Lectin-Dependent Modulation of Interaction between Human Alpha-Fetoprotein and Its Monoclonal Antibodies

Taketa, Kazuhisa; Kamakura, Kozue; Satomura, Shinji; Taga, Hiroko

doi:10.1159/000030024

Cited by 9 publications

(9 citation statements)

References 11 publications

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“…Yakimenko et al [16] in Dr. Abelev's laboratory confirmed the presence of 6 major epitope clusters and identified several minor epitopes. These results were almost identical to that found by Dr. Nustad et al [17] and Kamakura [18] found that one of the epitopes did apparently contain carbohydrate in their studies. Dr. Karamova et al [19] …”

supporting

confidence: 90%

Summary Report: Epitope Analysis of Human Alpha-Fetoprotein

Alpert¹,

Абелев²

1998

Tumor Biol

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supporting

confidence: 90%

Summary Report: Epitope Analysis of Human Alpha-Fetoprotein

Alpert¹,

Абелев²

1998

Tumor Biol

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“…Initially, some of the different forms have been attributed to carbohydrate microheterogeneity and variations in isoelectric points (Smith and Kelleher, 1980;Crandall, 1981). Some AFP isoforms were lectin glycoforms that were detected and isolated by isoelectric focusing, electrophoresis, and chromate-graphic methods (Breborowicz, 1988;Taketa et al, 1998). Other isoforms were detected following high-pressure liquid chromatography (HPLC), and lectin, heavy metal, and hydrophobic solid phase separation methods.…”

Section: Structural Variantsmentioning

confidence: 99%

Mapping of Structure-Function Peptide Sites on the Human Alpha-fetoprotein Amino Acid Sequence

Mizejewski¹

2011

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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The structure of alpha-fetoprotein (AFP) is presen-ted in light of AFP membership and position in the albuminoid gene family in comparison to other gene family members. Ontogenetic AFP gene expression is reviewed considering AFP mRNA presence in various tissues at different times during development. The multiple molecular variant forms of AFP are discussed in relation to published reports of AFP binding proteins and cell surface receptors. The atlas further shows AFP as a protein consisting of multiple peptide-cassettes consisting of amino acid (AA) sequence stretches matched to peptide segments on prohormones and biological response modifier proteins. Such AFP peptide segments could potentially serve as delivery agents which could target vascular, neuroendocrine, or gastrointestinal cells. A discussion follows in which peptide epitopes, extracellular matrix proteins, serine proteases, extracellular matrix, and cellular adhesion AA identity sites on AFP are considered. The AFP molecule is also viewed as a carrier/ transport protein based on AA sequence comparison of various proteins that bind hydropho-bic ligands and heavy metals similar to AFP binding of such components. An analysis of trans-cription factors, tumor suppressors, and AA-rich motifs follows, interfaced with dimerization and nuclear localization sequence matches identified on the AFP molecule. Emphasis is further placed upon homeodomain and apoptosis AA sequence identi-ties given that AFP serves as a fetal, phasespecific protein throughout embryogenesis, histogenesis, and organogenesis. AFP AA sequences are further presented as peptide identification sites for Mapping of Structure-Function Peptide Sites on the Human Alpha-fetoprotein Amino Acid SequenceMizejewski GJ Atlas Genet Cytogenet Oncol Haematol. 2010; 14(2) 170 growth factors, receptors, cytoskeletal proteins, and chemo-kines. A closing discussion summarizes the multi-ple and varied motifs of peptide sequences matched to AAs on each of AFP's three domains. This study indicates that short peptide segments, in addition to full-length AFP, and domain and subdomain fragments of AFP, could be employed as functional agents to help unravel the complexity of biological roles ascribed to human AFP.

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“…Tetrameric ConA efficiently inactivates viral infectivity (8) and may interfere with the interaction between Fab-pp and the epitope because of its spatial bulkiness when it reacts with the glycomoiety near the target epitope (20). Figure 2 ognized by anti-gH neutralizing MAbs were protein portions or at least not glycomoieties of gH that interact with ConA.…”

Section: Varicella-zoster Virus (Vzv) Glycoprotein H (Gh)mentioning

confidence: 99%

Characterization of Neutralizing Epitopes of Varicella-Zoster Virus Glycoprotein H

Akahori

Suzuki

Daikoku

et al. 2009

J Virol

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Varicella-zoster virus (VZV) glycoprotein H (gH)is the major neutralization target of VZV, and its neutralizing epitope is conformational. Ten neutralizing human monoclonal antibodies to gH were used to map the epitopes by immunohistochemical analysis and were categorized into seven epitope groups. The combinational neutralization efficacy of two epitope groups was not synergistic. Each epitope was partially or completely resistant to concanavalin A blocking of the glycomoiety of gH, and their antibodies inhibited the cell-to-cell spread of infection. The neutralization epitope comprised at least seven independent protein portions of gH that served as the target to inhibit cell-to-cell spread.Varicella-zoster virus (VZV) glycoprotein H (gH) is the major target for neutralization (4,5,7,9,18), and it plays an important role in viral entry and cell-to-cell spread of infection (1,3,11,12,15). We isolated human monoclonal antibodies (MAb) to gH using an antibody library called AIMS4 constructed from B-lymphocyte-rich tissues of several dozen people (6,19). Nine clones were selected for their neutralizing ability and their Fab sequences of heavy (H) and light (L) chains and used, in addition to TI-57, an anti-gH human MAb from a hybridoma, to characterize the neutralization epitopes of gH (18). Our system makes it possible to use the Fab form, which has about one-third the molecular weight of immunoglobulin G (IgG), in order to eliminate the spatial interaction between the Fc or other unreacted Fab of IgG molecules on one gH molecule. The neutralizing epitopes of gH are conformational, making gH hardly detectable by Western blot or enzyme-linked immunosorbent assay, and therefore, the conformational epitopes were mapped immunohistochemically. The combinational neutralizing activity between two species of Fab protein A (Fabpp) forms and the inhibition of cell-to-cell infection were characterized, and the neutralization domain of gH was found to comprise a cluster of the seven neutralization epitopes and to prevent cell-to-cell infection.Human embryonic lung cells were used to propagate Oka varicella vaccine, and cell-free virus was obtained by sonication of infected cells in SPGC medium (phosphate-buffered saline [PBS] containing 0.1% sodium glutamate, 5% sucrose, and 10% fetal bovine serum) followed by centrifugation (13,14,16).Except for TI-57, each MAb was expressed in two forms: Fab-pp and Fab with an avidin tag (Fab-Avi-tag). Fab-pp corresponds to an Fab molecule fused with two domains of the Fc-binding protein A from Staphylococcus aureus (8) and purified on an IgG-conjugated column (19). Fab-Avi-tag is composed of an Fab bearing a 23-amino-acid-long peptide tag that can be biotinylated by the bacterial BirA biotin ligase (1). Fab-Avi-tag antibodies were purified by using SoftLink soft release avidin resin (Promega, Madison, WI).To map the neutralizing epitope by Fab-pp, VZV-infected cells in 24-well plates were fixed by air-drying and then with 50% methanol and 50% acetone. The Fab-pp form (5 g/ml in 0.5 ml of ...

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Lectin-Dependent Modulation of Interaction between Human Alpha-Fetoprotein and Its Monoclonal Antibodies

Cited by 9 publications

References 11 publications

Summary Report: Epitope Analysis of Human Alpha-Fetoprotein

Summary Report: Epitope Analysis of Human Alpha-Fetoprotein

Mapping of Structure-Function Peptide Sites on the Human Alpha-fetoprotein Amino Acid Sequence

Characterization of Neutralizing Epitopes of Varicella-Zoster Virus Glycoprotein H

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