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Hybridoma technology, developed by Köhler and Milstein in 1975, introduced a method for the generation of monoclonal antibodies (mAbs) through the fusion of antigen-specific B lymphocytes with immortal myeloma cells. This approach enabled the long-term culture of hybrid cells—termed hybridomas—that produce highly specific antibodies targeting a single epitope.

Antibody fragments have become indispensable in modern biotechnology due to their smaller size, improved tissue penetration, and suitability for engineered constructs. Among these, camelid VHH nanobodies (single-domain antibodies) and single-chain variable fragments (scFvs) represent two widely studied and applied formats. Both can be produced recombinantly and tailored for diagnostic or therapeutic use, yet their origins, molecular structures, and functional properties are distinct.

Single-domain antibodies (sdAbs), often referred to as VHHs or nanobodies, are derived from the heavy-chain-only antibodies found in camelids such as llamas and alpacas. They are the smallest naturally occurring antibody fragments, about 15 kDa in size, and consist of a single variable domain.

VHH antibodies, also called single-domain antibodies or nanobodies, are the smallest functional fragments of antibodies capable of binding antigens. They originate from the heavy-chain-only antibodies found in camelids such as llamas and camels. Unlike conventional antibodies, which require both heavy and light chains for antigen recognition, VHHs operate as a single domain.

Camelid antibodies are specialized immunoglobulins naturally found in llamas, alpacas, and camels. Unlike conventional antibodies that use both heavy and light chains, camelids produce a unique form known as heavy-chain-only antibodies. Their variable domain, called the VHH or single-domain antibody, retains full antigen-binding activity even without light chains.

Affinity maturation is a hallmark of the adaptive immune system that enables B cells to generate antibodies with increased specificity and binding strength against antigens. Through cycles of somatic hypermutation (SHM) and clonal selection within germinal centers, antibody affinities can improve by several orders of magnitude. Understanding the molecular and biophysical mechanisms of this process has been essential for therapeutic antibody development and rational vaccine design.

Since the first recombinant protein therapeutic, human insulin, was approved in 1982, more than 250 protein-based drugs have entered the global market. Monoclonal antibodies (mAbs), in particular, are a rapidly growing class of biologics, representing nearly half of all therapeutic proteins approved by the U.S. Food and Drug Administration (FDA) in recent years.

Monoclonal antibodies (mAbs) are immunoglobulins that recognize a single epitope on a target antigen. Their specificity and reproducibility make them useful in therapeutic development, diagnostics, and life science research.

Over the past four decades, antibody discovery platforms have transformed biotherapeutics. Hybridoma technology, developed in 1975, pioneered the production of monoclonal antibodies, while more recent advances in single B cell screening have expanded access to rare, high-affinity clones.

DOI: 10.3389/fimmu.2021.7532941. Structural Overview of AntibodiesAntibodies, or immunoglobulins (Igs), are glycoproteins produced by plasma cells as part of the adaptive immune response. They are composed of two identical heavy chains (~50 kDa each) and two identical light chains (~25 kDa each), co

Cambridge Healthtech Institute’s 13th Annual 2025 Immuno-Oncology Summit was held in Philadelphia, PA, USA, from August 11-13. Read on for a summary of the event spanning solid tumor innovations and antibody therapeutics.

The immune system adapts from naïve to memory states. Biointron explains immunity, PAMPs, and therapeutic modulation strategies.