Cloning of the gene for phosphoglycerate kinase from Schistosoma mansoni and characterization of its gene product

Lee, Keung W.; Shalaby, Kamal A.; Thakur, Aditya; Medhat, Amina M.; Karim, Amr M.; LoVerde, Philip T.

doi:10.1016/0166-6851(95)91598-o

Cited by 38 publications

(28 citation statements)

References 42 publications

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“…It is unclear how proteins that are expected to be cytosolic, such as Sm15 (Abath et al 1993(Abath et al , 1994, glutathione S-transferase (GST; Balloul et al 1987), triose-phosphate isomerase (TPI; Harn et al 1992), glyceraldehyde-3-phosphate dehydrogenase (GAPDH; Goudot-Crozel et al 1989) and phosphoglycerate kinase Lee et al 1995), could be attached to the schistosome surface, since none has a conventional transmembrane domain and there is no evidence of a lipid anchor (Abath and Werkhauser 1996). The function of Sm13 in the context of the biology of the parasite is not clear.…”

Section: Discussionmentioning

confidence: 99%

Characterization of Sm13, a tegumental antigen of Schistosoma mansoni

Abath¹,

Xavier²,

Allen³

et al. 2000

Parasitol Res

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Sm13, a 13-kDa Schistosoma mansoni tegumental antigen, is one of the principal polypeptides recognized by antibodies from mice protectively vaccinated with adult-worm tegumental membranes. To obtain the complete gene encoding Sm13 we subcloned and sequenced a cDNA and a fragment of a genomic clone. The collated sequence contains 1,088 nucleotides and represents the full-length open reading frame of the gene, encoding a protein of 104 amino acids with a calculated molecular mass of 11,923 Da, compatible with the native protein identified in the tegumental membranes. The sequence derived from genomic DNA contains a 45-nucleotide intron. The analysis of the predicted protein suggests the presence of both N- and C-terminal hydrophobic membrane-spanning segments, and the coding region contains no homology in the currently available data bases. Additionally, the coding region is preceded by putative CCAAT and TATA boxes that may be involved in the control of expression. Western-blot analysis and indirect immunofluorescence resulted in the identification of a 13-kDa protein (Sm13) in the tegument of adult worms. The present study reveals that Sm13 behaves as an integral membrane protein upon partitioning in Triton X-1 14 and that it is present in worms of 3 weeks or older but not in schistosomula or miracidia. Moreover, it is also specifically recognized by sera from some schistosomiasis patients in enzyme-linked immunosorbent assay and Western-blot analysis, suggesting that it is immunogenic in human schistosomiasis.

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Section: Discussionmentioning

confidence: 99%

Characterization of Sm13, a tegumental antigen of Schistosoma mansoni

Abath¹,

Xavier²,

Allen³

et al. 2000

Parasitol Res

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“…Schistosomes are anaerobic parasitic helminths that utilize glucose as their main energy source. They consume glucose every hour at the equivalent of 26% of their dry body weight (Lee et al 1995). C. sinensis absorbs glucose from its environment (Seo and Lee 1971) and utilizes it for energy production through the glycolytic pathway (Kang et al 1969).…”

Section: Introductionmentioning

confidence: 99%

Ultrastructural localization of phosphoglycerate kinase in adult Clonorchis sinensis

Hong

Shin

Kang

et al. 2003

Parasitology Research

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Phosphoglycerate kinase (PGK) is an enzyme that produces one ATP molecule in the glycolytic pathway. Clonorchis sinensis is largely dependent on glycolysis for energy production. We performed immunoelectron microscopy on adult C. sinensis by using mouse immune serum raised against recombinant C. sinensis PGK. A high density of gold particles was found in the microvilli of the intestinal epithelium and in lamellae of the sperm duct. PGK was common in the somatic cells of intra-uterine eggs and in excreted products. It was localized with moderate intensity in muscular fibers of the subtegumental muscle layer, and in the myoepithelia of the intestine and excretory bladder. We suggest that PGK plays an essential role in C. sinensis energy production for movement via muscle contraction.

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“…During Streptococcus pyogenes infection GAPDH acts as an adhesion molecule and helps escape detection by neutrophils (31). Alcohol dehydrogenase was also detected on the surface of Entamoeba histolytica (32), and phosphoglycerate kinase, triose-phosphate isomerase, and GAPDH have been found on the surface of Schistosoma mansoni (33)(34)(35).…”

mentioning

confidence: 97%

The Crystal and Solution Structures of Glyceraldehyde-3-phosphate Dehydrogenase Reveal Different Quaternary Structures

Ferreira-da-Silva

Pereira

Gales

et al. 2006

Journal of Biological Chemistry

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The presence of an isoform of glyceraldehyde-3-phosphate dehydrogenase (kmGAPDH1p) associated with the cell wall of a flocculent strain of Kluyveromyces marxianus was the first report of a non-cytosolic localization of a glycolytic enzyme, but the mechanism by which the protein is transported to the cell surface is not known. To identify structural features that could account for the multiple localizations of the protein, the threedimensional structure of kmGAPDH1p was determined by x-ray crystallography and small angle x-ray scattering. The x-ray crystallographic structure of kmGAPDH1p revealed a dimer, although all GAPDH homologs studied thus far have a tetrameric structure with 222 symmetry. Interestingly, the structure of kmGAPDH1p in solution revealed a tetramer with a 70°t ilt angle between the dimers. Moreover, the separation between the centers of the dimers composing the kmGAPDH1p tetramer diminished from 34 to 30 Å upon NAD ؉ binding, this latter value being similar to the observed in the crystallographic models of GAPDH homologs. The less compact structure of apokmGAPDH1p could already be the first image of the transition intermediate between the tetramer observed in solution and the dimeric form found in the crystal structure, which we postulate to exist in vivo because of the protein's multiple subcellular localizations in this yeast species.The reversible oxidation of D-glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate with the concomitant reduction of NAD ϩ to NADH is a key step in glycolysis and gluconeogenesis catalyzed by the NAD ϩ -dependent D-glyceraldehyde-3-phos-

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Cloning of the gene for phosphoglycerate kinase from Schistosoma mansoni and characterization of its gene product

Cited by 38 publications

References 42 publications

Characterization of Sm13, a tegumental antigen of Schistosoma mansoni

Characterization of Sm13, a tegumental antigen of Schistosoma mansoni

Ultrastructural localization of phosphoglycerate kinase in adult Clonorchis sinensis

The Crystal and Solution Structures of Glyceraldehyde-3-phosphate Dehydrogenase Reveal Different Quaternary Structures

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