A ten-residue fragment of an antibody (mini-antibody) directed against lysozyme as ligand in immunoaffinity chromatography

Welling, Gjalt W.; Gorkum, Judith Van; Damhof, R.A.; Drijfhout, Jan W.; Bloemhoff, W.; Welling‐Wester, Sytske

doi:10.1016/s0021-9673(01)88605-2

Cited by 34 publications

(16 citation statements)

References 14 publications

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“…The diversity of paratopes is mainly generated by the sequences of the CDRs found in V H and V L , which are exposed hypervariable loop structures. Antigen binding by peptide sequences from selected CDRs of mAbs has been demonstrated to have specificities similar to those of the original antibody molecule (31)(32)(33)(34)(35)(36)(37)(38)(39)(40). Our previous results showed that the systematic exploration of the antigen binding capacity of short peptides derived from an antibody sequence leads to the identification of numerous paratope-derived peptides (PDPs) that display significant affinity for the antigen (40).…”

Section: Entry Into Cells (5-7) Cd4 Is a Member Of The Immunoglobulimentioning

confidence: 99%

Synthetic Peptides Derived from the Variable Regions of an Anti-CD4 Monoclonal Antibody Bind to CD4 and Inhibit HIV-1 Promoter Activation in Virus-infected Cells

Monnet¹,

Laune²,

Laroche‐Traineau³

et al. 1999

Journal of Biological Chemistry

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The monoclonal antibody (mAb) ST40, specific for the immunoglobulin complementarity-determining region (CDR) 3-like loop in domain 1 of the CD4 molecule, inhibits human immunodeficiency virus type 1 (HIV-1) promoter activity and viral transcription in HIV-infected cells. To design synthetic peptides from the ST40 paratope that could mimic these biological properties, a set of 220 overlapping 12-mer peptides frameshifted by one residue, corresponding to the deduced ST40 amino acid sequence, was synthesized by the Spot method and tested for binding to recombinant soluble CD4 antigen. Several peptides that included in their sequences amino acids from the CDRs of the antibody and framework residues flanking the CDRs were found to bind soluble CD4. Eleven paratope-derived peptides (termed CM1-CM11) were synthesized in a cyclic and soluble form. All the synthetic peptides showed CD4 binding capacity with affinities ranging from 1.6 to 86.4 nM. Moreover, peptides CM2, CM6, CM7, CM9, and CM11 were able to bind a cyclic peptide corresponding to the CDR3-like loop in domain 1 of CD4 (amino acids 81-92 of CD4). Peptide CM9 from the light chain variable region of mAb ST40 and, to a lesser extent, peptides CM2 and CM11 were able to inhibit HIV-1 promoter long terminal repeat-driven ␤-galactosidase gene expression in the HeLa P4 HIV-1 long terminal repeat ␤-galactosidase indicator cell line infected with HIV-1. The binding of mAb ST40 to CD4 was also efficiently displaced by peptides CM2, CM9, and CM11. Our results indicate that the information gained from a systematic exploration of the antigen binding capacity of synthetic peptides from immunoglobulin variable sequences can lead to the identification of bioactive paratope-derived peptides of potential pharmacological interest.

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Section: Entry Into Cells (5-7) Cd4 Is a Member Of The Immunoglobulimentioning

confidence: 99%

Synthetic Peptides Derived from the Variable Regions of an Anti-CD4 Monoclonal Antibody Bind to CD4 and Inhibit HIV-1 Promoter Activation in Virus-infected Cells

Monnet¹,

Laune²,

Laroche‐Traineau³

et al. 1999

Journal of Biological Chemistry

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“…Areas of amino acid hypervariability within the antigen- (12,13). The aim of this study was to identify the CDR region(s) of mAb F58 responsible for interacting with the HIV-1 V3 region.…”

mentioning

confidence: 99%

A complementarity-determining region synthetic peptide acts as a miniantibody and neutralizes human immunodeficiency virus type 1 in vitro.

Levi

Sällberg

Rudén

et al. 1993

Proc. Natl. Acad. Sci. U.S.A.

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A complementarity-determining region (CDR) of the mouse monoclonal antibody (mAb) F58 was constrcted with specificity to a neutalization-indudng region of human immunodeficiency virus type 1 (1HV-1). The mAb has its major reactivity to the amino acid sequence I-GPGRA in the V3 viral envelope region. All CDRs including several framework amno acids were synthesized from the sequence deduced by cloning and sequencing mAb F58 heavy-and light-chain variable d . Peptides derived from the third heavy-chain domain (CDR-H3) alone or in combination with the olher CDR sequences competed with F58 mAb for the V3 region. The CDR-H3 peptide was chemicaly modified by cyclization and then inhibited HIV-1 replication as well as syncytium formation by infected cels. Both the homologous lllB viral strain to which the F58 mAb was induced and the heterologous SF2 strain were inhibited. This synthetic peptide had unexpectedly potent antiviral activity and may be a potential tool for treatment of IRV-infected persons.

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“…Blank columns without any ligand were prepared from each chromatography material by hydrolyzation of epoxy groups with 0.5 M sulfuric acid. For selectivity experiments, a peptide directed against lysozyme [22] was immobilized on a CIM column and used as a blank.…”

Section: Immobilization Of Peptidesmentioning

confidence: 99%

“…Furthermore, ligand leakage into the product is also considered as a serious problem. For this reason several groups have started to reduce the size of large protein-ligands by designing single chain antibodies [21] and mini-antibodies [22].…”

Section: Introductionmentioning

confidence: 99%

Affinity Chromatography of Human Blood Coagulation Factor VIII on Monoliths with Peptides from a Combinatorial Library

Amatschek

Necina

Hahn

et al. 2000

J. High Resol. Chromatogr.

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A ten-residue fragment of an antibody (mini-antibody) directed against lysozyme as ligand in immunoaffinity chromatography

Cited by 34 publications

References 14 publications

Synthetic Peptides Derived from the Variable Regions of an Anti-CD4 Monoclonal Antibody Bind to CD4 and Inhibit HIV-1 Promoter Activation in Virus-infected Cells

Synthetic Peptides Derived from the Variable Regions of an Anti-CD4 Monoclonal Antibody Bind to CD4 and Inhibit HIV-1 Promoter Activation in Virus-infected Cells

A complementarity-determining region synthetic peptide acts as a miniantibody and neutralizes human immunodeficiency virus type 1 in vitro.

Affinity Chromatography of Human Blood Coagulation Factor VIII on Monoliths with Peptides from a Combinatorial Library

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