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Anti‐HIV‐1 activity of indolicidin, an antimicrobial peptide from neutrophils
Author(s) -
Robinson W. Edward,
McDougall Brenda,
Tran Dat,
Selsted Michael E.
Publication year - 1998
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1002/jlb.63.1.94
Subject(s) - biology , peptide , lysis , in vitro , antimicrobial , biological activity , antimicrobial peptides , biochemistry , cytoplasm , membrane , microbiology and biotechnology
Abstract Indolicidin is a tridecapeptide amide isolated from the cytoplasmic granules of bovine neutrophils. It has potent, broad spectrum microbicidal activities in vitro that are thought to be related to the membrane‐disruptive properties of the peptide. Based on the putative membrane‐targeted mode of action, we postulated that indolicidin would be active against HIV‐1, an enveloped virus. Indolicidin was reproducibly virucidal against HIV‐1 at a concentration of 333 μg/mL (174 μM) with a 50% inhibitory dose between 67 and 100 μg/mL. At 37°, killing was rapid with >50% killing of HIV occurring within 5 min, and nearly 100% viral inactivation achieved by 60 min. The anti‐HIV activity of indolicidin was temperature‐sensitive, a finding consistent with a membrane‐mediated antiviral mechanism. Parallel experiments revealed that indolicidin lysed cultured lymphoblastoid cells at concentrations similar to those required for antiviral activity. However, a des‐R13‐amide indolicidin analog (R12‐OH), previously shown to have less antibacterial activity than indolicidin, was significantly less active against HIV and was non‐toxic to lymphoid target cells at concentrations up to 333 μg/mL, the highest level tested. J. Leukoc. Biol . 63: 94–100; 1998.