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 Potency of antigenic and serologic tests based on CNTKCQTP linear epitope on H5N1 haemagglutinin for Avian Influenza

2016 ◽  
Vol 21 (1) ◽  
pp. 62
Author(s):  
Simson Tarigan ◽  
. Sumarningsih
Keyword(s):  
Avian Influenza ◽  
Point Of Care ◽  
Diagnostic Tools ◽  
Linear Epitope ◽  
Multiple Antigen ◽  
Antigen Peptide ◽  
Multiple Antigen Peptide ◽  
Hpai H5n1 ◽  
Peptide Map ◽  
Main Component

<p class="abstrak2">Rapid diagnostic tools or point-of-care (POC) test is needed in the effort to control and eradicate the high pathogenic avian influenza (HPAI) H5N1 in Indonesia. Accuracy of a POC test is determined by the specificity of antibodies, which is the main component of a POC test. Recently a linear epitope, CNTCKQTP epitope, located at 274-281 amino acid residue of H5 hemagglutinin has been confirmed to be present all clade of H5N1 viruses. This study aimed at producing and evaluating the reactivity of a monospecific, polyclonal antibody against the epitope. The Antibody was produced by immunising a goat with the peptide in the form of multiple antigen peptide (MAP). The specificity of the antibody was estimated by assaying its reactivity against influenza virus subtypes H3N3, H4N4, H5N1, H6N5, H7N7, H9N2, H10N7 and H11N9; and recombinant hemagglutinins H1-H12, H14 and H15 with ELISA and immunoblot. The results of the assay showed that CNTKCQTP antibody was not specific for H5 haemagglutinin because it cross-reacted with other haemagglutinins especially H7, H8 and H9. The potential of the peptide containing the epitope, GNCNTKCQTPMGAINSS. as an ELISA reagent for assaying H5 antibodies in chickens previously vaccinated and challenged with the H5N1 virus was also evaluated in this study. In contrast, the results of previous studies, the ELISA using GNCNTKCQTPMGAINSS as coating antigen was not sensitive in detecting antibody to haemagglutinin H5 in chickens.</p><strong>Key Words: </strong>AI Virus, Hemagglutinin H5, CNTKCQTP Epitope, MAP, Immunoassa<em>y</em>

scholarly journals A membrane penetrating multiple antigen peptide (MAP) incorporating ovalbumin CD8 epitope induces potent immune responses in mice

2010 ◽  
Vol 1798 (12) ◽  
pp. 2286-2295 ◽  
Author(s):  
Nicole A. Brooks ◽  
Dodie S. Pouniotis ◽  
Kuo-Ching Sheng ◽  
Vasso Apostolopoulos ◽  
Geoffrey A. Pietersz
Keyword(s):  
Immune Responses ◽  
Multiple Antigen ◽  
Antigen Peptide ◽  
Multiple Antigen Peptide ◽  
Peptide Map

scholarly journals Multiple Antigen Peptide Vaccines against Plasmodium falciparum Malaria

2010 ◽  
Vol 78 (11) ◽  
pp. 4613-4624 ◽  
Author(s):  
Babita Mahajan ◽  
Jay A. Berzofsky ◽  
Robert A. Boykins ◽  
Victoria Majam ◽  
Hong Zheng ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Plasmodium Falciparum Malaria ◽  
Cellular Responses ◽  
Background Strain ◽  
Mouse Major Histocompatibility Complex ◽  
Multiple Antigen ◽  
Antigen Peptide ◽  
Multiple Antigen Peptide ◽  
Outbred Strain ◽  
Peptide Map

ABSTRACT The multiple antigen peptide (MAP) approach is an effective method to chemically synthesize and deliver multiple T-cell and B-cell epitopes as the constituents of a single immunogen. Here we report on the design, chemical synthesis, and immunogenicity of three Plasmodium falciparum MAP vaccines that incorporated antigenic epitopes from the sporozoite, liver, and blood stages of the life cycle. Antibody and cellular responses were determined in three inbred (C57BL/6, BALB/c, and A/J) strains, one congenic (HLA-A2 on the C57BL/6 background) strain, and one outbred strain (CD1) of mice. All three MAPs were immunogenic and induced both antibody and cellular responses, albeit in a somewhat genetically restricted manner. Antibodies against MAP-1, MAP-2, and MAP-3 had an antiparasite effect that was also dependent on the mouse major histocompatibility complex background. Anti-MAP-1 (CSP-based) antibodies blocked the invasion of HepG2 liver cells by P. falciparum sporozoites (highest, 95.16% in HLA-A2 C57BL/6; lowest, 11.21% in BALB/c). Furthermore, antibodies generated following immunizations with the MAP-2 (PfCSP, PfLSA-1, PfMSP-142, and PfMSP-3b) and MAP-3 (PfRAP-1, PfRAP-2, PfSERA, and PfMSP-142) vaccines were able to reduce the growth of blood stage parasites in erythrocyte cultures to various degrees. Thus, MAP-based vaccines remain a viable option to induce effective antibody and cellular responses. These results warrant further development and preclinical and clinical testing of the next generation of candidate MAP vaccines that are based on the conserved protective epitopes from Plasmodium antigens that are widely recognized by populations of divergent HLA types from around the world.

Multiple antigen peptide (MAP) system: Detailed study of immunogenic and antigenic properties

Peptides ◽  
1992 ◽  
pp. 893-894
Author(s):  
J. P. Briand ◽  
C. Barin ◽  
M. H. V. Van Regenmortel ◽  
S. Muller
Keyword(s):  
Multiple Antigen ◽  
Antigenic Properties ◽  
Antigen Peptide ◽  
Multiple Antigen Peptide ◽  
Peptide Map
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