Sequence and expression of a major egg antigen from Schistosoma mansoni. Homologies to heat shock proteins and alpha-crystallins

Nene, Vishvanath; Dunne, David W.; Johnson, Kevin S.; Taylor, David W.; Cordingley, John S.

doi:10.1016/0166-6851(86)90021-6

Cited by 109 publications

(68 citation statements)

References 12 publications

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“…To date, only a handful of ESP and SEA components have been characterized. One of the most abundant egg proteins comprising 10% of total SEA is Schistosoma mansoni 40 kDa protein (Sm-p40, [14]), a protein with homology to small heat shock proteins (HSPs) and α-crystallin [15]. By examining the ability of SEA fractions to stimulate proliferation of CD4 + Th cells isolated from S. mansoni infected mice, not only Sm-p40, but p150/166 (albumin), phosphoenolpyruvate carboxykinase, glutathione S-transferase (GST)-(28K), peroxiredoxin 1, and SmEP25 [16] proteins have been identified.…”

Section: Introductionmentioning

confidence: 99%

Proteomic analysis of Schistosoma mansoni egg secretions

Cass

Johnson

Califf

et al. 2007

Molecular and Biochemical Parasitology

194

196

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Schistosomiasis remains a largely neglected, global health problem. The morbid pathology of the disease stems from the host's inflammatory response to parasite eggs trapped in host tissues. Long term host/parasite survival is dependent upon the successful modulation of the acute pathological response, which is induced by egg antigens. In this study, using Multidimensional Protein Identification Technology, we identified the Schistosoma mansoni egg secretome consisting of 188 proteins. Notably we identified proteins involved in redox balance, molecular chaperoning and protein folding, development and signaling, scavenging and metabolic pathways, immune response modulation, and 32 novel, previously uncharacterized schistosome proteins. We localized a subset of previously-characterized schistosome proteins identified in egg secretions in this study, to the surface of live S. mansoni eggs using the circumoval precipitin reaction. The identification of proteins actively secreted by live schistosome eggs provides important new information for understanding immune modulation and the pathology of schistosomiasis.

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Section: Introductionmentioning

confidence: 99%

Proteomic analysis of Schistosoma mansoni egg secretions

Cass

Johnson

Califf

et al. 2007

Molecular and Biochemical Parasitology

194

196

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“…Among the invertebrates, an additional Schistosoma mansoni egg antigen sequence, p40-2 (Cao et al 1993), has 57% amino acid identity to the previously reported p40 antigen (Nene et al 1986), and likewise contains a duplicate "o~-crystallin domain." These stage-specific …”

Section: New Members Of the Familymentioning

confidence: 99%

“…Apart from the shsps and c~-crystallins, this family also includes more disparate members, like certain surface antigens in parasitic eukaryotes and bacteria ( Nene et al 1986;Nerland et al 1988;Verbon et al 1992). All members of the family are characterized by the presence of a homologous sequence of about 80 residues, which has been dubbed the "o~-crystallin domain" and probably forms a distinct structural and functional unit.…”

Section: Introductionmentioning

confidence: 99%

The expanding small heat-shock protein family, and structure predictions of the conserved “α-crystallin domain”

1995

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The expanding small heat-shock protein family, and structure predictions of the conserved .. crystallin domain Caspers, G.J.M.; Leunissen, J.A.M.; de Jong, W.W. Disclaimer/Complaints regulationsIf you believe that digital publication of certain material infringes any of your rights or (privacy) interests, please let the Library know, stating your reasons. In case of a legitimate complaint, the Library will make the material inaccessible and/or remove it from the website. Please Ask the Library: http://uba.uva.nl/en/contact, or a letter to: Library of the University of Amsterdam, Secretariat, Singel 425, 1012 WP Amsterdam, The Netherlands. You will be contacted as soon as possible. Abstract. The ever-increasing number of proteins identified as belonging to the family of small heat-shock proteins (shsps) and a-crystallins enables us to reassess the phylogeny of this ubiquitous protein family. While the prokaryotic and fungal representatives are not properly resolved, most of the plant and animal shsps and related proteins are clearly grouped in distinct clades, reflecting a history of repeated gene duplications. The members of the shsp family are characterized by the presence of a conserved homologous "cz-crystallin domain," which sometimes is present in duplicate. Predictions are made of secondary structure and solvent accessibility of this domain, which together with hydropathy profiles and intron positions support the presence of two similar hydrophobic a-sheet-rich motifs, connected by a hydrophilic co-helical region. Together with an overview of the newly characterized members of the shsp family, these data help to define this family as being involved as stable structural proteins and as molecular chaperones during normal development and induced under pathological and stressful conditions.

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“…aA-and aB-crystallin share approximately 55% sequence identity at the amino acid level (49), and mammalian ot-crystallin genes exhibit conservation at the level of gene structure (12,22,42,48). aA-and aB-crystallin are distantly related to an egg antigen of Schistosoma mansoni (35) and the small heat shock proteins of Drosophila melanogaster (19), and both the a-crystallins and small heat shock proteins are found associated with high-molecularweight aggregates and may be phosphorylated (30). The two a-crystallin genes presumably arose from a gene duplication event, originating from an ancestor of a small heat shock gene.…”

mentioning

confidence: 99%

Expression of the murine alpha B-crystallin gene in lens and skeletal muscle: identification of a muscle-preferred enhancer.

Dubin¹,

Gopal-Srivastava²,

Wawrousek³

et al. 1991

Mol. Cell. Biol.

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The aB-crystallin gene is expressed at high levels in lens and at lower levels in some other tissues, notably skeletal and cardiac muscle, kidney, lung, and brain. A promoter fragment of the murine aeB-crystallin gene extending from positions -661 to +44 and linked to the bacterial chloramphenicol acetyltransferase (CAT) gene showed preferential expression in lens and skeletal muscle in transgenic mice. Transfection experiments revealed that a region between positions -426 and -257 is absolutely required for expression in C2C12 and G8 myotubes, while sequences downstream from position -115 appear to be determinants for lens expression. In association with a heterologous promoter, a -427 to -259 fragment functions as a strong enhancer in C2C12 myotubes and less efficiently in myoblasts and lens. Gel shift and methylation interference studies demonstrated that nuclear proteins from C2C12 myoblasts and myotubes specifically bind to the enhancer.Crystallins comprise approximately 90% of the watersoluble proteins of the transparent eye lens and are important for its optical properties (52, 53). The three dominant classes of mammalian crystallins (a, P, and -y) contain two or more related polypeptides ranging in size from approximately 20 to 30 kDa and display regulated spatial and temporal expression within the lens (38, 52). Additional crystallins, the taxon-specific crystallins, exhibit a more restricted phylogenetic distribution; they are closely related or identical to common metabolic enzymes and are expressed at low concentrations outside the lens (11, 39).The two a-crystallin proteins, axA and aB, have been the subject of extensive structural, biophysical, and evolutionary studies. aA-and aB-crystallin share approximately 55% sequence identity at the amino acid level (49), and mammalian ot-crystallin genes exhibit conservation at the level of gene structure (12,22,42,48). aA-and aB-crystallin are distantly related to an egg antigen of Schistosoma mansoni (35) and the small heat shock proteins of Drosophila melanogaster (19), and both the a-crystallins and small heat shock proteins are found associated with high-molecularweight aggregates and may be phosphorylated (30). The two a-crystallin genes presumably arose from a gene duplication event, originating from an ancestor of a small heat shock gene.Despite these similarities, the two a-crystallin genes are expressed differently. The oxA-crystallin gene is expressed only in the lens (13,37,50). In contrast, the aB-crystallin gene, while expressed abundantly in lens, is also expressed at reduced levels in a variety of other tissues, including heart, skeletal muscle, kidney, lung, brain, retina, and iris (3,13,20,21). aB-crystallin expression has been associated with a variety of pathological and experimental conditions, notably Alexander's disease (21) and Lewy body disease (31) in humans, scrapie infection in hamsters (14) (50). Moreover, the murine aA-crystallin promoter contains an element between positions -66 to -57 which binds a zinc finger protein homologo...

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Sequence and expression of a major egg antigen from Schistosoma mansoni. Homologies to heat shock proteins and alpha-crystallins

Cited by 109 publications

References 12 publications

Proteomic analysis of Schistosoma mansoni egg secretions

Proteomic analysis of Schistosoma mansoni egg secretions

The expanding small heat-shock protein family, and structure predictions of the conserved “α-crystallin domain”

Expression of the murine alpha B-crystallin gene in lens and skeletal muscle: identification of a muscle-preferred enhancer.

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