Immunogenicity of a free synthetic peptide: Carrier-conjugation enhances antibody affinity for the native protein

Mariani, Massimo A.; Bracci, Luisa; Presentini, R; Nucci, Daniele; Neri, Paolo; Antoni, G.

doi:10.1016/0161-5890(87)90148-9

Cited by 44 publications

(9 citation statements)

References 17 publications

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“…It is well-known that the method used to couple peptides to a carrier protein strongly influences both the immunogenicity and antigenicity of the conjugate [3,12,19,30,35]. In the present study the BPMV antisera recognized the region A20-27 only if the corresponding linear and cyclical peptides were conjugated via their C-terminal tyrosine by means of BDB.…”

Section: Discussionmentioning

confidence: 97%

Antigenic analysis of bean pod mottle virus using linear and cyclized synthetic peptides

Joisson

Kuster²,

Plaué³

et al. 1993

Archives of Virology

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The antigenic structure of the comovirus bean pod mottle virus (BPMV) was studied using synthetic peptides selected on the basis of the exposed location of certain regions of the viral protein. Three regions of domain A, four regions of domain B and two regions of domain C of BPMV coat protein were studied. Each of four regions were synthesized in the form of linear and cyclized peptides while the others were synthesized as linear peptides only. The peptides were tested for their ability to be recognized by antibodies directed against BPMV. The peptides were also used for producing rabbit antisera, which were tested for their ability to react with various BPMV antigens as well as with the linear and cyclized peptides. All the peptides were found to correspond to epitopes of BPMV coat protein. Several of the antigenic sites of BPMV located on exposed loops of the coat protein occupy positions which correspond to known epitopes in the structurally related picornaviruses. Only in some cases did cyclization sufficiently improve the level of conformational mimicry between peptides and the viral protein to allow cross-reactions between them to be observed.

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Section: Discussionmentioning

confidence: 97%

Antigenic analysis of bean pod mottle virus using linear and cyclized synthetic peptides

Joisson

Kuster²,

Plaué³

et al. 1993

Archives of Virology

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“…Binding constants were calculated in ELISA by second antibody binding curves, using a slightly modified version of a computer program (Mariani et al, 1987). Briefly, %well vinyl assay plates were coated with goat anti-mouse IgG (5 mg/mL in PBS) and incubated overnight at 4 "C. Serial dilutions (from 3 pmol/well to 0.03 pmol/well) of the MAbs were dispensed into the wells and incubated 20 h at 4 "C. Finally, HPR-Tf (0.125 pmol/well) was added to the wells and incubated for 1 h at 37 "C. Absorbance was read at 414 nm on an EIA reader.…”

Section: Determination Of the Binding Constants (Ko) Of The Mabsmentioning

confidence: 99%

Cloning, characterization, and modeling of a monoclonal anti‐human transferrin antibody that competes with the transferrin receptor

Orlandini¹,

Santucci²,

Tramontano³

et al. 1994

Protein Science

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In this report we describe the isolation and characterization of a monoclonal antibody against human serum transferrin (Tf) and the cloning and sequencing of its cDNA. The antibody competes with the transferrin receptor (TR) for binding to human Tf and is therefore expected to bind at or very close to a region of interaction between Tf and its receptor. From the deduced amino acid sequence, we constructed a 3-dimensional model of the variable domains of the antibody based on the canonical structure model for the hypervariable loops. The proposed structure of the antibody is a first step toward a more detailed characterization of the antibody-Tf complex and possibly toward a better understanding of the Tf interaction with its receptor. The model might prove useful in guiding site-directed mutagenesis studies, simplifying the experimental elucidation of the antibody structure, and in the use of automatic procedures to dock the interacting molecules as soon as structural information about the structure of the human Tf molecule will be available.

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“…A curve was determined using the 4 parameter logistic function in an IBM-PC desk-top computer program. The affinity constant was calculated as the reciprocal of the concentration of total added antibody that showed 50% of the maximum binding (Mariani et al, 1987).…”

Section: Determination Of the Afinity Constantmentioning

confidence: 99%

“…9). Binding values obtained were analyzed and plotted using the computer SAB program (Mariani et al, 1987) which is able to interpret values of an indirect immunoreaction. The calculated affinity constant (K,) of the MAb was determined by taking the reciprocal of the concentration of total added antibody giving 50% of the maximum binding.…”

Section: Afinity Of Mab57 For Its Epitopementioning

confidence: 99%

Characterization by somatic cell genetics of a monoclonal antibody to the MDR1 gene product (P‐glycoprotein): Determination of p‐glycoprotein expression in multi‐drug‐resistant kb and cem cell variants

Cenciarelli

Currier

Willingham

et al. 1991

Intl Journal of Cancer

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We isolated an IgG2a murine monoclonal antibody (MAb) termed MAb57, specifically reactive with multi-drug-resistant (MDR) human cells. Its specificity toward the MDRI gene product (P-glycoprotein) has been demonstrated by the concordant segregation of the MAb57 epitope with the MDRI gene in interspecific mouse x human cell hybrids, and the reactivity of several different MDRI gene-expressing cells with MAb57, particularly insect cells acutely infected with a baculovirus encoding the MDRI gene. MAb57 can be used to detect, by flow cytometry, variations in the relative drug-resistance levels of several MDR KB and CEM cell variants. This immunological probe has also proven useful in selectively destroying MDR target cells in an antibody-dependent cell-mediated (ADCC) assay system as well as in detecting P-glycoprotein expression in normal and malignant tissues and cells.

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Immunogenicity of a free synthetic peptide: Carrier-conjugation enhances antibody affinity for the native protein

Cited by 44 publications

References 17 publications

Antigenic analysis of bean pod mottle virus using linear and cyclized synthetic peptides

Antigenic analysis of bean pod mottle virus using linear and cyclized synthetic peptides

Cloning, characterization, and modeling of a monoclonal anti‐human transferrin antibody that competes with the transferrin receptor

Characterization by somatic cell genetics of a monoclonal antibody to the MDR1 gene product (P‐glycoprotein): Determination of p‐glycoprotein expression in multi‐drug‐resistant kb and cem cell variants

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