2002
DOI: 10.1046/j.1365-2567.2002.01473.x
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Modulation of the CD40–CD40 ligand interaction using human anti‐CD40 single‐chain antibody fragments obtained from the n‐CoDeR phage display library

Abstract: SUMMARYCD40 plays a central regulatory role in the immune system and antibodies able to modulate CD40 signalling may consequently have a potential in immunotherapy, in particular for treatment of lymphomas and autoimmune disease like multiple sclerosis. As a first step to achieve this goal, we describe the selection and characterization of a novel set of fully human anti-CD40 antibody fragments (scFv) from a phage display library (n-CoDeR). In order to determine their biological potential, these antibody fragm… Show more

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Cited by 17 publications
(22 citation statements)
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“…To translate these findings into the clinic, we set out to engineer a CD40 agonistic antibody (18,19), ADC-1013, using Fragment INduced Diversity (FIND; ref. 20).…”
Section: Introductionmentioning
confidence: 99%
“…To translate these findings into the clinic, we set out to engineer a CD40 agonistic antibody (18,19), ADC-1013, using Fragment INduced Diversity (FIND; ref. 20).…”
Section: Introductionmentioning
confidence: 99%
“…Recombinant antibodies derived from phage display libraries [1-10] are by now well established in medicine and biotechnology. A major objective of recombinant antibody research so far has been to develop new therapeutic agents for use in human patients.…”
Section: Introductionmentioning
confidence: 99%
“…The binding properties of the different anti-CD40 antibodies varied 20-fold between the strongest binder, A2-54, and the weakest binder F33; however, the ranking order did not correlate with the previously determined monovalent affinity for scFvs. 20,21 This difference is probably due to the steric hindrance of the larger IgG molecules (5.4 times higher molar weight) for binding to cell surface-expressed CD40. It appears that this effect may depend on the binding domain of the antibody, since F33, which binds to the domain located closest to the cell surface, binds poorly to CD40 ϩ cells despite its high affinity in the scFv format.…”
Section: Discussionmentioning
confidence: 99%
“…20,21 Antibodies obtained from this library have been demonstrated to be well tolerated, and in contrast to antibodies of murine origin, they do not elicit the human antimouse (HAMA) response found in most patients. 22 To date, several monoclonal anti-CD40 antibodies are in clinical trials for indications such as autoimmunity and cancer; 16,17,23 however, only one of them, CHIR-12.12, is a human antibody derived from Xeno mice.…”
Section: Introductionmentioning
confidence: 99%
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