicillin resistance only if their product is exported beyond the cytoplasm, support this proposition in both E. coli and H. parainfluenzae (24). Extracellular SODs have been described before in both eukaryotes and prokaryotes (3,22,42) and may play a protective role against toxic oxygen species released by macrophages during the respiratory burst. Beaman and Beaman (4) have suggested that Nocardia asteroides gains pathogenic potential through a capacity to neutralize superoxide within macrophages by excreting a manganese-containing SOD.…”

Section: Atcctgtttagcgccacgticttaaaaaattagatgaagttcctggtcattctattatgmentioning

confidence: 71%

Copper-zinc superoxide dismutase of Haemophilus influenzae and H. parainfluenzae

1991

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Copper-zinc superoxide dismutase ([Cu,Zn]-SOD) is widely found in eukaryotes but has only rarely been identified in bacteria. Here we describe sodC, encoding [Cu,Zn]-SOD in Haemophilus influenzae and H. parainfluenzae, frequent colonists and pathogens of the human respiratory tract. In capsulate H. influenzae, sodC was found in only one division of the bacterial population, and although the protein it encoded was clearly [Cu,Zn]-SOD from its deduced sequence, it lacked enzymatic activity. In H. parainfluenzae, in contrast, active enzyme was synthesized which appeared to be secreted beyond the cytoplasm when the gene was expressed in Escherichia coli minicells. The origin of gene transcription differed between the Haemophilus species, but protein synthesis from cloned genes in vitro was comparable. A C-T transition was found in the H. influenzae sequence compared with the H. parainfluenzae sequence, leading to a histidine, known to be crucial in eukaryotic [Cu,Zn]-SOD for copper ion coordination and so for enzymatic activity, to be changed to tyrosine. This is speculated to be the cause of inactivity of the H. influenzae enzyme. Secreted SODs have only been described in a few bacterial species, and this is the first identification of [Cu,Zn]-SOD in a common human upper respiratory tract colonist. The role of secreted bacterial SODs is unknown, and we speculate that in Haemophilus species the enzyme may confer survival advantage by accelerating dismutation of superoxide of environmental origin to hydrogen peroxide, disruptive to the normal mucociliary clearance process in the host.

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Section: Atcctgtttagcgccacgticttaaaaaattagatgaagttcctggtcattctattatgmentioning

confidence: 71%

Copper-zinc superoxide dismutase of Haemophilus influenzae and H. parainfluenzae

1991

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“…Schistosome EC-SOD contains a signal peptide sequence, but does not appear to be localized extracellularly in S. mansoni [10,13]. Far higher levels of S. mansoni EC-SOD transcripts are found in adult females than in adult males [16].…”

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confidence: 95%

“…One of these, Tag ID #10395, maps to the sequence for extracellular superoxide dismutase (EC-SOD; Sm00301) [13], which showed a 1.2-fold increase in the SNP-treated library as compared to the control library, with an R value of 0.56. SOD is potentially an interesting gene for further study, as NO is known to interact with reactive oxygen intermediates such as superoxide [14,15].…”

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confidence: 99%

Nitric oxide-dependent changes in Schistosoma mansoni gene expression

Messerli

Morgan²,

Birkeland³

et al. 2006

Molecular and Biochemical Parasitology

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Keywords Schistosoma mansoni; Nitric oxide (NO); Serial analysis of gene expression (SAGE); Extracellular superoxide dismutase (EC-SOD)Nitric oxide (NO)-related pathways potentially play at least two critical roles in schistosomes, the causative agents of schistosomiasis. First, these pathways may represent essential signaling cascades required for normal parasite physiology and survival. Second, NO-related pathways may also play an important role in parasite-host interactions. Several reports have demonstrated that platyhelminths have nitric oxide synthase (NOS) activity and that NO is likely acting as a signaling molecule in these organisms [1][2][3][4]. Furthermore, the host NO pathway may be involved in host defense against schistosome infection, though its precise role in vivo is not clear [5][6][7].Here we examine changes in parasite gene expression in response to exposure to exogenous NO in vitro. Prior studies have provided evidence of NO-related pathways in adult schistosomes [1,2,8]. However, the physiological role and downstream targets of NO have not been elucidated in adult worms. To assay NO-dependent changes in gene expression, we have used Long-SAGE (serial analysis of gene expression) [9], which provides both the identity of expressed genes and the relative levels of their expression.In Long-SAGE, a short 21 bp sequence tag from the most polyA proximal NlaIII restriction site of an mRNA molecule is used to uniquely identify the source gene from within the genome. Short sequence tags are sampled from all NlaIII-positive transcripts in a mRNA sample and are linked together to form long concatenated molecules that are cloned and sequenced. Quantification of all tags provides a relative measure of gene expression (i.e., mRNA abundance). Using SAGE, we have identified genes which respond to NO by changing expression levels, and we also show by RT-PCR that RNA encoding extracellular superoxide dismutase (EC-SOD, also referred to as signal peptide-SOD [10][11] Publisher's Disclaimer:This article was originally published in a journal published by Elsevier, and the attached copy is provided by Elsevier for the author's benefit and for the benefit of the author's institution, for non-commercial research and educational use including without limitation use in instruction at your institution, sending it to specific colleagues that you know, and providing a copy to your institution's administrator. All other uses, reproduction and distribution, including without limitation commercial reprints, selling or licensing copies or access, or posting on open internet sites, your personal or institution's website or repository, are prohibited. For exceptions, permission may be sought for such use through Elsevier's permissions site at: http://www.elsevier.com/ locate/permissionusematerial NIH Public Access After correcting for sequencing error, we sampled 26,072 SAGE tags for the control library and 26,815 tags for the SNP-exposed library. We used log-likelihood statistics (R > 1.5) to reduce the effects of sampling...

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“…The other subfamily comprises Cu,Zn-SOD (SODC), which occurs primarily in the cytosol of eukaryotic cells and in plant chloroplasts. An extracellular form of Cu,Zn-SOD (EC SOD) has been identified in mammalian fluids (Marklund, 1984), some parasites (Simurda et al, 1988;Tang et al, 1994;Liddell and Knox, 1998) and, recently, attached to cell surface of crayfish and blue crab haemocytes (Holmblad and Soderhall, 1999;Johansson et al, 1999;Brouwer and Brouwer, 2000). Both types of Cu,Zn-SODs are believed to have evolved from a common ancestor, which is different from that of Mn-and Fe-SODs (Fridovich, 1989;Matsumoto et al, 1991).…”

Section: Introductionmentioning

confidence: 99%

Cu,Zn superoxide dismutase in Rhodotorula and Udeniomyces spp. isolated from sea water: cloning and sequencing the encoding region

Hernández-Saavedra

2003

Yeast

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The gene encoding the copper-zinc superoxide dismutase enzyme (SODC or Cu,Zn-SOD) has been cloned from several species of higher eukaryotes, but superoxide dismutase genes from moulds and yeast have not been studied extensively. For U. puniceus, the cloned nucleotide sequence contains all necessary information to produce a functional protein, which correlates with activity detected in cell homogenates, both under normal conditions and by copper induction experiments. Finally, we clearly showed that the key factor in protection against oxidative stress on pigmented yeast is related not only to the presence of protective pigments but also to their amounts and spectra, as well as the presence and activity of SODC. The sod1 sequences reported in this paper have been deposited in the NCBI public data library under Accession Nos AY064723, AY064724 and AF301901.

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Schistosoma mansoni: Identification and analysis of an mRNA and a gene encoding superoxide dismutase ()

Cited by 67 publications

References 22 publications

Copper-zinc superoxide dismutase of Haemophilus influenzae and H. parainfluenzae

Copper-zinc superoxide dismutase of Haemophilus influenzae and H. parainfluenzae

Nitric oxide-dependent changes in Schistosoma mansoni gene expression

Cu,Zn superoxide dismutase in Rhodotorula and Udeniomyces spp. isolated from sea water: cloning and sequencing the encoding region

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