Antibacterial activity of peptides derived from envelope glycoproteins of HIV-1.
Recent reports have highlighted the anti-HIV-1 activities of defensins, whose structure and charge resemble portions of the HIV-1 transmembrane envelope glycoprotein gp41. The current report explores the obverse, whether peptides derived from HIV-1 envelope glycoproteins can exert antimicrobial activity. Fifteen-residue peptides spanning the entire sequence of HIV-1(MN) gp120 and gp41 were subjected to radial diffusion assays against laboratory strains of Escherichia coli and Listeria monocytogenes. Twenty-four active peptides corresponded predominantly to membrane-active domains of gp120 and gp41. Several peptides retained significant activity in higher ionic conditions and may serve as templates for the development of novel peptide antibiotics. The strategies employed herein could uncover additional antimicrobial peptides from envelope proteins of other lytic viruses.
Cole
Alexander M
AM
Department of Medicine, Division of Pulmonary and Critical Care Medicine, UCLA School of Medicine, 10833 Le Conte Ave., Room CHS 37-055, Los Angeles, CA 90095-1690, USA. acole@mednet.ucla.edu
Liao
Hsiang-I
HI
Ganz
Tomas
T
Yang
Otto O
OO
D000595:Amino Acid Sequence; D004926:Escherichia coli / Q000187:drug effects*; D015699:HIV Envelope Protein gp120 / Q000737:chemistry; D015700:HIV Envelope Protein gp41 / Q000737:chemistry; D015497:HIV-1 / Q000737:chemistry*; D008089:Listeria monocytogenes / Q000187:drug effects*; D008826:Microbial Sensitivity Tests; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000494:pharmacology*; D017434:Protein Structure, Tertiary / Q000502:physiology; D013329:Structure-Activity Relationship; D014759:Viral Envelope Proteins / Q000737:chemistry*
D015699:HIV Envelope Protein gp120; D015700:HIV Envelope Protein gp41; D010446:Peptide Fragments; D014759:Viral Envelope Proteins