Abstract
In this brief commentary, I highlight the remarkable properties of antibodies (also known as immunoglobulins) revealed by more than 100 years of biomedical research. Since antibodies can be elicited through one or another means against almost any molecule or macromolecule, the universe of antibodies represents a sort of molecular mirror for the totality of molecules that make life possible. Consequently, as recounted below, antibodies play a role in almost every aspect of medicine and biomedical research.
Highlights
RANGE OF ANTIBODY FUNCTIONS Antibodies are functionally protean proteins [3]. They serve in an unparalleled range of roles in biology and medicine by virtue of a remarkable constellation of attributes including inducibility, or potential inducibility by, and noncovalent affinity for, almost any small molecule or macromolecule, prodigious capacity for molecular discrimination, structural and functional stability, remarkably extended serum half-life, structural features conducive to detection in laboratory assays, and biologically efficacious interactions, known as effector functions
Antibodies, known as immunoglobulins, originate in an almost unique process of gene rearrangement that depends on what might be referred to as a series of dynamic, approximately one-dimensional immunoglobulin gene jigsaw puzzles [4]
Each antibody polypeptide chain is constructed of 3 or 4 domains encoded by gene segments that are separated by intervening stretches of nucleotide sequence in the germline DNA and that become juxtaposed, prior to translation, by either DNA rearrangement or RNA splicing. These nucleic acid acrobatics generate new amino acid sequences, not originally encoded in the germline genome, in regions of the polypeptide chains referred to, with astonishing creativity, as variable regions. Superimposed on these mutation-generating events that are integral to the processes required for the assembly of complete antibody-encoding genes is another unique process, termed somatic hypermutation that can lead to affinity maturation [5]
Summary
They serve in an unparalleled range of roles in biology and medicine by virtue of a remarkable constellation of attributes including inducibility, or potential inducibility by, and noncovalent affinity for, almost any small molecule or macromolecule, prodigious capacity for molecular discrimination, structural and functional stability, remarkably extended serum half-life, structural features conducive to detection in laboratory assays, and biologically efficacious interactions, known as effector functions. These immunity-mediating effector systems involve complement and Fc receptor-bearing cells and more recently-discovered intracellular molecules.
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