Analyses of monoclonal antibodies reacting with porcine wCD6: Results from the Second International Swine CD workshop

Among the 57 monoclonal antibodies analyzed within the T-cell group of the Second International Swine CD Workshop, one mAb fell within cluster T14a that included the CD6 standard a38b2 (No. 175). The new mAb MIL8 (No. 082) and a38b2 both precipitated from activated T-cells a 150 kDa monomeric protein. Staining patterns on the various cell types were similar. There was no inhibition of binding of either mAb to peripheral blood T-cells with the opposite mAb. The new mAb, MIL8, reacts with a separate epitope on porcine wCD6.     

Report on the analyses of mAb reactive with porcine CD8 for the second international swine CD workshop

Based on an analysis of their reactivity with porcine peripheral blood lymphocytes (PBL), only three of the 57 mAbs assigned to the T cell/activation marker group were grouped into cluster T9 along with the two wCD8 workshop standard mAbs 76-2-11 (CD8a) and 11/295/33 (CD8b). Their placement was verified through the use of two-color cytofluorometry which established that all three mAbs (STH101, #090; UCP1H12-2, #139; and PG164A, #051) bind exclusively to CD8⁺ cells. Moreover, like the CD8 standard mAbs, these three mAbs reacted with two proteins with a MW of 33 and 35 kDa from lymphocyte lysates and were, thus, given the wCD8 designation. Because the mAb STH101 inhibited the binding of mAb 76-2-11 but not of 11/295/33, it was given the wCD8a designation. The reactivity of the other two new mAbs in the T9 cluster with the various subsets of CD8⁺ lymphocytes were distinct from that of the other members in this cluster including the standards. Although the characteristic porcine CD8 staining pattern consisting of CD8^low and CD8^high cells was obtained with the mAb UCP1H12-2, a wider gap between the fluorescence intensity of the CD8^low and CD8^high lymphocytes was observed. In contrast, the mAb PG164A, not only exclusively reacted with CD4⁻/CD8^high lymphocytes, but it also failed to recognize CD4/CD8 double positive lymphocytes. It was concluded that this mAb is specific for a previously unrecognized CD8 epitope, and was, thus, given the wCD8c designation. A very similar reactivity pattern to that of PG164A was observed for two other mAbs (STH106, #094; and SwNL554.1, #009). Although these two mAbs were not originally positioned in the T cell subgroup because of their reactivity and their ability to inhibit the binding of PG164A, they were given the wCD8c designation. Overall, five new wCD8 mAbs were identified. Although the molecular basis for the differences in PBL recognition by these mAbs is not yet understood, they will be important in defining the role of CD8⁺ lymphocyte subsets in health and disease.     

Analyses of monoclonal antibodies reacting with porcine CD3: results from the Second International Swine CD Workshop

Among the 57 monoclonal antibodies (mAb) analyzed within the T-cell group from the Second Swine CD Workshop, six mAb fell within clusters T10 and T11 (No. 088, STH164; No. 148, FY1A3; No. 149, FY2C1; No. 150, FY1H2; No. 151, FY2A11; No. 169, BB23-8E6). The mAb within these two groups gave a similar appearance on flow cytometry and stained all peripheral blood T-cells as defined by CD4 and wCD8 staining. All six mAb precipitated a 24 kDa protein. On the basis of inhibition analyses performed as part of the workshop and from published data, the mAb define at least three epitopes. There is only minimal stimulation of resting peripheral lymphocytes, but four of the mAb produce strong stimulation in the presence of PMA. With the exception of STH164, all have been shown to react with CD3-transfected COS cells. The new mAb, therefore, react with three epitopes on porcine CD3 designated CD3a (BB23-8E6, FY2A11), CD3b (FY1A3, FY2C1), and CD3c (FY1H2). mAb STH164 appears to be reactive with another epitope, however, since its reactivity with CD3 has not been confirmed it is designated as wCD3.     

Direct mapping of nuclear shell effects in the heaviest elements

Quantum-mechanical shell effects are expected to strongly enhance nuclear binding on an "island of stability" of superheavy elements. The predicted center at proton number Z = 114, 120, or 126 and neutron number N = 184 has been substantiated by the recent synthesis of new elements up to Z = 118. However, the location of the center and the extension of the island of stability remain vague. High-precision mass spectrometry allows the direct measurement of nuclear binding energies and thus the determination of the strength of shell effects. Here, we present such measurements for nobelium and lawrencium isotopes, which also pin down the deformed shell gap at N = 152.     

Treatment of Cotton by β-Cyclodextrin/Triclosan Inclusion Complex and Factors Affecting Antimicrobial Properties

The efficacy of antimicrobial treatment of cotton fabrics depends on various parameters of the coating process, such as the chemical nature and concentration of the antimicrobial agent, the composition of the crosslinking formulation, and the curing temperature. The inclusion complex of triclosan with β-cyclodextrin (βCD) was synthesized and characterized by FTIR, XRD, NMR, Raman, SEM, and TGA. The minimum inhibitory concentration and minimum bactericidal concentration of the complex against Klebsiella pneumoniae and Staphylococcus aureus were compared to those of its precursor. A multifactorial study included an evaluation of the effects of triclosan complexation with β-cyclodextrin, a comparison between the glyoxal and tetracarboxylic acid as crosslinkers, an investigation of the effect of crosslinker and catalyst concentrations, and a comparison of curing at 120°C and 180°C. The cotton was characterized by FTIR-ATR, the micrographs of treated samples were obtained by SEM and the weight add-on was calculated. The bactericidal properties were determined according to AATCC-147. The correlation between the coating process parameters and the antimicrobial efficacy was determined. The optimal combination leading to the highest weight add-on and the antimicrobial coating that was most durable to multiple detergent washes at an elevated temperature was the use of complexed triclosan grafted onto the cotton in the presence of tetracarboxylic acid, followed by curing at 180°C. The curing temperatures were 120°C (P=0.002) and 180°C (P=0.008), catalysts were 1 % and 2 % aluminium sulfate and sodium hypophosphite (P<0.001), and the crosslinkers were 5 % and 10 % glyoxal and butanetetracarboxylic acid (P<0.001); these parameters significantly enhanced the antimicrobial properties of the treated fabrics. The study showed that βCD did not have antimicrobial activity, while the βCD/triclosan-treated textile exhibited potential antimicrobial properties. Overall, the bactericidal activity of fabrics can be enhanced by using βCD/triclosan with 10 % butanetetracarboxylic acid as a cross-linker and 5 % sodium hypophosphite as a catalyst at a curing temperature of 180°C.