Acanthoscurrin: a novel glycine-rich antimicrobial peptide constitutively expressed in the hemocytes of the spider Acanthoscurria gomesiana.
We report the isolation of a novel antimicrobial peptide, acanthoscurrin, from the hemocytes of unchallenged tarantula spider Acanthoscurria gomesiana. A combination of Edman degradation, mass spectrometry and cDNA cloning revealed the presence of two isoforms of acanthoscurrin, differing by two glycine residues. Both displayed cationic properties and a high percentage of glycine residues. However, acanthoscurrins have no structural similarities with already known glycine-rich antimicrobial peptides from animals and plants. As deduced from cDNA cloning and mass spectrometry, the amino acid sequence of acanthoscurrin begins with a putative signal peptide of 23 amino acids followed by the mature peptide, which is post-translationally modified by a C-terminal amidation. Acanthoscurrins are constitutively expressed in hemocytes and released to plasma following an immune challenge.
Lorenzini
Daniel M
DM
Departamento de Parasitologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, Av. Prof. Lineu Prestes, 1374, CEP 05508-900, São Paulo, Brazil.
da Silva
Pedro I
PI
Fogaça
Andréa C
AC
Bulet
Philippe
P
Daffre
Sirlei
S
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002851:Chromatography, High Pressure Liquid; D006434:Hemocytes / Q000378:metabolism*; D007113:Immunity, Innate / Q000235:genetics* / Q000502:physiology; D019476:Insect Proteins / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D008969:Molecular Sequence Data; D010455:Peptides / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D020133:Reverse Transcriptase Polymerase Chain Reaction; D013112:Spiders / Q000235:genetics* / Q000378:metabolism
D019476:Insect Proteins; D010455:Peptides; C483971:acanthoscurrin 1 protein, Acanthoscurria gomesiana; C483972:acanthoscurrin 2 protein, Acanthoscurria gomesiana