Unknown

Dataset Information

0

Stable peptide inhibitors prevent binding of lethal and oedema factors to protective antigen and neutralize anthrax toxin in vivo.


ABSTRACT: The lethal and oedema toxins produced by Bacillus anthracis, the aetiological agent of anthrax, are made by association of protective antigen with lethal and oedema factors and play a major role in the pathogenesis of anthrax. In the present paper, we describe the production of peptide-based specific inhibitors in branched form which inhibit the interaction of protective antigen with lethal and oedema factors and neutralize anthrax toxins in vitro and in vivo. Anti-protective antigen peptides were selected from a phage library by competitive panning with lethal factor. Selected 12-mer peptides were synthesized in tetra-branched form and were systematically modified to obtain peptides with higher affinity and inhibitory efficiency.

SUBMITTER: Pini A 

PROVIDER: S-EPMC1409687 | biostudies-literature | 2006 Apr

REPOSITORIES: biostudies-literature

altmetric image

Publications

Stable peptide inhibitors prevent binding of lethal and oedema factors to protective antigen and neutralize anthrax toxin in vivo.

Pini Alessandro A   Runci Ylenia Y   Falciani Chiara C   Lelli Barbara B   Brunetti Jlenia J   Pileri Silvia S   Fabbrini Monica M   Lozzi Luisa L   Ricci Claudia C   Bernini Andrea A   Tonello Fiorella F   Dal Molin Federica F   Neri Paolo P   Niccolai Neri N   Bracci Luisa L  

The Biochemical journal 20060401 1


The lethal and oedema toxins produced by Bacillus anthracis, the aetiological agent of anthrax, are made by association of protective antigen with lethal and oedema factors and play a major role in the pathogenesis of anthrax. In the present paper, we describe the production of peptide-based specific inhibitors in branched form which inhibit the interaction of protective antigen with lethal and oedema factors and neutralize anthrax toxins in vitro and in vivo. Anti-protective antigen peptides we  ...[more]

Similar Datasets

| S-EPMC1986636 | biostudies-literature
| S-EPMC1307059 | biostudies-literature
| S-EPMC2891133 | biostudies-literature
| S-EPMC5666345 | biostudies-literature
| S-EPMC7012834 | biostudies-literature
| S-EPMC2892534 | biostudies-literature
| S-EPMC1808072 | biostudies-literature
| S-EPMC7458312 | biostudies-literature
| S-EPMC4519040 | biostudies-literature
| S-EPMC3527960 | biostudies-literature