1. |
|
|
2. |
|
|
3. |
- Griffiths, G, et al.
(författare)
-
Characterization of the glycosyltransferase enzyme from the Escherichia coli K5 capsule gene cluster and identification and characterization of the glucuronyl active site.
- 1998
-
Ingår i: Journal of Biological Chemistry. - 0021-9258 .- 1083-351X. ; 273:19, s. 11752-7
-
Tidskriftsartikel (refereegranskat)abstract
- Bacterial capsular polysaccharides play an important role in virulence and survival. The Escherichia coli K5 capsule consists of a repeat structure of -4)GlcA-beta(1,4)-GlcNAc alpha(1-, identical to N-acetylheparosan. A 60-kDa protein, KfiC, has been identified as a bifunctional glycosyltransferase, responsible for the alternating alpha and beta addition of each UDP-sugar to the nonreducing end of the polysaccharide chain. Using hydrophobic cluster analysis, a conserved secondary structure motif characteristic of beta-glycosyltransferases was identified along with two highly conserved aspartic acid residues at positions 301 and 352 within the KfiC protein. Site-directed mutagenesis was used to identify catalytically active amino acids within domain A of the KfiC protein. The conserved aspartic acid residues at 301 and 352 were shown to be critical for the beta addition of UDP-GlcA (uridine diphosphoglucuronic acid) to defined nonreducing end oligosaccharide acceptors, suggesting that these conserved aspartic acid residues are catalytically important for beta-glycosyltransferase activity. A deleted derivative of the kfiC gene was generated, which encoded for a truncated KfiC (kfiC') protein. This protein lacked 139 amino acids at the C terminus. This enzyme had no UDP-GlcA transferase activity but still retained UDP-GlcNAc transferase activity, indicating that two separate active sites are present within the KfiC protein.
|
|
4. |
|
|
5. |
|
|
6. |
|
|
7. |
- Varna, Janis, et al.
(författare)
-
Damage in composite laminates with off-axis plies
- 1999
-
Ingår i: Composites Science And Technology. - 0266-3538 .- 1879-1050. ; 59:14, s. 2139-2147
-
Tidskriftsartikel (refereegranskat)abstract
- Damage in off-axis plies of composite laminates is studied by examining the configuration [0/±θ4/01/2]s with θ=25, 40, 55, 70 and 90 subjected to tensile loading in the axial direction. It is found that for the values of θ, where the stress in the off-axis plies normal to the fibers is tensile, ply cracks lying along fibers initiate and increase in number, while for other θ values the plies do not undergo this damage, as expected. However, the overall laminate elastic moduli are also found to change for the θ values where no ply cracks exist. It is postulated that a shear-induced degradation of the off-axis plies is responsible for the observed laminate moduli changes. The prediction of changes in these moduli by using the ply shear modulus measured on [±θ4]s appears to support this postulate. For the case of moduli changes caused by ply cracks the recently proposed synergistic damage-mechanics approach [1] is applied. The implications of the findings of this work on a class of continuum damage-mechanics formulations proposed in the literature are discussed.
|
|
8. |
- Zabel, B A, et al.
(författare)
-
Human G protein-coupled receptor GPR-9-6/CC chemokine receptor 9 is selectively expressed on intestinal homing T lymphocytes, mucosal lymphocytes, and thymocytes and is required for thymus-expressed chemokine-mediated chemotaxis
- 1999
-
Ingår i: Journal of Experimental Medicine. - 1540-9538. ; 190:9, s. 1241-1256
-
Tidskriftsartikel (refereegranskat)abstract
- TECK (thymus-expressed chemokine), a recently described CC chemokine expressed in thymus and small intestine, was found to mediate chemotaxis of human G protein-coupled receptor GPR-9-6/L1.2 transfectants. This activity was blocked by anti-GPR-9-6 monoclonal antibody (mAb) 3C3. GPR-9-6 is expressed on a subset of memory alpha4beta7(high) intestinal trafficking CD4 and CD8 lymphocytes. In addition, all intestinal lamina propria and intraepithelial lymphocytes express GPR-9-6. In contrast, GPR-9-6 is not displayed on cutaneous lymphocyte antigen-positive (CLA(+)) memory CD4 and CD8 lymphocytes, which traffic to skin inflammatory sites, or on other systemic alpha4beta7(-)CLA(-) memory CD4/CD8 lymphocytes. The majority of thymocytes also express GPR-9-6, but natural killer cells, monocytes, eosinophils, basophils, and neutrophils are GPR-9-6 negative. Transcripts of GPR-9-6 and TECK are present in both small intestine and thymus. Importantly, the expression profile of GPR-9-6 correlates with migration to TECK of blood T lymphocytes and thymocytes. As migration of these cells is blocked by anti-GPR-9-6 mAb 3C3, we conclude that GPR-9-6 is the principal chemokine receptor for TECK. In agreement with the nomenclature rules for chemokine receptors, we propose the designation CCR-9 for GPR-9-6. The selective expression of TECK and GPR-9-6 in thymus and small intestine implies a dual role for GPR-9-6/CCR-9, both in T cell development and the mucosal immune response.
|
|