@article{KressJarrinThuroffetal.2004,
  author    = {Kress, H. and Jarrin, A. and Thuroff, E. and Saunders, R. and Weise, C. and Schmidt am Busch, Marcel and Knapp, E. W. and Wedde, M. and Vilcinskas, Andreas},
  title     = {A Kunitz type protease inhibitor related protein is synthesized in Drosophila prepupal salivary glands and released into the moulting fluid during pupation},
  issn      = {0965-1748},
  year      = {2004},
  abstract  = {From the Drosophila virilis late puff region 31C, we microcloned two neighbouring genes, Kil-1 and Kil-2, that encode putative Kunitz serine protease inhibitor like proteins. The Kil-1 gene is expressed exclusively in prepupal salivary glands. Using a size mutant of the KIL-1 protein and MALDI-TOF analysis, we demonstrate that during pupation this protein is released from the prepupal salivary glands into the pupation fluid covering the surface of the pupa. 3-D- structure predictions are consistent with the known crystal structure of the human Kunitz type protease inhibitor 2KNT. This is the first experimental proof for the extra-corporal presence of a distinct Drosophila prepupal salivary gland protein. Possible functions of KIL-1 in the context of the control of proteolytic activities in the pupation fluid are discussed. (C) 2004 Elsevier Ltd. All rights reserved},
  language  = {en}
}
@article{ClermontWeddeSeitzetal.2004,
  author    = {Clermont, A. and Wedde, M. and Seitz, V. and Podsiadlowski, L. and Lenze, D. and Hummel, M. and Vilcinskas, Andreas},
  title     = {Cloning and expression of an inhibitor of microbial metalloproteinases from insects contributing to innate immunity},
  issn      = {0264-6021},
  year      = {2004},
  abstract  = {The first IMPI (inhibitor of metalloproteinases from insects) was identified in the greater wax moth, Galleria mellonella [Wedde, Weise, Kopacek, Franke and Vilcinskas (1998) Eur. J. Biochem. 255, 535-543]. Here we report cloning and expression of a cDNA coding for this IMPI. The IMPI mRNA was identified among the induced transcripts from a subtractive and suppressive PCR analysis after bacterial challenge of G. mellonella larvae. Induced expression of the IMPI during a Immoral immune response was confirmed by real-time PCR, which documented up to 500 times higher amounts of IMPI mRNA in immunized larvae in comparison with untreated ones. The IMPI sequence shares no similarity with those of tissue inhibitors of metalloproteinases or other natural inhibitors of metalloproteinases, and the recombinant IMPI specifically inhibits thermolysin-like metalloproteinases, but not matrix metalloproteinases. These results support the hypothesis that the IMPI represents a novel type of immune-related protein which is induced and processed during the G. mellonella humoral immune response to inactivate pathogen-associated thermolysin-like metalloproteinases},
  language  = {en}
}