Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.5.1.52 (PNGase F)
 1,527 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Antigenic differences between European and American isolates of porcine reproductive and respiratory syndrome virus (PRRSV) were revealed by serologic analysis of a recombinant protein derived from PRRSV open reading frame 3 (ORF 3). The hydrophilic carboxyterminal 199 amino acids encoded by the ORF 3 of a European (Lelystad) isolate of PRRSV were expressed as a recombinant fusion protein (BP03-P) in a baculovirus gene expression system. Sera from gnotobiotic swine exposed to prototypic reference European and American isolates of PRRSV and sera from conventionally reared European and American swine convalescing from naturally acquired PRRSV infections were used to characterize the BP03-P protein. Sera from gnotobiotic and conventionally reared swine exposed to European isolates of PRRSV were significantly more reactive (P < 0.01) with BP03-P than were the corresponding American PRRSV antisera using the indirect immunoperoxidase monolayer assay (IPMA). Prototypic European, but not American, PRRSV antisera also recognized BP03-P using western immunoblotting and radioimmunoprecipitation assay (RIPA) procedures. However, gnotobiotically derived antiserum to an atypical American-origin PRRSV was reactive with BP03-P by both IPMA and western immunoblot. Despite a predicted potential for N-linked glycosylation, studies with tunicamycin and peptide-N-glycosidase F (PNGase F) indicated that BP03-P was not N-glycosylated in either insect cell cultures or Trichoplusia ni larvae infected with the recombinant baculovirus. Sera from rabbits inoculated with BP03-P failed to neutralize both the European (Lelystad) and American (ATCC VR-2332) reference isolates of PRRSV and did not react by IPMA with PRRSV-infected cell cultures. Taken together, the data suggest that the carboxyterminal portion of PRRSV ORF 3 encodes a non-neutralizing viral peptide that is partially responsible for the serologic differences noted between European and most American isolates of PRRSV.
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PMID:Antigenic differences between European and American isolates of porcine reproductive and respiratory syndrome virus (PRRSV) are encoded by the carboxyterminal portion of viral open reading frame 3. 766 7

The PAG family is encoded by distinct genes expressed in extra-embryonic chorionic membranes (TR--trophoblast, TRD--trophectoderm) of various pregnant mammals. The objective of our study was to determine N-glycodiversity of porcine PAG protein family (pPAG) produced in vitro by TR or TRD explants of gilts (n=26) throughout pregnancy (16-77 dpc). Explants were cultured for over 1200 h (TR, 16 dpc) or for 8 h (TRD, 17-77 dpc). Released proteins were isolated from media by separating ultra-filtration (>10 kDa). A deglycosylation (removal of N-linked carbohydrate side chains) of proteins was performed by glycopeptidase F, and compared to non-deglycosylated forms by PAGE-Western blotting with anti-pPAG sera and additionally to polypeptide pPAG precursors, coded by ORF of their cloned cDNAs. We demonstrated gestation-stage dependent diversity of deglycosylated/glycosylated forms of the pPAG proteins produced in vitro in the pig. TR explants harvested on 16 dpc during long term culture released 43 kDa pPAG proteins. These proteins were deglycosylated to approximately 36.9 and approximately 39.6 kDa (16 dpc). Tissue harvested on 17 dpc in vitro secreted 65-68 kDa pPAG proteins which were reduced to three forms, 50.6, 58.7 and 63.5 kDa. In addition, approximately 73.3 kDa major pPAG proteins (77 dpc) were reduced to at least three forms: approximately 39.6, approximately 36.9 and approximately 33.4 kDa. Such N-deglycosylation was not detected on days 25-61. N-deglycosylation of native pPAG proteins clearly corresponded to three N-glycosylation sites of asparagines (N-x-S/T) found in ORF of the pPAG2-like precursors, identified by their in silico translated cDNAs. Thus, the pregnancy-stage dependent N-glycodiversity of the pPAG protein family, containing an average 9.66% of N-linked oligosaccharides, may play some role(s) in porcine conceptus attachment, successful implantation and during advanced pregnancy.
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PMID:N-glycodiversity of the Pregnancy-Associated Glycoprotein family (PAG) produced in vitro by trophoblast and trophectoderm explants during implantation, placentation and advanced pregnancy in the pig. 1509 96

Peptide: N-glycanase (PNGase) enzyme is found throughout eukaryotes and plays an important role in the misfolded glycoprotein degradation pathway. This communication reports the expression patterns of the pngase transcript (as studied by the analysis of beta-galactosidase reporter driven by the putative pngase promoter) and protein (as studied by the analysis of beta-galactosidase reporter expressed under the putative pngase promoter as a fusion with the pngase ORF) during development and further elucidated the developmental defects of the cells lacking PNGase (png(-)). The results show that the DdPNGase is an essential protein expressed throughout development and beta-galactosidase activity was present in the anterior part of the slug. In structures derived from a null mutant for pngase, the prestalk A and AO patterning was expanded and covered a large section of the prespore region of the slugs. When developed as chimeras with wild type, the png(-) cells preferentially populate the prestalk/stalk region. When the mutants were mixed in higher ratios, they also tend to form the prespore/spore cells. The results emphasize that the DdPNGase has an essential role during development and the mutants have defects in a system that changes the physiological dynamics in the prespore cells. DdPNGase play a role in development both during aggregation and in the differentiation of prespore cells.
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PMID:Peptide: N- glycanase is expressed in prestalk cells and plays a role in the differentiation of prespore cells during development of Dictyostelium discoideum. 2466 62