The collectin protein family and its multiple biological activities

The collectin protein family and its multiple biological activities / Uday Kishore, Taruna Madan, Robert B. Sim, editors.

The topic of this book, Collectins, is a family of proteins whose major function is in innate immunity, where Collectins act as pattern recognition receptors (PRRs). In general they recognize targets such as microbial surfaces and apoptotic cells, and once bound to a target, Collectins promote the c...

Full description

Saved in:
Bibliographic Details
Other Authors: Kishore, Uday (Editor), Madan, Taruna (Editor), Sim, Robert B. (Editor)
Format: eBook
Language:English
Published: Cham : Springer, [2021]
Subjects:
Collectins.
Natural immunity.
Collectins
Natural immunity
Electronic books.
Online Access:Click for online access
Table of Contents:
  • Intro
  • Foreword
  • Preface
  • Contents
  • About the Editors
  • Discovering the Role of Mannose-Binding Lectin (MBL) in Innate Immunity: The Early History
  • Introduction
  • Early Studies on Defective Opsonisation
  • A Question of Nomenclature
  • A Decade of Biochemical Studies
  • Microbiological Studies in the 1980s
  • Determination of the Underlying Cause of the Opsonic Deficiency
  • Some Concluding Thoughts
  • References
  • Mannose-Binding Lectin in Human Health and Disease
  • Introduction
  • MBL Structure
  • Various Functions of MBL
  • Binding of MBL with Ligands and Pathogens
  • Physiological Role of MBL
  • MBL-Associated Serine Proteases
  • Serum MBL Levels
  • MBL Genetics and Deficiency
  • Organization of the Human MBL2 Gene
  • Deficiency
  • MBL Associated with Diseases
  • MBL and Infection
  • Neonatal Sepsis
  • Autoimmune Diseases
  • MBL Replacement Therapy
  • Conclusions and Perspectives
  • References
  • Activities of MASPs, The Complement Proteases Associated with Collectins and Ficolins
  • Brief History
  • The Role of MASPs in Lectin Pathway Activation
  • Role of the MASPs in the Alternative Pathway Activation
  • Cross-Talk Between the Lectin Pathway and Coagulation
  • Endothelial Cell Activation by MASP-1
  • Regulation of MASPs
  • Conclusion and Perspectives
  • References
  • Structures of the MASP Proteases and Comparison with Complement C1r and C1s
  • Common Protease Modular Structure and Mode of Interaction with Defence Collagens
  • Central CUB1-EGF Interactions in LP and CP Proteases Assembly: A Marked Similarity
  • Similar Interaction Properties Mediate Protease Association with Defence Collagens
  • Opposite Binding Orientations for CUB1 and CUB2 Modules with Collagen: A Structural View
  • How Details of CUB-Collagen Interactions Explain the Differences in Orientation
  • CUB1-EGF-CUB2 Homodimer (LP) Versus Heterodimer (CP) Interactions: Common Features and Differences
  • How CCP1 and CCP2 Modulate LP and CP Catalytic Activities
  • CCP1-CCP2 as Elongated Arms or Handles
  • CCP1-CCP2 Include a C4 Binding Exosite in MASP-2 and C1s
  • CCP Modules Potentially Restricting Spontaneous Activation: A C1r Exception
  • Structural Similarities in the C-Terminal Trypsin-Like SP Domain
  • Structural Differences Shaping Protease Specificity, an Opportunity to Design Specific Inhibitors
  • Structural Uncertainties Beyond Common Principles in the LP and CP Activation Mechanism
  • LP and CP Protease Enzymatic Activities Out of the Complement System
  • General Comments and Conclusion
  • References
  • Biological Activities of SP-A and SP-D Against Extracellular and Intracellular Pathogens
  • Introduction
  • Protective Effects of SP-A and SP-D Against Viral Pathogens
  • Influenza A Virus
  • Human Immunodeficiency Virus-1 (HIV-1)
  • Herpes Simplex Viruses (HSV)
  • Respiratory Syncytial Virus (RSV)
  • Human Papillomavirus (HPV)
  • SARS Coronavirus (SARS CoV)
  • Other Viruses

Similar Items