Recombinant production of a VL single domain antibody in Escherichia coli and analysis of its interaction with peptostreptococcal protein L

Cossins, Aimee J.; Harrison, S.; Popplewell, Andrew G.; Gore, Michael G.

doi:10.1016/j.pep.2006.07.013

Cited by 21 publications

(15 citation statements)

References 18 publications

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“…They are approximately one-tenth the molecular weight (MW) of a normal antibody (150-160 kDa), one fourth the MW of an average Fab (50 kDa) and half the MW of a typical scFv (25 kDa) [8,[50][51][52]. Although dAbs contain only three of the six CDRs from the parent antibody, they exhibit antigen binding specificity and affinity [52]. They can be remarkably stable under harsh conditions of temperature, pressure, and denaturing chemicals [53].…”

Section: Antibodies and Their Fragmentsmentioning

confidence: 99%

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Antibody Fragments and Their Purification by Protein L Affinity Chromatography

Rodrigo¹,

Gruvegard²,

Alstine

2015

Antibodies

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Antibodies and related proteins comprise one of the largest and fastest-growing classes of protein pharmaceuticals. A majority of such molecules are monoclonal antibodies; however, many new entities are antibody fragments. Due to their structural, physiological, and pharmacological properties, antibody fragments offer new biopharmaceutical opportunities. In the case of recombinant full-length antibodies with suitable Fc regions, two or three column purification processes centered around Protein A affinity chromatography have proven to be fast, efficient, robust, cost-effective, and scalable. Most antibody fragments lack Fc and suitable affinity for Protein A. Adapting proven antibody purification processes to antibody fragments demands different affinity chromatography. Such technology must offer the unit operation advantages noted above, and be suitable for most of the many different types of antibody fragments. Protein L affinity chromatography appears to fulfill these criteria-suggesting its consideration as a key unit operation in antibody fragment processing.

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Section: Antibodies and Their Fragmentsmentioning

confidence: 99%

“…Such affinity resins have been used in the noncommercial purification of scFv's [31,41,80,89,105,106], Fab's [91,[106][107][108], and single-domain antibodies [52,91,98,103,108,109].…”

Section: Protein L and Its Use In Antibody Fragment Bioprocessingmentioning

confidence: 99%

Antibody Fragments and Their Purification by Protein L Affinity Chromatography

Rodrigo¹,

Gruvegard²,

Alstine

2015

Antibodies

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“…These result from the in vitro cleavage of functional IgG fragments, as in the case of the VL binder specific for the streptococcal protein L [36] and of the VL-barnase immunotoxin that accumulates soluble and functional in E. coli cytoplasm [37]. …”

Section: Introductionmentioning

confidence: 99%

Biotechnological applications of recombinant single-domain antibody fragments

Marco

2011

Microb Cell Fact

147

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BackgroundSingle-domain antibody fragments possess structural features, such as a small dimension, an elevated stability, and the singularity of recognizing epitopes non-accessible for conventional antibodies that make them interesting for several research and biotechnological applications.ResultsThe discovery of the single-domain antibody's potentials has stimulated their use in an increasing variety of fields. The rapid accumulation of articles describing new applications and further developments of established approaches has made it, therefore, necessary to update the previous reviews with a new and more complete summary of the topic.ConclusionsBeside the necessary task of updating, this work analyses in detail some applicative aspects of the single-domain antibodies that have been overseen in the past, such as their efficacy in affinity chromatography, as co-crystallization chaperones, protein aggregation controllers, enzyme activity tuners, and the specificities of the unconventional single-domain fragments.

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“…Protein L from Peptostreptococcus magnus (PpL) interacts with two-thirds of mouse and almost half of the human Ig repertoires. IgG-binding domains from PpL have been shown to bind specifically to κ-light chains (κ1, κ3 and κ4, but not κ2) and λ light chains of antibodies (Cossins et al, 2007).…”

Section: Purification Of Antibodies On Immobilized Proteins a G And Lmentioning

confidence: 99%