Molecular Recognition in Host-Parasite Interactions (eBook, PDF)

Redaktion: Korhonen, Timo K.; Mäkelä, P. Helena; Hovi, Tapani

• Format: PDF

Produktbeschreibung

A very early step in microbial colonization and pathogenesis is that involving recog nition of the host by the microbe. In the final analysis such recognition is due to interaction between specific molecules on the two sides, without which host and microbe would ignore each other. It is therefore exciting to learn the rules that govern host-microbe interaction at to a large extent determines whether or not we are infected by the molecular level, which influenza virus, leishmanias, staphylococci and other pathogens. This book is a compendium of the addresses delivered at a symposium on molecular interaction at Porvoo, Finland in August 1991. Realizing that there are no a priori differ ences in receptor recognition in viruses, eukaryotic parasites and bacteria, we freely inter mingled these microbes at the symposium, and in this book. We found the interdisciplinary discussions and comparisons both educative and stimulating. Thus the book is divided into parts that focus on host cell receptors, on microbial recognition molecules and molecules that mediate microbial interaction with a host cell receptor and, briefly, on the molecular events that follow. Although many microbes and many cellular receptors are missing from the book -owing to the limited duration and size of the symposium -the articles presented here constitute an impressive body of examples of how initial host-microbe interaction can come about. We believe that as such the book is a useful and interesting overview of the mechanisms and principles involved in these interactions.

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Produktdetails

• Verlag: Springer US
• Seitenzahl: 230
• Erscheinungstermin: 6. Dezember 2012
• Englisch
• ISBN-13: 9781461530381
• Artikelnr.: 44325077

Inhaltsangabe

Microbial Components in Recognition.- Biology of Adhesins of Bordetella pertussis: Integrins, Selectins, and Mimicry of Leukocyte Adherence to Endothelia.- Structure-Function Relationships of the Reovirus Cell-Attachment Protein ?l.- Macrophage Receptors and Leishmania.- Streptococcal M Protein: A Common Structural Motif Used by Gram-positive Bacteria for Biologically Active Surface Molecules.- Properties and Synthesis of K88 Fimbriae.- Function and Organization of Escherichia coli Adhesins.- Fibronectin-Binding Proteins of Staphylococci and Streptococci.- S-Layers in Bacterial Pathogenesis: The Tetragonal Paracrystalline Surface Protein Array of Aeromonas salmonicida as a Special Example.- Streptococcal IgA Receptors.- Molecular Investigation of Escherichia coli Virulence in Extraintestinal infections.- Multifunctional Nature of Enterobacterial Fimbriae.- Host Components in Recognition.- Virus Interaction with Host Cell Receptors: Does gp120 of Human Immunodeficiency Virus Resemble an MHC Class II Alloepitope?.- Role of Cell Receptors for Poliovirus in Pathogenesis, Host Range and Virus Entry.- Membrane Proximity and Internal Binding in the Microbial Recognition of Host Cell Glycolipids: A Conceptual Discussion.- Bacterial Adherence and Host Tropism in Escherichia coli.- Role of Interactions Between Cytomegalovirus and ?2-Microglobulin in the Pathogenesis of Infection.- Complement Activation and Use of Complement Receptors for Cell Entry in Salmonellosis.- Binding and Activation of Plasminogen on the Surface of Staphylococcus aureus and Group A, C, and G Streptococci.- Escherichia coli S Fimbriae: Oligosaccharide-Specific Binding to Host Tissues and Enhancement of Plasminogen Activation.- Recognition Molecules on Red Cells for Malarial Parasites.- Host CellInvasion.- Inhibitory Action of Amantadine During Influenza Viral Entry: A Hypothesis.- Effect of Host Proteases on Early Steps of Enterovirus Infection.- Proteolytic Activation of Influenza Viruses: Substrates and Proteases.- Regulation of the Entry into Host Cytoplasm and Cell-to-Cell Spread of Listeria monocytogenes.- Protein Translocation from the Exterior to the Cytosol: Diphtheria Toxin as a Model System.