BookEva Böttcher-Friebertschäuser, Wolfgang Garten, Hans Dieter Klenk, editors.
Summary: This book will give an overview on viruses undergoing proteolytic activation through host proteases. The chapters will be organized in three themed parts, the first part describing respective viruses and their characteristics in detail. In the second part the molecular and cellular biology of the proteases involved as well as their physiological functions will be further explored. The third part will contain a chapter on protease inhibitors that are promising tools for antiviral therapy. This book will engage scholars in virology and medical microbiology as well as researchers with an interest in enzymology and protein structure and function relationship.
Contents:
Intro; Preface; Contents; Part I: Viral Proteins Activated By Host Proteases; 1: Activation of the Hemagglutinin of Influenza Viruses; 1.1 Structural Basis for Activation of HA Fusion Potential; 1.2 Structure of HA0 Cleavage Sites; 1.3 Activating Proteases; References; 2: Proteolytic Activation of Paramyxoviruses and Pneumoviruses; 2.1 Paramyxoviruses and Pneumoviruses; 2.2 The Role of Protease Cleavage in Fusion Protein Activation; 2.3 Proteases Involved in Paramyxovirus F Protein Proteolytic Cleavage; 2.3.1 Furin and Its Role in F Protein Cleavage. 2.3.2 Extracellular Cleavage of Paramyxovirus F Proteins with Monobasic Cleavage Sites2.3.3 The Henipavirus F proteins: Intracellular Cleavage by Endosomal Proteases; 2.4 Proteases Involved in Pneumovirus F Protein Proteolytic Cleavage; 2.4.1 Respiratory Syncytial Virus F Proteins: A Novel Case of Two Proteolytic Processing Events; 2.4.2 Extracellular Cleavage of F Proteins from the Metapneumoviruses; 2.5 F protein Proteolytic Processing, Pathogenesis, and Antiviral Approaches; 2.6 Proteolytic Activation of the Hemagglutinin-Neuraminidase Glycoprotein; References. 3.7.2 Peptide-Based Compounds and Small Molecules3.7.3 A Novel Cell-Based Sensor for SKI-1/S1P as a Platform for High-Throughput Drug Screening; 3.7.4 Use of the SKI-1/S1P Sensor to Predict Protease Use of Newly Emerging Arenaviruses; References; 4: Priming Time: How Cellular Proteases Arm Coronavirus Spike Proteins; 4.1 Introduction; 4.2 The Coronavirus Spike Protein: Viral Key for Entry into the Target Cell; 4.3 Proteolytic Priming of Coronavirus Spike Proteins: Basic Concepts; 4.4 Proteolytic Activation of the Spike Proteins of SARS-CoV and MERS-Co
V. 3: Cleavage of the Glycoprotein of Arenaviruses3.1 Arenavirus Structure, Genome Organization, and Basic Virology; 3.2 Arenavirus GP Structure and Function; 3.3 The Proprotein Convertase SKI-1/S1P Cleaves Arenavirus GPC; 3.4 The Mechanism of SKI-1/S1P Processing of Arenavirus GPC Differs from Cellular Substrates; 3.5 Optimized Recognition of Arenavirus GPC by SKI-1/S1P: Viral Advantage and Achilles' Heel; 3.6 The Processing of Reptarenavirus GPC Is Largely Unknown; 3.7 Targeting SKI-1/S1P-Mediated GPC Processing as an Anti-arenaviral Strategy; 3.7.1 Protein-Based Strategies. 4.4.1 Cathepsin L: Endosomal Activator of the Spike Protein4.4.2 Activation of the Spike Protein by Type II Transmembrane Serine Proteases at the Cell Surface; 4.4.3 Furin Can Activate Coronavirus Spike Proteins in the Constitutive Secretory Pathway of Infected Cells and During Viral Entry into Target Cells; References; 5: Proteolytic Processing of Filovirus Glycoproteins; 5.1 Introduction; 5.2 Biosynthesis and Maturation of Filovirus Glycoproteins; 5.3 The Role of GP in Host Cell Entry; 5.4 Proteases Responsible for GP Processing; References.