Activities of temporin family peptides against the chytrid fungus (Batrachochytrium dendrobatidis) associated with global amphibian declines.
Temporin A and structurally related peptides produced in amphibian dermal granular glands and in wasp venom were tested for growth inhibition of Batrachochytrium dendrobatidis, a pathogen associated with global amphibian declines. Two natural amphibian temporins, a wasp temporin, and six synthetic analogs effectively inhibited growth. Differences in potency due to amino acid substitution suggest that ability to penetrate membranes and form an alpha-helical structure is important for their effectiveness against this pathogen.
Rollins-Smith
Louise A
LA
Department of Microbiology and Immunology, Vanderbilt University Medical Center, Nashville, Tennessee 37232, USA. louise.rollins-smith@vanderbilt.edu
Carey
Cynthia
C
Conlon
J Michael
JM
Reinert
Laura K
LK
Doersam
Jennifer K
JK
Bergman
Tomas
T
Silberring
Jerzy
J
Lankinen
Hilkka
H
Wade
David
D
D019943:Amino Acid Substitution; D000663:Amphibians / Q000382:microbiology*; D000820:Animal Diseases / Q000635:transmission*; D000818:Animals; D000890:Anti-Infective Agents / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides; D005658:Fungi / Q000187:drug effects* / Q000254:growth & development; D008826:Microbial Sensitivity Tests; D009181:Mycoses / Q000635:transmission / Q000662:veterinary*; D011153:Population; D011506:Proteins / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*; D014862:Wasp Venoms / Q000737:chemistry
D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D011506:Proteins; D014862:Wasp Venoms; C104501:temporin