Sequence and function of lysosomal and digestive cathepsin D-like proteinases of Musca domestica midgut

Padilha, Marcelo Henrique Peteres; Pimentel, André C.; Ribeiro, Alberto F.; Terra, Walter R.

doi:10.1016/j.ibmb.2009.09.003

Cited by 57 publications

(50 citation statements)

References 36 publications

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“…Only in some Coleoptera and cyclorrhaphous Diptera the digestive part of the midgut possesses an acidic pH of 5.4e6.9 and 3.1e6.8, respectively (Terra and Ferreira, 1994). In these insects, cysteine and aspartate proteases are secreted into the lumen of the midgut as major digestive enzymes (Thie and Houseman, 1990;Cristofoletti et al, 2005;Padilha et al, 2009). In the triatomine R. prolixus, according to pH determinations via pH indicators the pH value alternates feedingdependently between 5.5 and 7.4 (J. M. C. Ribeiro and E. S. Garcia, personal communication).…”

Section: Discussionmentioning

confidence: 99%

“…However, this difference is apparently sufficient to branch TiCatD far from all protein sequences containing this motif in the cladogram. The proline loop was suggested to be a motif found in lysosomal cathepsin D-like enzymes which are not secreted into the lumen of the digestive tract (Padilha et al, 2009). Enzymes which are lacking this motif like ppCAD3 from M. domestica are therefore luminal digestive enzymes.…”

Section: Discussionmentioning

confidence: 99%

“…In T. brasiliensis only the pH value of the stomach in the first 24 h after blood feeding was measured. The possible involvement in intestinal immune reactions is also supported by the synergistic action of lysozymes and cathepsin D-like proteases in the digestion of bacteria in the region of the gut of the housefly larva with an acidic pH (Espinoza-Fuentes and Terra, 1987;Padilha et al, 2009). In triatomines, investigations on the interaction of digestive proteases in the gut with symbionts or the pathogen T. cruzi are of high impact for understanding how microorganisms establish in this harsh environment, and further efforts to elucidate this interplay are indispensable.…”

Section: Discussionmentioning

confidence: 99%

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Intestinal aspartate proteases TiCatD and TiCatD2 of the haematophagous bug Triatoma infestans (Reduviidae): Sequence characterisation, expression pattern and characterisation of proteolytic activity

Balczun

Siemanowski

Pausch

et al. 2012

Insect Biochemistry and Molecular Biology

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Intestinal aspartate proteases TiCatD and TiCatD2 of the haematophagous bug Triatoma infestans (Reduviidae): Sequence characterisation, expression pattern and characterisation of proteolytic activity

Balczun

Siemanowski

Pausch

et al. 2012

Insect Biochemistry and Molecular Biology

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“…Especially a homologue lysozyme enzyme working at a low pH which is capable of breaking down the peptidoglycan layer in the cell wall of Gram-positive bacteria may be involved (Lemos et al, 1993). However, a number of other enzymes have also been isolated from the M. domestica mid gut (Padilha et al, 2009). Another explanation for the reduction inside the larvae could be bacterial antagonisms exerted by the microbial flora from the manure, because no reduction was reported when gnotobiotic larvae were reared in media without competing microorganisms (Greenberg and Klowden, 1972); however, autoclaving the manure did not affect the elimination in another study (Erickson et al, 2004).…”

Section: Journal Of Insects As Food and Feed 3(2) 151mentioning

confidence: 99%

Reduction of Escherichia coli, Salmonella Enteritidis and Campylobacter jejuni in poultry manure by rearing of Musca domestica fly larvae

Nordentoft

Fischer

Bjerrum

et al. 2017

JIFF

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A major barrier for using animal waste as substrate for production of insects for feed or food is the concern for safety of the end products. In this study we investigated how rearing of fly larvae of Musca domestica in poultry manure influenced the counts of three pathogenic test strains (Escherichia coli, Salmonella Enteritidis and Campylobacter jejuni) and investigated whether these were transferred from manure to larvae, pupae or adults flies. We monitored quantitative microbiological changes over a study period of seven days. We showed that the decay in the numbers of E. coli, S. Enteritidis, and C. jejuni was faster in manure with rearing of fly larvae than in manure without larvae; an 8 log10 reduction of all three test bacteria was observed within four days in manure with larvae; compared to manure without larvae where a 1 to 2 log10 was observed. We found no sign of propagation of the pathogens in the larvae gut. All test strains were detectable in low numbers at day 4 in the larvae gut but only C. jejuni survived until day 7. In the pupae, only S. Enteritidis was detectable at day 3, and no test strains were found later than day 3. None of the test strain was isolated from adult flies. The total aerobic bacterial count remained at a high level throughout the study both in manure, in larvae and in pupae. In conclusion, our results showed that elimination of the pathogens from the manure was accelerated by larvae rearing, but were still detectable at low number in the larvae gut until end of the larvae stage. This study provides data for evaluation of feed safety of fly larvae reared on animal waste. Furthermore suggests a potential use for reduction of these pathogens in manure.

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“…These types of peptidases develop their maximum activity under alkaline to neutral pH conditions [2]. In some insect groups the intestinal lumen is acidic and the digestion switched to cysteine-like proteinases such as cathepsin D or L [3,4]. Some Coleoptera groups (e.g.…”

Section: Editorialmentioning

confidence: 99%

Pathways of Insect Protein Digestion: Triatominae (Kissing Bugs)

Waniek¹

2014

Entomol Ornithol Herpetol

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EditorialThe majority of insects use serine proteinases like trypsin and chymotrypsin as main enzymes to digest their food [1]. These types of peptidases develop their maximum activity under alkaline to neutral pH conditions [2]. In some insect groups the intestinal lumen is acidic and the digestion switched to cysteine-like proteinases such as cathepsin D or L [3,4]. Some Coleoptera groups (e.g. Bruchidae, Tenebrionidae) developed a digestive system based on such proteinases [2,5]. But the major group using acid proteinases are the Hemiptera. This taxon uses cysteine proteinases because ancestral groups were using plant seeds containing serine proteinases inhibitors as a food source and therefore had to evolve their digestive system [6,7]. The conquest of this food source was a challenge for the digestive system [8] but it certainly contributed to the success of this insect group opening up new niches.One of the best analyzed hemipteran groups considering their digestion is the Triatominae (Heteroptera, Reduviidae) subfamily. Many species of this group -especially from the genera Triatoma, Rhodnius and Panstrongylus [9] -are medically important because they are able to transmit Trypanosoma cruzi (Kinetoplastida, Trypanosomatidae), the causative agent of Chagas disease [10]. In contrast to mosquitoes which develop from egg to adult in few weeks and frequently show low rates of parasitic infection, some long-lived triatomine species needs several months to complete their life cycle [1]. Besides this, kissing bugs takes huge amounts of blood from their vertebrate host at each nymph stage and, consequently usually show higher infection rates (up to about 80%) [1,[11][12][13][14][15]. In this insect group several digestive enzymes and their respective genes were identified and characterized. In the beginning of the 1980s activities of cathepsin B and D, aminopeptidase and carboxypeptidase have been shown [16,17]. Later, when the appropriate molecular biology methods were available, different isoforms of genes from different triatomine species have been identified encoding cathepsin B, L and D and serine carboxypeptidase [18][19][20][21][22]. At the same time Borges et al. [23] have demonstrated a significant increase of cathepsin D activity in Rhodnius prolixus infected with T. cruzi. However, despite the numerous studies concerning the Triatominae, many questions about their digestive system and its interactions with the parasite are still unanswered. For example, it is quite possible that there are further types of luminal digestive enzymes waiting to be discovered in triatomines. A recent transcriptome analysis of the R. prolixus intestine has revealed many genes related to digestive physiology including digestive enzymes lacking some amino acid residues important for enzymatic activity [24]. Furthermore, it would be very important to know whether or not microbiota plays a role in the digestion of triatomines and how strong the influence of T. cruzi on the digestive system might be. It would also be interesting ...

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Sequence and function of lysosomal and digestive cathepsin D-like proteinases of Musca domestica midgut

Cited by 57 publications

References 36 publications

Intestinal aspartate proteases TiCatD and TiCatD2 of the haematophagous bug Triatoma infestans (Reduviidae): Sequence characterisation, expression pattern and characterisation of proteolytic activity

Intestinal aspartate proteases TiCatD and TiCatD2 of the haematophagous bug Triatoma infestans (Reduviidae): Sequence characterisation, expression pattern and characterisation of proteolytic activity

Reduction of Escherichia coli, Salmonella Enteritidis and Campylobacter jejuni in poultry manure by rearing of Musca domestica fly larvae

Pathways of Insect Protein Digestion: Triatominae (Kissing Bugs)

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