Antibodies for Growth Hormone and Prolactin Using Multiple Antigen Peptide Immunogens

1999 ◽  
Vol 1 (3) ◽  
pp. 211-220 ◽  
Author(s):  
Lucía Irene González-Villaseñor ◽  
Thomas T. Chen
Keyword(s):  
Growth Hormone ◽  
Multiple Antigen ◽  
Antigen Peptide ◽  
Multiple Antigen Peptide

scholarly journals Immunogenicity of NS4b Dengue 3 Virus Mimotope Presented to the Immune System as Multiple Antigen Peptide System

ISRN Virology ◽  
2013 ◽  
Vol 2013 ◽  
pp. 1-7 ◽  
Author(s):  
Nevis Amin ◽  
Maritza Pupo ◽  
Alicia Aguilar ◽  
Frank Camacho ◽  
Mayling Alvarez ◽  
...  
Keyword(s):  
Dengue Virus ◽  
Vaccine Design ◽  
Amino Acid Sequences ◽  
Diagnostic Assays ◽  
Random Peptide ◽  
Multiple Antigen ◽  
Antigen Peptide ◽  
Multiple Antigen Peptide ◽  
Human Sera ◽  
Phage Displayed Peptide Library

The availability of random peptide libraries displayed on bacteriophage (RPL) has provided a powerful tool for selecting sequences that mimic binding properties of natural antigen epitopes (mimotopes). These mimotopes can be used for vaccine design, drug development, and diagnostic assays. Several mimotopes have been shown to induce production of antibodies against the natural antigen. We have previously identified four dengue virus mimotopes from a phage-displayed peptide library using antidengue 3 human sera. Three of them showed similarity in their amino acid sequences with the NS4b proteins of dengue. Few studies have examined the role of NS4b proteins in the antibody response to dengue virus infection. A multiple antigen peptide (MAP) system was chemically synthesized containing this mimotope (NS4b MAP), and BALB/c mice were immunized to evaluate its immunogenicity. Antipeptide responses were induced and recognised DENV-3 infected cells as determined by immunofluorescence. The high levels of the IgG2a subtype against NS4bMAP suggest the induction of a Th1-like response. Our findings suggest that the NS4b mimotope might be a useful tool for the development of multiepitope diagnostic assays, dengue virus vaccine design, and pathogenesis studies.

Structural probing of human lutropin using antibodies raised against synthetic peptides constructed by classical and multiple antigen peptide system approaches

1990 ◽  
Vol 27 (4) ◽  
pp. 363-368 ◽  
Author(s):  
Frédéric Troalen ◽  
Alain Razafindratsita ◽  
Alain Puisieux ◽  
Thibault Voeltzel ◽  
Claude Bohuon ◽  
...  
Keyword(s):  
Synthetic Peptides ◽  
Multiple Antigen ◽  
Antigen Peptide ◽  
Multiple Antigen Peptide ◽  
Peptide System ◽  
System Approaches

Autoantibodies directed against ribosomal P proteins: use of a multiple antigen peptide as the coating agent in ELISA

1995 ◽  
Vol 179 (2) ◽  
pp. 193-202 ◽  
Author(s):  
L. Caponi ◽  
S. Pegoraro ◽  
V. Di Bartolo ◽  
P. Rovero ◽  
R. Revoltella ◽  
...  
Keyword(s):  
Coating Agent ◽  
Multiple Antigen ◽  
Antigen Peptide ◽  
Multiple Antigen Peptide ◽  
P Proteins ◽  
Ribosomal P

scholarly journals A Cyclic Dodecapeptide–Multiple-Antigen Peptide Conjugate from the Undecapeptidyl Arch (from Arg168 to Cys178) of Extracellular Loop 2 in CCR5 as a Novel Human Immunodeficiency Virus Type 1 Vaccine

2001 ◽  
Vol 75 (23) ◽  
pp. 11614-11620 ◽  
Author(s):  
Shogo Misumi ◽  
Reina Nakajima ◽  
Nobutoki Takamune ◽  
Shozo Shoji
Keyword(s):  
Human Immunodeficiency Virus ◽  
Extracellular Loop ◽  
Specific Domain ◽  
Multiple Antigen ◽  
Immunodeficiency Virus ◽  
Antigen Peptide ◽  
Multiple Antigen Peptide ◽  
Loop 2 ◽  
Hiv 1

ABSTRACT A cyclic closed-chain dodecapeptide (cDDR5) mimicking the conformation-specific domain of CCR5 was prepared in which Gly-Asp, as a dipeptide forming a spacer arm, links the amino and carboxyl termini of the decapeptidyl linear chain (Arg168 to Thr177) derived from the undecapeptidyl arch (UPA; Arg168 to Cys178) of extracellular loop 2 (ECL2) in CCR5. Novel monoclonal antibodies were raised against cDDR5 conjugated with a multiple-antigen peptide (cDDR5-MAP), and the purified antibody [KB8C12, immunoglobulin M(κ)] reacted with cDDR5, but not with linear DDR5, in real-time biomolecular interaction analysis using surface plasmon resonance. The antibody also reacted with cells expressing CCR5, but not with cells expressing CXCR4, and the immunoreaction was competed by cDDR5-MAP. The antibody significantly interfered with chemotaxis induced by macrophage inflammatory protein, 1β, and at a concentration of 1.67 nM it almost completely inhibited infection by human immunodeficiency virus type 1 (HIV-1) R5, but not by HIV-1 X4, as observed by use of a new phenotypic assay for drug susceptibility of HIV-1 using the CCR5-expressing HeLa CD4+ cell clone 1-10 (MAGIC-5). Furthermore, cDDR5-MAP suppressed infection by HIV-1 R5 at relatively high concentrations (50 to 400 μM) in a dose-dependent manner but did not suppress infection by HIV-1 X4. Taken together, these results indicate that the antibody is conformation specific and recognizes the conformation-specific domain of the UPA of ECL2. Moreover, both the antibody and its immunogen, the cDDR5-MAP conjugate, may be useful in developing a new candidate vaccine for HIV therapy.

scholarly journals Antimicrobial Activity of Novel Dendrimeric Peptides Obtained by Phage Display Selection and Rational Modification

2005 ◽  
Vol 49 (7) ◽  
pp. 2665-2672 ◽  
Author(s):  
Alessandro Pini ◽  
Andrea Giuliani ◽  
Chiara Falciani ◽  
Ylenia Runci ◽  
Claudia Ricci ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Multidrug Resistant ◽  
Cytotoxic Effects ◽  
E Coli ◽  
Multiple Antigen ◽  
Antigen Peptide ◽  
Multiple Antigen Peptide ◽  
Residue Substitution ◽  
Peptide Map ◽  
Phage Peptide Library

ABSTRACT A large 10-mer phage peptide library was panned against whole Escherichia coli cells, and an antimicrobial peptide (QEKIRVRLSA) was selected. The peptide was synthesized in monomeric and dendrimeric tetrabranched form (multiple antigen peptide [MAP]), which generally allows a dramatic increase of peptide stability to peptidases and proteases. The antibacterial activity of the dendrimeric peptide against E. coli was much higher than that of the monomeric form. Modification of the original sequence, by residue substitution or sequence shortening, produced three different MAPs, M4 (QAKIRVRLSA), M5 (KIRVRLSA), and M6 (QKKIRVRLSA) with enhanced stability to natural degradation and antimicrobial activity against a large panel of gram-negative bacteria. The MICs of the most potent peptide, M6, were as low as 4 to 8 μg/ml against recent clinical isolates of multidrug-resistant Pseudomonas aeruginosa and members of the Enterobacteriaceae. The same dendrimeric peptides showed high stability to blood proteases, low hemolytic activity, and low cytotoxic effects on eukaryotic cells, making them promising candidates for the development of new antibacterial drugs.

scholarly journals Diepitope multiple antigen peptide of hTERT trigger stronger anti-tumor immune responses in vitro

2013 ◽  
Vol 16 (4) ◽  
pp. 444-450 ◽  
Author(s):  
Zhong-Li Liao ◽  
Gang Luo ◽  
Xia Xie ◽  
Xu-Dong Tang ◽  
Jian Ying Bai ◽  
...  
Keyword(s):  
Immune Responses ◽  
Multiple Antigen ◽  
Antigen Peptide ◽  
Multiple Antigen Peptide
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