Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.11.8 (FAST)
 758 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Cysticercosis, a disease caused by the larval form of Taenia solium, is diagnosed by detection of specific antibodies or by imaging techniques. Our preferred immunologic assay for cysticercosis is the enzyme-linked immunoelectrodifusion transfer blot, or immunoblot, using the lentil lectin bound antigens from larval cysts. Antibody reactivity with any one of seven glycoproteins is diagnostic for cysticercosis. To develop a simple antibody detection assay for field use, we have synthesized an 8-kD diagnostic antigen, sTs18var1 (a secreted protein with a mature size of 67 amino acids), and expressed a 50-kD membrane protein antigen, rGp50. We used these two diagnostic proteins in a quantitative Falcon assay screening test-enzyme-linked immunosorbent assay (FAST-ELISA) to measure the antibody responses in Peruvian pigs with cysticercosis. Three study designs were used. First, we followed the kinetics of antibody responses against these two diagnostic proteins in pigs with cysticercosis that were treated with oxfendazole. Second, we measured antibody response in naive experimentally infected pigs. Third, we followed the maternal antibodies against rGp50 and sTs18var1 in piglets born from sows with cysticercosis. These studies showed that antibody responses against the two diagnostic proteins in the FAST-ELISA are quantitatively correlated with infection by viable cysts, with anti-sTs18var1 activity being most responsive to the status of infection.
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PMID:Porcine antibody responses to taenia solium antigens rGp50 and sTs18var1. 1538 14

The FAST proteins are a unique family of virus-encoded cell-cell membrane fusion proteins. In the absence of a cleavable N-terminal signal peptide, a single-pass transmembrane domain (TMD) functions as a reverse signal-anchor to direct the FAST proteins into the plasma membrane in an N(exo)/C(cyt) topology. There is little information available on the role of the FAST protein TMD in the cell-cell membrane fusion reaction. We show that in the absence of conservation in the length or primary amino acid sequence, the p14 TMD can be functionally exchanged with the TMDs of the p10 and p15 FAST proteins. This is not the case for chimeric p14 proteins containing the TMDs of two different enveloped viral fusion proteins or a cellular membrane protein; such chimeric proteins were defective for both pore formation and syncytiogenesis. TMD structural features that are conserved within members of the FAST protein family presumably play direct roles in the fusion reaction. Molecular modeling suggests that the funnel-shaped architecture of the FAST protein TMDs may represent such a conserved structural and functional motif. Interestingly, although heterologous TMDs exert diverse influences on the trafficking of the p14 FAST protein, these TMDs are capable of functioning as reverse signal-anchor sequences to direct p14 into lipid rafts in the correct membrane topology. The FAST protein TMDs are therefore not primary determinants of type III protein topology, but they do play a direct, sequence-independent role in the membrane fusion reaction.
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PMID:Reovirus FAST protein transmembrane domains function in a modular, primary sequence-independent manner to mediate cell-cell membrane fusion. 1912 51

The creation of transgenic plants has contributed extensively to the advancement of plant science. Establishing homozygous transgenic lines is time-consuming and laborious, and using antibiotics or herbicides to select transformed plants may adversely affect the growth of some transgenic plants. Here we describe a novel technology, which we have named FAST (fluorescence-accumulating seed technology), that overcomes these difficulties. Although this technology was designed for use in Arabidopsis thaliana, it may be adapted for use in other plants. The technology is based on the expression of a fluorescent co-dominant screenable marker FAST, under the control of a seed-specific promoter, on the oil body membrane. The FAST marker harbors a fusion gene encoding either GFP or RFP with an oil body membrane protein that is prominent in seeds. The marker protein was only expressed in a specific organ (i.e. in dry seeds) and at a specific time (i.e. during dormancy), which are desirable features of selectable and/or screenable markers. This technique provides an immediate and non-destructive method for identifying transformed dry seeds. It identified the heterozygous transformed seeds among the T(1) population and the homozygous seeds among the T(2) population with a false-discovery rate of <1%. The FAST marker reduces the length of time required to produce homozygous transgenic lines from 7.5 to 4 months. Furthermore, it does not require sterilization, clean-bench protocols or the handling of large numbers of plants. This technology should greatly facilitate the generation of transgenic Arabidopsis plants.
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PMID:A rapid and non-destructive screenable marker, FAST, for identifying transformed seeds of Arabidopsis thaliana. 1989 5