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- Aspholm-Hurtig, Marina, et al.
(författare)
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Functional adaptation of BabA, the H. pylori ABO blood group antigen binding adhesin.
- 2004
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Ingår i: Science (New York, N.Y.). - : American Association for the Advancement of Science (AAAS). - 1095-9203 .- 0036-8075. ; 305:5683, s. 519-22
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Tidskriftsartikel (refereegranskat)abstract
- Adherence by Helicobacter pylori increases the risk of gastric disease. Here, we report that more than 95% of strains that bind fucosylated blood group antigen bind A, B, and O antigens (generalists), whereas 60% of adherent South American Amerindian strains bind blood group O antigens best (specialists). This specialization coincides with the unique predominance of blood group O in these Amerindians. Strains differed about 1500-fold in binding affinities, and diversifying selection was evident in babA sequences. We propose that cycles of selection for increased and decreased bacterial adherence contribute to babA diversity and that these cycles have led to gradual replacement of generalist binding by specialist binding in blood group O-dominant human populations.
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| 4. |
- Brunsell, Per, et al.
(författare)
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Feedback Stabilization of Multiple Resistive Wall Modes
- 2004
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Ingår i: Physical Review Letters. - 0031-9007 .- 1079-7114. ; 93:22, s. 225001-
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Tidskriftsartikel (refereegranskat)abstract
- Active feedback stabilization of multiple independent resistive wall modes is experimentally demonstrated in a reversed-field pinch plasma. A reproducible simultaneous suppression of several nonresonant resistive wall modes is achieved. Coupling of different modes due to the limited number of the feedback coils is observed in agreement with theory. The feedback stabilization of nonresonant RWMs also has an effect on tearing modes that are resonant in the central plasma, leading to a significant prolongation of the discharge pulse.
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| 5. |
- Cecconello, Marco, et al.
(författare)
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Current profile modification experiments in EXTRAP T2R
- 2004
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Ingår i: Plasma Physics and Controlled Fusion. - : IOP Publishing. - 0741-3335 .- 1361-6587. ; 46:1, s. 145-161
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Tidskriftsartikel (refereegranskat)abstract
- Pulsed poloidal current drive (PPCD) experiments have been conducted in the resistive shell EXTRAP T2R reversed-field pinch experiment. During the current profile modification phase, the fluctuation level of the m = 1 internally resonant tearing modes decreases, and the velocity of these modes increases. The m = 0 modes are not affected during PPCD, although termination occurs with a burst in the m = 0 amplitude. The PPCD phase is characterized by an increase in the central electron temperature (up to 380 eV) and in the soft x-ray signal. Spectroscopic observations confirm an increase in the central electron temperature. During PPCD, the plasma poloidal beta increases to 14%, and the estimated energy confinement time doubles, reaching 380 mus. The reduction in the fluctuation level and the corresponding increase in the energy confinement time are qualitatively consistent with a reduction in parallel transport along stochastic magnetic field lines.
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| 10. |
- Godl, Klaus, et al.
(författare)
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The N terminus of the MUC2 mucin forms trimers that are held together within a trypsin-resistant core fragment.
- 2002
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Ingår i: The Journal of biological chemistry. - 0021-9258 .- 1083-351X. ; 277:49, s. 47248-56
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Tidskriftsartikel (refereegranskat)abstract
- The N terminus of the human MUC2 mucin (amino acids 1-1397) has been expressed as a recombinant tagged protein in Chinese hamster ovary cells. The intracellular form was found to be an endoglycosidase H-sensitive monomer, whereas the secreted form was an oligomer that gave monomers upon disulfide bond reduction. The secreted MUC2 N terminus contained a trypsin-resistant core fragment. Edman sequencing and mass spectrometry of the peptides obtained localized this core fragment to the C-terminal end of the recombinant protein. This core retained its oligomeric nature with an apparent mass of approximately 240 kDa. Upon reduction, peptides of approximately 85 kDa were found, suggesting that the N terminus forms trimers. This interpretation was also supported by gel electrophoresis and gel filtration of the intact MUC2 N terminus. Electron microscopy revealed three globular domains each linked via an extended and flexible region to a central part in a trefoil-like manner. Immunostaining with gold-labeled antibodies localized the N-terminal end to the three globular structures, and the antibodies directed against the Myc and green fluorescent protein tags attached at the C terminus localized these to the stalk side of the central trefoil. The N terminus of the MUC2 mucin is thus assembled into trimers that contain proteolytically stable parts, suggesting that MUC2 can only be partly degraded by intestinal proteases and thus is able to maintain a mucin network protecting the intestine.
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