A Kunitz type protease inhibitor related protein is synthesized in Drosophila prepupal salivary glands and released into the moulting fluid during pupation

Kress, Horst; Jarrin, Andres; Thüroff, Eduardo; Saunders, Robert D. C.; Weise, Christoph; Busch, Marcel Schmidt am; Knapp, Ernst-W; Wedde, Marianne; Vilcinskas, Andreas

doi:10.1016/j.ibmb.2004.05.006

Cited by 22 publications

(11 citation statements)

References 53 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The phenotypes that we observed for ectopic expression of the predicted protease inhibitors CG9334 (serpin) and CG10284 (Kunitz protease inhibitor; Kress et al 2004; as well as a cysteine-rich secretory protein; Mueller et al 2004) and a predicted protease, CG6168, suggest that Acp proteolysis regulators play important functions in the immunity of mated females. Two previous studies of D. melanogaster immune genes support our results.…”

Section: Resultsmentioning

confidence: 84%

An Ectopic Expression Screen Reveals the Protective and Toxic Effects of Drosophila Seminal Fluid Proteins

Mueller¹,

2007

View full text Add to dashboard Cite

In Drosophila melanogaster, seminal fluid regulates the reproductive and immune responses of mated females. Some seminal fluid proteins may provide protective functions to mated females, such as antimicrobial activity and/or stimulation of antimicrobial gene expression levels, while others appear to have negative effects, contributing to a ''cost of mating.'' To identify seminal proteins that could participate in these phenomena, we used a systemic ectopic expression screen to test the effects on unmated females of proteins normally produced by the male accessory gland (Acps). Of the 21 ectopically expressed Acps that we tested for ability to assist in the clearance of a bacterial infection with Serratia marcescens, 3 Acps significantly reduced the bacterial counts of infected females, suggesting a protective role. Of the 23 Acps that we tested for toxicity, 3 were toxic, including one that has been implicated in the cost of mating in another study. We also tested ectopic expression females for other Acp-induced effects, but found no additional Acps that affected egg laying or receptivity upon ectopic expression.

show abstract

Section: Resultsmentioning

confidence: 84%

An Ectopic Expression Screen Reveals the Protective and Toxic Effects of Drosophila Seminal Fluid Proteins

Mueller¹,

2007

View full text Add to dashboard Cite

show abstract

“…Interestingly, serine proteases have been shown to be involved in the control of molting and larval development in insects (79 -84). In addition, Kunitz-type serine protease inhibitors are constituents of the molting fluid in D. melanogaster where they are believed to control enzymes involved in tissue remodeling (85). Recently, using genome wide RNAi screening, it has been shown that serine protease inhibitors containing the Kunitz/bovine pancreatic trypsin inhibitor domains are also essential for molting in C. elegans (77).…”

Section: Discussionmentioning

confidence: 99%

Characterization of a Novel Filarial Serine Protease Inhibitor, Ov-SPI-1, from Onchocerca volvulus, with Potential Multifunctional Roles during Development of the Parasite

Ford

Guiliano

Oksov

et al. 2005

Journal of Biological Chemistry

View full text Add to dashboard Cite

A novel filarial serine protease inhibitor (SPI) from the human parasitic nematode Onchocerca volvulus, Ov-SPI-1, was identified through the analysis of a molting third-stage larvae expressed sequence tag dataset. Subsequent analysis of the expressed sequence tag datasets of O. volvulus and other filariae identified four other members of this family. These proteins are related to the low molecular weight SPIs originally isolated from Ascaris suum where they are believed to protect the parasite from host intestinal proteases. The two Ov-spi transcripts are up-regulated in the molting larvae and adult stages of the development of the parasite. Recombinant Ov-SPI-1 is an active inhibitor of serine proteases, specifically elastase, chymotrypsin, and cathepsin G. Immunolocalization of the Ov-SPI proteins demonstrates that the endogenous proteins are localized to the basal layer of the cuticle of third-stage, molting third-stage, and fourth-stage larvae, the body channels and multivesicular bodies of third-stage larvae and the processed material found between the two cuticles during molting. In O. volvulus adult worms the Ov-SPI proteins are localized to the sperm and to eggshells surrounding the developing embryos. RNA interference targeting the Ov-spi genes resulted in the specific knockdown of the transcript levels of both Ov-spi-1 and Ov-spi-2, a loss of native proteins, and a significant reduction in both molting and viability of third-stage larvae. We suggest the Ov-SPI proteins play a vital role in nematode molting by controlling the activity of an endogenous serine protease(s). The localization data in adults also indicate that these inhibitors may be involved in other processes such as embryogenesis and spermatogenesis.The cuticle is an extracellular hydroskeleton that overlays the hypodermis of all nematodes. Most nematodes molt their cuticles four times during pre-adult development. Although being fairly inert and structurally robust, the cuticle is also permeable to small compounds and expands during growth periods between molts (1). A number of enzymes have been implicated in the shedding of old cuticles and the remodeling process that occurs as the new cuticle develops (2-8). Proteolytic enzymes have been shown to play a vital role in these processes, and inhibitor studies and rational cloning strategies have identified several nematode proteases whose functions are required for molting (9 -11).To identify novel filarial proteins involved in the molting process, we adopted a transcriptomics approach. Thousands of expressed sequence tags (ESTs) 4 have been sequenced from cDNA libraries constructed from the infective third-stage larvae (L3) and molting L3 (mL3) of the human filarial nematode Onchocerca volvulus (12, 13). Analysis of these datasets identified novel cysteine proteases involved in the molting process (14,15). Also identified in these analyses was an O. volvulus small molecular weight serine protease inhibitor (SPI) with similarities to other nematode SPI; Ascaris suum chymotrypsin/elastase in...

show abstract

“…Kazal and Kunitz type inhibitors share intra-domain disulfide cross-links determined by six conserved cystein residues. 59,60 Interestingly, all three serine proteinase inhibitors purified from immunized G. mellonella larvae were found to inhibit the trypsin-like proteinase (Pr2) produced by M. anisopliae, and ISPI-3 was also active against the chymoelastase secreted by this fungus. 58 These findings and our observation that inducible proteinase inhibitors in the hemolymph of G. mellonella inhibit both fungal proteases and fungal development in the host lend some credit to our hypothesis that low molecular mass proteinase inhibitors participate in antifungal defense in G. mellonella by inactiviation of secreted fungal proteinases thereby preventing host defense molecules from degradation.…”

Section: Coevolution Between Fungal Proteinases and Host Proteinase Imentioning

confidence: 99%

“…For example, Kunitz-type inhibitors from insects seem to exert pleiotropic roles associated either with tissue remodeling during metamorphosis or with antimicrobial defense. 59 The IMPI mentioned above represents a unique example for an inhibitor with pleiotropic roles in immunity and development. Its gene is expressed during innate immune responses and during pupation when histolysis of larval tissues occurs in G. mellonella.…”

Section: Coevolution Between Fungal Proteinases and Host Proteinase Imentioning

confidence: 99%

Coevolution between pathogen-derived proteinases and proteinase inhibitors of host insects

Vilcinskas¹

2010

Virulence

Self Cite

View full text Add to dashboard Cite

Virulence is thought to coevolve as a result of reciprocal selection between pathogens and their hosts. This paper focuses on coevolution between microbial proteinases operating as virulence factors and host defense molecules of insects. Owing to shorter generation times and smaller genomes, microbes exhibit a high evolutionary adaptability in comparison with their hosts. Indeed, the latter can only compete with pathogens if they evolve mechanisms providing a comparable genetic plasticity. Gene or domain duplication and shuffling by recombination is the driving force behind the countermeasures in host defense effectors. Recent literature provides evidence for both diversifications of fungal proteinases involved in pathogenesis and expansion host proteinase inhibitors subsets contributing to insect innate immunity. For example, the pathogen-associated spectrum of proteolytic enzymes encompasses thermolysin-like metalloproteinases that putatively promoted the evolution of corresponding host inhibitors of these virulence factors which complement the insect repertoire of antimicrobial defense molecules. Beyond mutual diversification of effector molecules coevolution resulted also in sophisticated molecular adaptations of host insects such as sensing and feedback-loop regulation of microbial metalloproteinases and corresponding countermeasures of pathogens providing evasion of host immunity induced by these virulence factors

show abstract

A Kunitz type protease inhibitor related protein is synthesized in Drosophila prepupal salivary glands and released into the moulting fluid during pupation

Cited by 22 publications

References 53 publications

An Ectopic Expression Screen Reveals the Protective and Toxic Effects of Drosophila Seminal Fluid Proteins

An Ectopic Expression Screen Reveals the Protective and Toxic Effects of Drosophila Seminal Fluid Proteins

Characterization of a Novel Filarial Serine Protease Inhibitor, Ov-SPI-1, from Onchocerca volvulus, with Potential Multifunctional Roles during Development of the Parasite

Coevolution between pathogen-derived proteinases and proteinase inhibitors of host insects

Contact Info

Product

Resources

About