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Full Description
This book presents an unprecedented exploration of the protein landscape and structural biology of Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis (TB), a persistent global health crisis. It carefully differentiates Mtb proteins and their subclasses, along with associated byproducts, to deepen our understanding of the physiological variations within M. tuberculosis under diverse conditions and to drive the development of innovative treatment strategies.
Organized by the functional roles of proteins, the chapters reveal how individual proteins can perform multiple functions depending on the environmental context, highlighting the bacterium's remarkable adaptability. The book systematically examines the contributions of surface and secreted proteins, metabolic enzymes, efflux pumps, pili, and proteins essential during both exponential growth and persistence phases of the Mtb life cycle. Special focus is given to novel protein targets involved in carbon, nitrogen, and iron-sulfur cluster assembly, as well as proteins with complex domain architectures known for their roles in immune modulation and antigenic variation. Additionally, it addresses protein alterations linked to drug resistance and discusses how structural dynamics and domain combinations influence resistance mechanisms and therapeutic vulnerabilities. By mapping these essential and species-specific proteins, the book emphasizes their potential as therapeutic targets to combat multidrug-resistant and extensively drug-resistant TB. It integrates computational, structural, and experimental approaches for protein target identification and validation, supporting the discovery of new inhibitors and combination therapies.
This comprehensive resource is invaluable for researchers, clinicians, and students in microbiology and infectious disease, offering foundational insights and cutting-edge research to guide future understanding of M. tuberculosis physiology under varying conditions and to inform novel treatment approaches.
