Proteolytic Enzymes and their Inhibitors in Infectious Pathogens

Proteolytic Enzymes and their Inhibitors in Infectious Pathogens brings together key experts to provide a thorough discussion of proteolytic enzymes and their endogenous inhibitors found in parasites, bacteria and viruses. The book focuses on the respective roles of the different catalytic classes of proteolytic enzymes and their protein-protease inhibitors at the host-infectious organism interface and how this knowledge may inform drug and vaccine design. Following a foundational overview of proteases and macromolecular inhibitors of pathogenic organisms, the book discuss recent research on distinct classes of proteolytic enzymes in pathogens. Classes include aspartic proteases, cysteine proteases, metalloproteases, serine proteases, and threonine proteases with experts contributing chapters on distinct enzymes and inhibitors. New methods to identify protease substrates and inhibitors are also provided, with step-by-step protocols to advance new research and drive drug discovery. Discusses proteolytic enzymes of parasites, bacteria and viruses arranged by peptide bond cleavage classes for improved integration of information across the infectious organisms Includes information on the structure and interaction with proteases of macromolecular protease inhibitors and how these structures can be engineered to provide more potent and specific protease inhibitors Provides instructions in methods and technologies to identify physiological protease substrates, their cleavage specificities, and inhibitors Features rich illustrations and diagrams of core concepts, including informative three-dimensional protein structures and molecular interactions INDICE: Part 1: Introduction1. Overview of proteases of pathogenic organisms2. Introducing endogenous macromolecular protease inhibitors of pathogenic organismsPart 2: New methods to identify protease substrates and inhibitors3. DNA-linked inhibitor antibody assay (DIANA) to capture proteases in complex mixtures and identify novel small-molecule inhibitors 4. New advances in positional proteomics strategies to study protein processing5. Bioinformatics approaches for accurate prediction of protease-specific substrates and their cleavage sites6. Delineating peptidase specificities at the host-parasite interface using Multiplex Substrate Profiling by Mass Spectrometry (MSP-MS) 7. Recent Advances in Applications of Proteomic Approaches and Chemical Tools for Pathogen Profiling 8. Methods for mapping the mutational landscape of virus protease inhibitor binding sites to predict drug resistance Part 3: Aspartic proteases and their inhibitors9. Bacterial signal peptidases 10. Plasmepsins of the malaria parasite Plasmodium 11. Aspartic proteases of kinetoplasts12. HIV1 subtype C protease hinge region dynamics and flap flexibility in drug resistance13. Aspartic protease inhibitors of nematodesPart 4: Cysteine proteases and their inhibitors14. Polyprotein processing in SARS Cov-215. Gingipains of Porphyromonas gingivalis deactivators of innate immune and inflammatory defense mechanisms16. Sortases in pilus biogenesis of Gram-positive bacteria17. Cysteine proteases of protozoa18. Multifunctional Nidovirus papain-like proteases 19. Chagasins: Inhibitors of Cysteine Proteases in Protozoa20. Targeting the 3C-like proteases of Picornaviruses, Noroviruses, and CoronavirusesPart 5: Metalloproteases and their inhibitors21. The FusC about proteases involved in microbial iron piracy 22. Metallo-aminopeptidases in parasites and bacteriaPart 6: Serine proteases and their inhibitors23. Oligopeptidase B popping up in many pathogens as a virulence factor24. Ecotins of bacteria and protozoa25. Serpins of trematodes and nematodes26. Flaviviral serine NS2B-NS3 endoproteases Part 7: Threonine proteases 27. Proteasome in Plasmodium and kinetoplast parasites28. Proteasome in infectious organisms

• ISBN: 978-0-323-91801-5
• Editorial: Academic Press
• Encuadernacion: Rústica
• Páginas: 472
• Fecha Publicación: 01/05/2023
• Nº Volúmenes: 1
• Idioma: Inglés