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      • Record: found
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      BIS(4-FLUOROPHENYLSULFONYLDITHIOCARBIMATO)ZINCATE(II) SALTS: NEW ANTIFUNGALS FOR THE CONTROL OF <italic>Botrytis</italic> BLIGHT

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          Abstract

          <p>Botrytis blight or gray mold is a highly destructive disease caused by <italic>Botrytis</italic> spp., that infects flowers, trees vegetables, fruit, especially grapevines and strawberry. Three new compounds with general formula (A)<sub>2</sub>[Zn(4-FC<sub>6</sub>H<sub>4</sub>SO<sub>2</sub>N=CS<sub>2</sub>)<sub>2</sub>], where A = PPh<sub>3</sub>CH<sub>3</sub> (<bold>2a</bold>), PPh<sub>3</sub>C<sub>2</sub>H<sub>5</sub> (<bold>2b</bold>), PPh<sub>3</sub>C<sub>4</sub>H<sub>9</sub> (<bold>2c</bold>), and the previously published compounds where A = PPh<sub>4</sub> (<bold>2d</bold>) and NBu<sub>4</sub> (<bold>2e</bold>), were synthesized by the reaction of 4-fluorophenylsulfonyldithiocarbimate potassium dihydrate and zinc(II) acetate dihydrate with the appropriate counter cations (A) halides. The new compounds were characterized by infrared, <sup>1</sup>H and <sup>13</sup>C NMR spectroscopies. All these salts inhibited the growth of <italic>Botrytis cinerea</italic>, with compounds <bold>2c</bold> and <bold>2d</bold> showing greater antifungal activity than zinc dimethyldithiocarbamate, the active principle of the fungicide Ziram. The bis(dithiocarbimate)zincate(II) salts are also active against the bacteria <italic>Escherichia coli</italic> and <italic>Staphylococcus aureus</italic>.</p>

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          The heat-stable antigen determines pathogenicity of self-reactive T cells in experimental autoimmune encephalomyelitis.

          X Bai, Yong-feng Liu, Shi-Qi Liu … (2000)
          Induction of myelin-specific CD4 T cells is a pivotal event in the development of experimental autoimmune encephalomyelitis (EAE). Other checkpoints in EAE pathogenesis have not been clearly defined, although multiple genetic loci are known to influence EAE development. We report here that targeted mutation of the heat-stable antigen (HSA) abrogates development of EAE despite a complete lack of effect on induction of autoimmune T cells. To test whether T-cell expression of HSA is sufficient, we created transgenic mice in which HSA is expressed exclusively in the T-cell lineage. We found that these mice remain resistant to EAE induction. Adoptive transfer studies demonstrate that both T cells and non-T cells must express HSA in order for the pathogenic T cells to execute their effector function. Moreover, HSAIg, a fusion protein consisting of the extracellular domain of the HSA and the Fc portion of immunoglobulin, drastically ameliorates the clinical sign of EAE even when administrated after self-reactive T cells had been expanded. Thus, identification of HSA as a novel checkpoint, even after activation and expansion of self-reactive T cells, provides a novel approach for immunotherapy of autoimmune neurologic diseases, such as multiple sclerosis.
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            Inactivation of human factor VIII by activated protein C. Cofactor activity of protein S and protective effect of von Willebrand factor.

            Berto J. Bouma, J J Sixma, J Koedam … (1988)
            Activated protein C (APC) acts as a potent anticoagulant enzyme by inactivating Factor V and Factor VIII. In this study, protein S was shown to increase the inactivation of purified Factor VIII by APC ninefold. The reaction rate was saturated with respect to the concentration of protein S when protein S was present in a 10-fold molar excess over APC. The heavy chain of Factor VIII was cleaved by APC and protein S did not alter the degradation pattern. Factor VIII circulates in a complex with the adhesive protein von Willebrand factor. When purified Factor VIII was recombined with von Willebrand factor, the inactivation of Factor VIII by APC proceeded at a 10-20-fold slower rate as compared with Factor VIII in the absence of von Willebrand factor. Protein S had no effect on the inactivation of the Factor VIII-von Willebrand factor complex by APC. After treatment of this complex with thrombin, however, the actions of APC and protein S towards Factor VIII were completely restored. In hemophilia A plasma, purified Factor VIII associated with endogenous von Willebrand factor, resulting in a complete protection against APC (4 nM). By mixing hemophilic plasma with plasma from a patient with severe von Willebrand's disease, we could vary the amount of von Willebrand factor. 1 U of von Willebrand factor was needed to provide protection of 1 U Factor VIII. Also in plasma from patients with the IIA-type variant of von Willebrand's disease, Factor VIII was protected. In von Willebrand's disease plasma, which was depleted of protein S, APC did not inactivate Factor VIII. These results indicate that protein S serves as a cofactor in the inactivation of Factor VIII and Factor VIIIa by APC and that von Willebrand factor can regulate the action of these two anticoagulant proteins.
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              The agent of Human Granulocytic Ehrlichiosis resides in an endosomal compartment.

              Christopher P Webster, J IJdo, L Chicoine … (1998)
              The composition of cytoplasmic vacuoles containing the agent of Human Granulocytic Ehrlichiosis (HGE) was studied to investigate how this pathogen exists within infected host cells. Electron microscopy demonstrated that the HGE organism resides in a membrane-bound compartment within HL-60 cells: early forms of the HGE agent have a round reticular appearance while later structures are small and dense. Vacuoles containing HGE bacteria incorporated endocytosed colloidal gold particles, suggesting that they are part of the endocytic pathway. Antibodies directed to the mannose-6-phosphate receptor labeled vacuole membranes. Antibodies to the transferrin receptor and to the lysosomal membrane glycoprotein LAMP 1 did not. Moreover, 3-(2,4-dinitroanilino)-3'-amino-N-methyldipropylamine, which normally accumulates in compartments with low pH, was not present inside these vacuoles. These results suggest that vacuoles containing the agent of HGE fail to mature into phagolysosomes. We conclude that the agent of HGE appears to enter and modify part of the endocytic pathway.
              Article 0 comments Cited 46 times – based on 0 reviews     Review now
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                Author and article information

                Contributors
                Alexandre A. Oliveira: Role: ND
                Marcelo R. L. Oliveira: Role: ND
                Mayura M. M. Rubinger: Role: ND
                Elisa L. Piló: Role: ND
                Daniele C. Menezes: Role: ND
                Laércio Zambolim: Role: ND
                Journal
                Journal ID (publisher): qn
                Title: Química Nova
                Abbreviated Title: Quím. Nova
                Publisher: Sociedade Brasileira de Química (São Paulo )
                ISSN: 1678-7064
                Publication date (Print): July 2015
                Volume: 38
                Issue: 6
                Pages: 757-761
                Affiliations
                [1 ] Universidade Federal de Viçosa Brazil
                [2 ] Universidade Federal de Viçosa Brazil
                Article
                Publisher ID: S0100-40422015000600757
                DOI: 10.5935/0100-4042.20150075
                SO-VID: 3679f05c-5a92-4aca-83f7-26af372a5045
                License:

                http://creativecommons.org/licenses/by/4.0/

                History
                Product

                SciELO Brazil

                Self URI (journal page): http://www.scielo.br/scielo.php?script=sci_serial&pid=0100-4042&lng=en
                Categories
                Subject: CHEMISTRY, MULTIDISCIPLINARY

                ScienceOpen disciplines: General chemistry
                Keywords: dithiocarbimates,antimicrobial activity,<italic>Botrytis cinerea</italic>,<italic>Escherichia coli</italic>,<italic>Staphylococcus aureus</italic>
                Data availability:
                ScienceOpen disciplines: General chemistry
                Keywords: dithiocarbimates, antimicrobial activity, <italic>Botrytis cinerea</italic>, <italic>Escherichia coli</italic>, <italic>Staphylococcus aureus</italic>

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