TY - JOUR
T1 - Purification, characterization, and cDNA cloning of an antifungal protein from the hemolymph of Sarcophaga peregrina (flesh fly) larvae
AU - Iijima, Ryosuke
AU - Kurata, Shoichiro
AU - Natori, Shunji
PY - 1993/6/5
Y1 - 1993/6/5
N2 - An antifungal protein (AFP) was purified from the hemolymph of third instar larvae of Sarcophaga peregrina. This protein repressed the growth of Candida albicans in Sabouraud medium in the presence of nitrofurazone. However, in distilled water or saline, AFP alone killed C. albicans. Significant synergism was detected between AFP and sarcotoxin IA, an antibacterial protein of Sarcophaga. The lethal effect of AFP on C. albicans was greatly enhanced by the presence of a small amount of sarcotoxin IA. AFP was shown to bind to C. albicans and cause leakage of a substance(s) with absorbance at 260 nm from the cells. Analysis of its cDNA showed that AFP is a novel histidine-rich protein consisting of 67 amino acid residues. * This work was supported by a Grant-in-Aid for Specially Promoted Research from the Ministry of Education, Science and Culture of Japan and by Grant-in-Aid BMP 93-IV-2-5 (Bio-Media Program) from the Ministry of Agriculture, Forestry, and Fisheries of Japan. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
AB - An antifungal protein (AFP) was purified from the hemolymph of third instar larvae of Sarcophaga peregrina. This protein repressed the growth of Candida albicans in Sabouraud medium in the presence of nitrofurazone. However, in distilled water or saline, AFP alone killed C. albicans. Significant synergism was detected between AFP and sarcotoxin IA, an antibacterial protein of Sarcophaga. The lethal effect of AFP on C. albicans was greatly enhanced by the presence of a small amount of sarcotoxin IA. AFP was shown to bind to C. albicans and cause leakage of a substance(s) with absorbance at 260 nm from the cells. Analysis of its cDNA showed that AFP is a novel histidine-rich protein consisting of 67 amino acid residues. * This work was supported by a Grant-in-Aid for Specially Promoted Research from the Ministry of Education, Science and Culture of Japan and by Grant-in-Aid BMP 93-IV-2-5 (Bio-Media Program) from the Ministry of Agriculture, Forestry, and Fisheries of Japan. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
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M3 - Article
C2 - 8505329
AN - SCOPUS:0027157001
SN - 0021-9258
VL - 268
SP - 12055
EP - 12061
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 16
ER -