Pre-exposure to yeast protects larvae of Galleria mellonella from a subsequent lethal infection by Candida albicans and is mediated by the increased expression of antimicrobial peptides

被引:129
作者
Bergin, David
Murphy, Lisa
Keenan, Joanne
Clynes, Martin
Kavanagh, Kevin [1 ]
机构
[1] Natl Univ Ireland, NICB, Dept Biol, Med Mycol Unit, Maynooth, Kildare, Ireland
[2] Dublin City Univ, Natl Inst Cellular Biotechnol, Dublin 9, Ireland
关键词
Galleria mellonella; antimicrobial proteins; host defence; 2D gel electrophoresis; MALDI TOF analysis; gene expression;
D O I
10.1016/j.micinf.2006.03.005
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
Pre-exposure of the larvae of Galleria mellonella to Candida albicans or Saccharomyces cerevisiae protects against a subsequent infection with 10(6) C. albicans cells. This protection can also be induced by exposing larvae to glucan or laminarin prior to the administration of the potentially lethal inoculum. Analysis of the genes coding for galiomicin, a defensin in G. mellonella, a cysteine-rich antifungal peptide gallerimycin, an iron-binding protein transferrin and an inducible metalloproteinase inhibitor (IMPI) from G. mellonella demonstrated increased expression, which is at its highest after 24 h of the initial inoculum. Examination of the expression of proteins in the insect haemolymph using 2D electrophoresis and MALDI TOF analysis revealed an increased expression of a number of proteins associated with the insect immune response to infection 24 h after the initial exposure. This study demonstrates that the larvae of G. mellonella can withstand a lethal inoculum of C. albicans if pre-exposed to a non-lethal dose of yeast or polysaccharide 24 h previously which is mediated by increased expression of a number of antimicrobial peptides and the appearance of a number of peptides in the challenged larvae. (c) 2006 Elsevier SAS. All rights reserved.
引用
收藏
页码:2105 / 2112
页数:8
相关论文
共 30 条
[1]   A family of fibrinogen-related proteins that precipitates parasite-derived molecules is produced by an invertebrate after infection [J].
Adema, CM ;
Hertel, LA ;
Miller, RD ;
Loker, ES .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (16) :8691-8696
[2]  
BOMAN HG, 1981, TRENDS BIOCHEM SCI, V6, P306, DOI 10.1146/annurev.mi.41.100187.000535
[3]   Immune response of Drosophila melanogaster to infection with the flagellate parasite Crithidia spp. [J].
Boulanger, N ;
Ehret-Sabatier, L ;
Brun, R ;
Zachary, D ;
Bulet, P ;
Imler, JL .
INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY, 2001, 31 (02) :129-137
[4]  
Brennan M, 2002, FEMS IMMUNOL MED MIC, V34, P153, DOI 10.1111/j.1574-695X.2002.tb00617.x
[5]   Antimicrobial peptides in insects; structure and function [J].
Bulet, P ;
Hetru, C ;
Dimarcq, JL ;
Hoffmann, D .
DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY, 1999, 23 (4-5) :329-344
[6]   Cloning and expression of an inhibitor of microbial metalloproteinases from insects contributing to innate immunity [J].
Clermont, A ;
Wedde, M ;
Seitz, V ;
Podsiadlowski, L ;
Lenze, D ;
Hummel, M ;
Vilcinskas, A .
BIOCHEMICAL JOURNAL, 2004, 382 :315-322
[7]  
Cotter G, 2000, FEMS IMMUNOL MED MIC, V27, P163, DOI 10.1111/j.1574-695X.2000.tb01427.x
[8]   Lipopolysaccharide interaction with hemolin, an insect member of the Ig-superfamily [J].
Daffre, S ;
Faye, I .
FEBS LETTERS, 1997, 408 (02) :127-130
[9]   Drosophila melanogaster larval hemolymph protein mapping [J].
Guedes, SD ;
Vitorino, R ;
Tomer, K ;
Domingues, MRM ;
Correia, AJF ;
Amado, F ;
Domingues, P .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2003, 312 (03) :545-554
[10]   Toll-like receptors and their function in innate and adaptive immunity [J].
Heine, H ;
Lien, E .
INTERNATIONAL ARCHIVES OF ALLERGY AND IMMUNOLOGY, 2003, 130 (03) :180-192