| 1. |
- Lloyd, Scott A, et al.
(author)
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Molecular characterization of type III secretion signals via analysis of synthetic N-terminal amino acid sequences
- 2002
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In: Molecular Microbiology. - : Wiley. - 0950-382X .- 1365-2958. ; 43:1, s. 51-9
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Journal article (peer-reviewed)abstract
- Yersinia species utilize a type III secretion system to inject toxins, called Yops (Yersinia outer proteins), into eukaryotic cells. The N-termini of the Yops serve as type III secretion signals, but they do not share a consensus sequence. To simplify the analysis of type III secretion signals, we replaced amino acids 2–8 of the secreted protein YopE with all permutations (27 or 128) of synthetic serine/isoleucine sequences. The results demonstrate that amphipathic N-terminal sequences, containing four or five serine residues, have a much greater probability than hydrophobic or hydrophilic sequences to target YopE for secretion. Multiple linear regression analysis of the synthetic sequences was used to obtain a model for N-terminal secretion signals. The model accurately classifies the N-terminal sequences of native type III substrates as efficient secretion signals.
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| 2. |
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| 3. |
- Nikolić, Dragan, et al.
(author)
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Dielectronic recombination resonances in Na8
- 2004
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In: Physical Review A. Atomic, Molecular, and Optical Physics. - : The American Physical Society. - 1050-2947 .- 1094-1622. ; 70:6
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Journal article (peer-reviewed)abstract
- The electron-ion recombination spectrum of the Li-like Na8+ ion in the energy range 0.0–0.5 eV is presented. Experimental results obtained by storage-ring techniques are compared with a calculated spectrum, based on a combination of relativistic many-body methods and complex rotation, and the agreement is found to be very good. The deviations between measured and calculated dielectronic recombination resonance energies are usually below about 2 meV with a maximum difference at 5.5 meV, while the theoretical cross sections deviate by at most 20% from the experiment. The recombination spectrum in the investigated energy region is determined by the 2pj7ℓj′ Rydberg manifold of dielectronic recombination resonances, comprising 61 states within half an eV above the ground state of Na8+. The theoretical resonance parameters of all contributing states are provided.
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| 4. |
- Pivarcsi, Andor, et al.
(author)
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CC chemokine ligand 18, an atopic dermatitis-associated and dendritic cell-derived chemokine, is regulated by staphylococcal products and allergen exposure.
- 2004
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In: Journal of Immunology. - : The American Association of Immunologists. - 0022-1767 .- 1550-6606. ; 173:9, s. 5810-7
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Journal article (peer-reviewed)abstract
- Atopic dermatitis is a chronic inflammatory skin disease with a steadily increasing prevalence. Exposure to allergens or bacterial superantigens triggers T and dendritic cell (DC) recruitment and induces atopic skin inflammation. In this study, we report that among all known chemokines CCL18/DC-CK1/PARC represents the most highly expressed ligand in atopic dermatitis. Moreover, CCL18 expression is associated with an atopic dermatitis phenotype when compared with other chronic inflammatory skin diseases. DCs either dispersed within the dermis or clustering at sites showing perivascular infiltrates are abundant sources of CCL18. In vitro, microbial products including LPS, peptidoglycan, and mannan, as well as the T cell-derived activation signal CD40L, induced CCL18 in monocytes. In contrast to monocytes, monocyte-derived, interstitial-type, and Langerhans-type DCs showed a constitutive and abundant expression of CCL18. In comparison to Langerhans cells, interstitial-type DCs produced higher constitutive levels of CCL18. In vivo, topical exposure to the relevant allergen or the superantigen staphylococcal enterotoxin B, resulted in a significant induction of CCL18 in atopic dermatitis patients. Furthermore, in nonatopic NiSO4-sensitized individuals, only relevant allergen but not irritant exposure resulted in the induction of CCL18. Taken together, findings of the present study demonstrate that CCL18 is associated with an atopy/allergy skin phenotype, and is expressed at the interface between the environment and the host by cells constantly screening foreign Ags. Its regulation by allergen exposure and microbial products suggests an important role for CCL18 in the initiation and amplification of atopic skin inflammation.
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