Antigen-independent and dependent maturation of the immunoglobulin sequence from the germline repertoire is the basis of the adaptive humoral response. This process produces a vast repertoire of mature, secreted immunoglobulins with virtually unique sequences. Along this pathway, however, acquisition of specific sets of mutations and usage of specific germlines may translate into acquisition of detrimental properties, such as the ability to aggregate and to cause cell and organ damage. These features often become clinically evident when aberrant immunoglobulins are produced in excess by a plasma cell or B cell clone. Peculiar biochemical/biophysical traits, pathogenic interaction with the environment, and intrinsic proteotoxicity are associated with development of specific diseases, such as light chain (AL) and heavy chain (AH) amyloidosis, light chain deposition disease (LCDD), and related conditions.
Defining the relation between primary structure of light and heavy chains and specific pathogenic properties is key for understanding the molecular bases of a set of dreadful diseases caused by aberrant immunoglobulins. This knowledge could form the basis to develop tools for risk prediction in patients and for the rationale design of potential therapeutic molecules. The main focus of this Research Topic is to characterize the role that specific sequence determinants play in conferring aggregation propensity and proteotoxicity to disease-associated immunoglobulin proteins. Research may range from patients-based genetic studies, to the biochemical, biophysical, biological and computational characterization of in vitro or ex-vivo material.
This Research Topic accepts manuscripts highlighting the relation between immunoglobulin sequence and pathogenicity in vivo and in vitro.
Themes to be addressed include, but are not limited to:
• Clinical and experimental studies concerning diseases related to aberrant immunoglobulins, such as light chain amyloidosis, heavy chain amyloidosis, light chain deposition disease, cryoglobulinemia/crystal-cryo globulinemia, heavy chain deposition disease
• In vitro study of biochemical, biophysical, structural and biological properties of immunoglobulins with pathogenic sequence
• Relation between antibody sequence and tropism of organ damage light and heavy chain aggregation diseases
• Novel approaches for immunoglobulin sequence investigation, such as NGS- and mass spectrometry-based studies
• Databases of immunoglobulin sequences
Manuscripts of interest:
• Original Research
• Perspective
• Hypothesis and Theory
• Review
Antigen-independent and dependent maturation of the immunoglobulin sequence from the germline repertoire is the basis of the adaptive humoral response. This process produces a vast repertoire of mature, secreted immunoglobulins with virtually unique sequences. Along this pathway, however, acquisition of specific sets of mutations and usage of specific germlines may translate into acquisition of detrimental properties, such as the ability to aggregate and to cause cell and organ damage. These features often become clinically evident when aberrant immunoglobulins are produced in excess by a plasma cell or B cell clone. Peculiar biochemical/biophysical traits, pathogenic interaction with the environment, and intrinsic proteotoxicity are associated with development of specific diseases, such as light chain (AL) and heavy chain (AH) amyloidosis, light chain deposition disease (LCDD), and related conditions.
Defining the relation between primary structure of light and heavy chains and specific pathogenic properties is key for understanding the molecular bases of a set of dreadful diseases caused by aberrant immunoglobulins. This knowledge could form the basis to develop tools for risk prediction in patients and for the rationale design of potential therapeutic molecules. The main focus of this Research Topic is to characterize the role that specific sequence determinants play in conferring aggregation propensity and proteotoxicity to disease-associated immunoglobulin proteins. Research may range from patients-based genetic studies, to the biochemical, biophysical, biological and computational characterization of in vitro or ex-vivo material.
This Research Topic accepts manuscripts highlighting the relation between immunoglobulin sequence and pathogenicity in vivo and in vitro.
Themes to be addressed include, but are not limited to:
• Clinical and experimental studies concerning diseases related to aberrant immunoglobulins, such as light chain amyloidosis, heavy chain amyloidosis, light chain deposition disease, cryoglobulinemia/crystal-cryo globulinemia, heavy chain deposition disease
• In vitro study of biochemical, biophysical, structural and biological properties of immunoglobulins with pathogenic sequence
• Relation between antibody sequence and tropism of organ damage light and heavy chain aggregation diseases
• Novel approaches for immunoglobulin sequence investigation, such as NGS- and mass spectrometry-based studies
• Databases of immunoglobulin sequences
Manuscripts of interest:
• Original Research
• Perspective
• Hypothesis and Theory
• Review