Identification of antigenic peptide recognized by the anti-JL1 leukemia-specific monoclonal antibody from combinatorial peptide phage display libraries

Chung, Jaeyoung; Park, Sojung; Kim, Dongjo; Rhim, Jung-Hyo; Kim, Ik-Jung; Choi, Inhak; Yi, Kye-Sook; Ryu, Sung Ho; Suh, Pann‐Ghill; Chung, Doohyun; Bae, Young-Soo; Shin, Young Kee; Park, Sunghoe

doi:10.1007/s00432-002-0390-x

Cited by 10 publications

(4 citation statements)

References 29 publications

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“…Epitope mapping was performed using Ph.D.-7 Phage Display Peptide Libraries (New England Biolabs) through a total of three rounds of biopanning on NPBR9 IgG 1 or NPBC20 IgG 1 , immobilized on microtiter plates (Corning), as described previously. 18 After the third round of biopanning, peptide-displaying phage clones were prepared and subjected to a phage enzyme immunoassay using NPBR9 IgG 1 or NPBC20 IgG 1 -coated microtiter plates, as described previously. 11 The nucleotide sequences of positive clones were determined by Sanger nucleotide sequencing using a sequencing primer (5′-CCCTCATAGTTAGCGTAACG-3′, NEB).…”

Section: Methodsmentioning

confidence: 99%

An antibody reactive to the Gly63–Lys68 epitope of NT-proBNP exhibits O-glycosylation-independent binding

2014

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The N-terminal fragment of prohormone brain natriuretic peptide (NT-proBNP) is a commonly used biomarker for the diagnosis of congestive heart failure, although its biological function is not well known. NT-proBNP exhibits heavy O-linked glycosylation, and it is quite difficult to develop an antibody that exhibits glycosylation-independent binding. We developed an antibody that binds to the recombinant NT-proBNP protein and its deglycosylated form with similar affinities in an enzyme immunoassay. The epitope was defined as Gly63–Lys68 based on mimetic peptide screening, site-directed mutagenesis and a competition assay with a peptide mimotope. The nearest O-glycosylation residues are Thr58 and Thr71; therefore, four amino acid residues intervene between the epitope and those residues in both directions. In conclusion, we report that an antibody reactive to Gly63–Lys68 of NT-proBNP exhibits O-glycosylation-independent binding.

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Section: Methodsmentioning

confidence: 99%

An antibody reactive to the Gly63–Lys68 epitope of NT-proBNP exhibits O-glycosylation-independent binding

2014

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“…E. coli 2738 was infected with the eluted phages, grown overnight, and collected by centrifugation at 1000 Â g for 15 min. The phages in the culture supernatant were precipitated by 20% (w/v) polyethylene glycol-8000 in 2.5 M NaCl (Chung et al 2002). After centrifugation at 10,000Âg for 20 min the pellet was resuspended in TBS (1 ml) and used for the next round of biopanning.…”

Section: Biopanning and Bead-based Enzyme Immunoassaymentioning

confidence: 99%

Selection of Peptides for Lipopolysaccharide Binding on to Epoxy Beads and Selective Detection of Gram-negative Bacteria

et al. 2006

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Lipopolysaccharide (LPS)-binding peptides were enriched by using epoxy beads as a novel support to immobilize LPS for a phage displayed peptide library screening. The sequence of Phe-Ala-Pro-Trp (FAPW) was the most significant consensus motif of 10 selected clones, and Pro-Phe (PF) was the key dipeptide for binding at the apex of the loop to form a characteristic structure of CXXPFXXXC. Moreover, AWLPWAK, one of the highly conserved heptamer peptides, could detect specifically Gram-negative bacteria via a whole cell binding test at 10(6) cells ml(-1).

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“…Although JL1 expression is restricted to specific populations of thymocytes and BM cells, it is also expressed in approximately 60% of acute leukemias, regardless of lineage [7]. Moreover, JL1 is significantly expressed in adult and childhood acute leukemias [28] and on BM hematopoietic precursor cells [479]; however, JL1 expression on BM lymphoma cells has not been assessed using flow cytometry. An anti-JL1 antibody combined with a toxic substance targeting JL1-positive leukemia has a therapeutic effect [10].…”

Section: Introductionmentioning

confidence: 99%

JL1 Antigen Expression on Bone Marrow Lymphoma Cells from Patients With Non-Hodgkin Lymphoma

et al. 2020

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BackgroundJL1, a CD43 epitope and mucin family cell surface glycoprotein, is expressed on leukemic cells. An anti-JL1 antibody combined with a toxic substance can have targeted therapeutic effects against JL1-positive leukemia; however, JL1 expression on bone marrow (BM) lymphoma cells has not been assessed using flow cytometry. We investigated JL1 expression on BM lymphoma cells from patients with non-Hodgkin lymphoma (NHL) to assess the potential of JL1 as a therapeutic target.MethodsPatients with BM involvement of mature B-cell (N=44) or T- and natural killer (NK)-cell (N=4) lymphomas were enrolled from May 2015 to September 2016. JL1 expression on BM lymphoma cells was investigated using flow cytometry. Clinical, pathological, and cytogenetic characteristics, and treatment responses were compared according to JL1 expression status.ResultsOf the patients with NHL and BM involvement, 37.5% (18/48) were JL1-positive. Among mature B-cell lymphomas, 100%, 38.9%, 33.3%, 100%, and 25.0% of Burkitt lymphomas, diffuse large B-cell leukemias, mantle cell leukemias, Waldenstrom macroglobulinemia, and other B-cell lymphomas, respectively, were JL1-positive. Three mature T- and NK-cell NHLs were JL1-positive. JL1 expression was associated with age (P=0.045), complete response (P=0.004), and BM involvement at follow-up (P=0.017), but not with sex, performance status, the B symptoms, packed marrow pattern, cytogenetic abnormalities, or survival.ConclusionsJL1 positivity was associated with superior complete response and less BM involvement in NHL following chemotherapy.

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Identification of antigenic peptide recognized by the anti-JL1 leukemia-specific monoclonal antibody from combinatorial peptide phage display libraries

Abstract: An epitope-mimetic peptide of anti-JL1 mAb was found using combinatorial peptide phage display libraries. It induced strong humoral response against itself, but only a limited fraction of this humoral response was cross-reactive with the original JL1 antigen.

Cited by 10 publications

References 29 publications

An antibody reactive to the Gly63–Lys68 epitope of NT-proBNP exhibits O-glycosylation-independent binding

An antibody reactive to the Gly63–Lys68 epitope of NT-proBNP exhibits O-glycosylation-independent binding

Selection of Peptides for Lipopolysaccharide Binding on to Epoxy Beads and Selective Detection of Gram-negative Bacteria

JL1 Antigen Expression on Bone Marrow Lymphoma Cells from Patients With Non-Hodgkin Lymphoma

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