Zinc-metalloproteases in insects: ACE and ECE

Macours, Nathalie; Hens, Korneel

doi:10.1016/j.ibmb.2004.03.007

Cited by 39 publications

(32 citation statements)

References 55 publications

(61 reference statements)

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“…In this species, feeding the ACE inhibitors captopril or lisinopril reduced, in a dosedependent manner, the size of the batch of eggs laid by females (Ekbote et al, 2003). It should be noted that many insects' ACE-like enzymes are not membranebound but secrete proteins (Macours and Hens, 2004;Yan et al, 2007).…”

Section: E Developmentmentioning

confidence: 90%

A Modern Understanding of the Traditional and Nontraditional Biological Functions of Angiotensin-Converting Enzyme

et al. 2012

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Section: E Developmentmentioning

confidence: 90%

A Modern Understanding of the Traditional and Nontraditional Biological Functions of Angiotensin-Converting Enzyme

et al. 2012

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“…ACE have been described as nonspecific dipeptydyl carboxypeptidases [28] and have been characterised in a number of insects, including Bombyx mori, D. melanogaster, L. migratoria, Musca domestica, and S. littoralis [29][30][31][32][33]. In insects, ACE are thought to be involved in regulating peptide hormones and neuropeptides by removing dipeptides, dipeptideamides and tripeptideamides from the C terminus of short peptides ( [31,32,34,35], reviewed in [36]). The matched protein identified here from pea aphid saliva is homologous to Drosophila ACE (Ance; AAF53353).…”

Section: Discussionmentioning

confidence: 99%

The secreted salivary proteome of the pea aphid Acyrthosiphon pisum characterised by mass spectrometry

et al. 2009

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Nine proteins secreted in the saliva of the pea aphid Acyrthosiphon pisum were identified by a proteomics approach using GE-LC-MS/MS and LC-MS/MS, with reference to EST and genomic sequence data for A. pisum. Four proteins were identified by their sequences: a homolog of angiotensin-converting enzyme (an M2 metalloprotease), an M1 zinc-dependant metalloprotease, a glucose-methanol-choline (GMC)-oxidoreductase and a homolog to regucalcin (also known as senescence marker protein 30). The other five proteins are not homologous to any previously described sequence and included an abundant salivary protein (represented by ACYPI009881), with a predicted length of 1161 amino acids and high serine, tyrosine and cysteine content. A. pisum feeds on plant phloem sap and the metalloproteases and regucalcin (a putative calcium-binding protein) are predicted determinants of sustained feeding, by inactivation of plant protein defences and inhibition of calcium-mediated occlusion of phloem sieve elements, respectively. The amino acid composition of ACYPI009881 suggests a role in the aphid salivary sheath that protects the aphid mouthparts from plant defences, and the oxidoreductase may promote gelling of the sheath protein or mediate oxidative detoxification of plant allelochemicals. Further salivary proteins are expected to be identified as more sensitive MS technologies are developed.

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“…Type IV pilusmediated secretion mutants could therefore more easily disseminate via the blood circulatory system. Although this theory may not explain the hypervirulent phenotype in the fly, it is interesting to note that D. melanogaster expresses several homologues of endothelin converting enzyme 1, the closest being neprilysin 3 (4,30). Two other observations are interesting in this respect.…”

Section: Discussionmentioning

confidence: 99%

Directed Screen of Francisella novicida Virulence Determinants Using Drosophila melanogaster

et al. 2010

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Francisella tularensis is a highly virulent, facultative intracellular human pathogen whose virulence mechanisms are not well understood. Occasional outbreaks of tularemia and the potential use of F. tularensis as a bioterrorist agent warrant better knowledge about the pathogenicity of this bacterium. Thus far, genome-wide in vivo screens for virulence factors have been performed in mice, all however restricted by the necessity to apply competition-based, negative-selection assays. We wanted to individually evaluate putative virulence determinants suggested by such assays and performed directed screening of 249 F. novicida transposon insertion mutants by using survival of infected fruit flies as a measure of bacterial virulence. Some 20% of the genes tested were required for normal virulence in flies; most of these had not previously been investigated in detail in vitro or in vivo. We further characterized their involvement in bacterial proliferation and pathogenicity in flies and in mouse macrophages. Hierarchical cluster analysis of mutant phenotypes indicated a functional linkage between clustered genes. One cluster grouped all but four genes of the Francisella pathogenicity island and other loci required for intracellular survival. We also identified genes involved in adaptation to oxidative stress and genes which might induce host energy wasting. Several genes related to type IV pilus formation demonstrated hypervirulent mutant phenotypes. Collectively, the data demonstrate that the bacteria in part use similar virulence mechanisms in mammals as in Drosophila melanogaster but that a considerable proportion of the virulence factors active in mammals are dispensable for pathogenicity in the insect model.

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Zinc-metalloproteases in insects: ACE and ECE

Cited by 39 publications

References 55 publications

A Modern Understanding of the Traditional and Nontraditional Biological Functions of Angiotensin-Converting Enzyme

A Modern Understanding of the Traditional and Nontraditional Biological Functions of Angiotensin-Converting Enzyme

The secreted salivary proteome of the pea aphid Acyrthosiphon pisum characterised by mass spectrometry

Directed Screen of Francisella novicida Virulence Determinants Using Drosophila melanogaster

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