Cryo-EM and Crystallographic Insights into Immune Receptor and Antibody Function

Structural biology has emerged as a pivotal field in uncovering the intricate architectures and functional mechanisms of biomolecules central to immunity. Cryo–electron microscopy (cryo-EM) and X-ray crystallography have become foundational techniques, offering unparalleled resolution of immune receptors and antibodies, enabling detailed visualization of antigen recognition, receptor activation, and immune signaling. Many challenges persist, however. A particularly pressing issue involves capturing transient states, conformational flexibility, and dynamic interactions, characteristics fundamental to immune specificity and regulation, yet elusive to singular structural approaches. Notably, technological leaps in cryo-EM, ranging from detector improvements and algorithmic advancements to refined sample preparation, have begun to democratize access to complex immune assemblies at near-atomic scales.Across a range of recent studies, the integration of cryo-EM and crystallography has started to resolve questions that were previously out of reach, including the structural basis for immune discrimination and therapeutic resistance, including where immune-associated enzymes, such as proteases involved in complement activation or antigen processing, play a regulatory role. Enhanced imaging, combined with time-resolved crystallographic methods and integrative modelling, is beginning to illuminate a wider spectrum of functional states and intermolecular interactions within the immune system. Nonetheless, many mechanistically relevant conformations and dynamic processes remain uncharacterized, limiting our ability to devise precision immunotherapeutics or fully understand immune regulation at the molecular level.This Research Topic aims to delineate and advance our understanding of the molecular underpinnings of immune receptors and antibodies, with particular emphasis on challenges associated with conformational heterogeneity, dynamic regulation, and transient complex formation. The main objective is to showcase research that leverages the latest developments in cryo-EM and X-ray crystallography, alongside complementary biophysical, computational, and integrative methodologies, to unravel unresolved functional states and mechanisms within immunity. By fostering contributions at the intersection of technological innovation and immune biology, this collection aspires to deliver an updated, holistic structural framework for immunity, ultimately guiding structure-based therapeutic strategies.This Research Topic encompasses studies focused on the structural elucidation of immune receptors, antibodies, and their associated regulatory machinery via cryo-EM, crystallography, and integrated approaches. Submissions addressing enzymes or systems unrelated to immune function will not be considered, unless the enzyme in question plays a direct regulatory role within an immune pathway. We welcome articles addressing, but not limited to, the following themes:- Structural mechanisms of immune receptor activation, signaling, and regulation- Antibody–antigen recognition, affinity maturation, and conformational diversity- Cryo-EM and crystallographic studies of flexible, dynamic, or heterogeneous immune complexes- Structural insights into the regulation of immune-associated enzymes, such as complement proteases or antigen-processing enzymes- Integration of cryo-EM and crystallography with complementary methods such as biophysics, computational modeling, and mass spectrometry- Methodological advances in sample preparation, data collection, image processing, and model validation relevant to immune systems- Structure-guided drug and biologic design informed by high-resolution structural data of immune targets Topic editors: S Saif Hasan, Abhishek Dey Source: https://www.frontiersin.org/research-topics/78476/cryo-em-and-crystallographic-insights-into-immune-receptor-and-antibody-function