LEADER 04162nam 22005775 450 001 9910253959203321 005 20200630113557.0 010 $a3-319-58893-1 024 7 $a10.1007/978-3-319-58893-3 035 $a(CKB)4100000001381994 035 $a(DE-He213)978-3-319-58893-3 035 $a(MiAaPQ)EBC5178324 035 $a(PPN)222228113 035 $a(EXLCZ)994100000001381994 100 $a20171201d2017 u| 0 101 0 $aeng 135 $aurnn|008mamaa 181 $ctxt$2rdacontent 182 $cc$2rdamedia 183 $acr$2rdacarrier 200 10$aUptake and Trafficking of Protein Toxins /$fedited by Holger Barth 205 $a1st ed. 2017. 210 1$aCham :$cSpringer International Publishing :$cImprint: Springer,$d2017. 215 $a1 online resource (VII, 256 p.) 225 1 $aCurrent Topics in Microbiology and Immunology,$x0070-217X ;$v406 311 $a3-319-58891-5 320 $aIncludes bibliographical references at the end of each chapters. 327 $aTwo feet on the membrane: uptake of clostridial neurotoxins -- Receptors and binding structures for Clostridium difficile Toxins A and B -- Cell entry of C3 exoenzyme from Clostridium botulinum.- Receptor-binding and up-take of binary actin-ADP-ribosylating toxins -- Clostridial Binary Toxins: Basic Understandings that Include Cell-Surface Binding and an Internal ?Coup de Grace? -- Host cell chaperones Hsp70/Hsp90 and peptidyl-prolyl cis/trans isomerases are required for the membrane translocation of bacterial ADP-ribosylating toxins -- Multivalent Inhibitors of Channel-Forming Bacterial Toxins -- Toxin Transport by A-B Type of Toxins in Eukaryotic Target Cells and its inhibition by Positively Charged Heterocyclic Molecules. 330 $aThis volume focuses on the transport of medically relevant bacterial protein toxins into mammalian cells, and on novel pharmacological strategies to inhibit toxin uptake. The first chapters review our current understanding of the cell-surface receptors and cellular transport processes of Clostridium botulinum neurotoxins, Clostridium botulinum C3 toxin, Clostridium difficile toxins, binary clostridial enterotoxins, anthrax toxins and diphtheria toxin. In brief, specific binding/transport (B) subunits deliver the enzyme (A) subunits into the cytosol, where the latter modify their substrates, producing cytotoxic effects and the characteristic toxin-associated diseases. Key mechanisms for the transport of the A subunits from endosomes into the cytosol and the role of trans-membrane pores formed by the B subunits and host cell chaperones for this process are reviewed. The book?s closing chapters focus on compounds which inhibit the transport of the A subunits from endosomes into the cytosol and therefore might lead to novel therapeutic strategies for toxin-associated diseases. These substances include pharmacological inhibitors of the host cell chaperones involved, as well as multivalent and heterocyclic molecules that specifically block the toxins? translocation channels. This volume offers an up-to-date resource for scientists. 410 0$aCurrent Topics in Microbiology and Immunology,$x0070-217X ;$v406 606 $aMedical microbiology 606 $aPharmacology 606 $aInfectious diseases 606 $aMedical Microbiology$3https://scigraph.springernature.com/ontologies/product-market-codes/B16003 606 $aPharmacology/Toxicology$3https://scigraph.springernature.com/ontologies/product-market-codes/B21007 606 $aInfectious Diseases$3https://scigraph.springernature.com/ontologies/product-market-codes/H33096 615 0$aMedical microbiology. 615 0$aPharmacology. 615 0$aInfectious diseases. 615 14$aMedical Microbiology. 615 24$aPharmacology/Toxicology. 615 24$aInfectious Diseases. 676 $a615.95299 702 $aBarth$b Holger$4edt$4http://id.loc.gov/vocabulary/relators/edt 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bMiAaPQ 906 $aBOOK 912 $a9910253959203321 996 $aUptake and Trafficking of Protein Toxins$92262474 997 $aUNINA