Morphological and enzymatic analysis of the midgut of Anopheles darlingi during blood digestion

Okuda, K; Caroci, Abrahim de Souza; Ribolla, Paulo Eduardo Martins; Marinotti, Osvaldo; Bianchi, A.G. de; Bijovsky, A. Tania

doi:10.1016/j.jinsphys.2005.03.010

Cited by 35 publications

(23 citation statements)

References 33 publications

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“…Such proteolytic mechanisms are highly regulated and are involved in a variety of physiologic processes, such as programmed cell death, stress responses (heat shock and anoxia), skeletal muscle atrophy, cellcell recognition, signal transduction and learning, morphogenesis, and photoreceptor light adaptation (Mykles 1998). Different classes of proteases such as cysteine proteases, metalloproteases and serino proteases have been described both in adults and larvae of several species of the Diptera (Han et al 1997, Rosenfeld & Vanderberg 1998, Cho et al 1999, Noriega et al 2002, Vierstraete et al 2003, Okuda et al 2005, Fazito do Vale et al 2007, Pires et al 2007, Rodrigues et al 2007). Despite the existence of information about morphology, taxonomy and ecology of this genus, as far as we know, no data has been published on the biochemical traits of O. thornax.…”

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confidence: 99%

Serine protease activities in Oxysarcodexia thornax (Walker) (Diptera: Sarcophagidae) first instar larva

Cuervo¹,

Mesquita-Rodrigues²,

d’Avila-Levy³

et al. 2008

Mem. Inst. Oswaldo Cruz

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We report for the first time the expression of multiple protease activities in the first instar larva (L1) of the flesh fly Oxysarcodexia thornax (Walker). Zymographic analysis of homogenates from freshly obtained L1 revealed a complex proteolytic profile ranging from 21.5 to 136 kDa. Although some activities were detected at pH 3.5 and 5.5, the optimum pH for most of the proteolytic activities was between pH 7.5 and 9.5. Seven of 10 proteases were completely inactivated by phenyl-methyl sulfonyl-fluoride, suggesting that main proteases expressed by L1 belong to serine proteases class. Complete inactivation of all enzymatic activities was obtained using N-p-Tosyl-L-phenylalanine chloromethyl ketone (100 µM), a specific inhibitor of chymotrypsin-like serine proteases.Keywords: Oxysarcodexia thornax -Sarcophagidae -chymotrypsin-like serine proteasesThe genus Oxysarcodexia belongs to the Sarcophagidae family (flesh flies) whose major biological feature is the ovo-larvipary (Pape 1996). Females may deposit first instar larvae directly onto the vertebrate host at predisposing sites (causing secondary myiasis), carcasses, decomposing organic matter, and dung (Panu et al. 2000). Genus Oxysarcodexia is widely distributed in the Neotropical regions (Lopes 1946), and in Brazil, O. thornax (Walker) is found in both urban and rural areas of several states. This species is abundant in the state of Rio de Janeiro, occurring preferentially in the summer season, with the population peak between January and February (Oliveira et al. 2002).In biological systems, proteases may carry out (i) a regulatory function by activation or inactivation of specific proteins via selective proteolysis, and (ii) a nonspecific proteolytic function involved in general protein hydrolysis. Such proteolytic mechanisms are highly regulated and are involved in a variety of physiologic processes, such as programmed cell death, stress responses (heat shock and anoxia), skeletal muscle atrophy, cellcell recognition, signal transduction and learning, morphogenesis, and photoreceptor light adaptation (Mykles 1998). Different classes of proteases such as cysteine proteases, metalloproteases and serino proteases have been described both in adults and larvae of several species of the Diptera (Han et al. 1997, Rosenfeld & Vanderberg 1998, Cho et al. 1999, Noriega et al. 2002, Vierstraete et al. 2003, Okuda et al. 2005, Fazito do Vale et al. 2007, Pires et al. 2007, Rodrigues et al. 2007). Despite the existence of information about morphology, taxonomy and ecology of this genus, as far as we know, no data has been published on the biochemical traits of O. thornax. In the present study, the proteolytic profile of O. thornax first instar larvae was investigated using zymographic analysis. O. thornax adults were collected as previously described (Oliveira et al. 2002) and females were kept in a 50 ml plastic vial for 24 h at room temperature. Following death of the females, abundant live first instar larvae (L1) were released and immediately collected. Larvae were ...

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confidence: 99%

Serine protease activities in Oxysarcodexia thornax (Walker) (Diptera: Sarcophagidae) first instar larva

Cuervo¹,

Mesquita-Rodrigues²,

d’Avila-Levy³

et al. 2008

Mem. Inst. Oswaldo Cruz

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“…stephensi (Freyvogel and Staubli, 1965), An. darlingi (Okuda et al, 2005), the PM developed 18,30,30,36,13,32,18 h PBM, respectively. Compared to other mosquitoes, such as Culex tarsalis (Freyvogel and Staubli, 1965), Cx.…”

Section: Discussionmentioning

confidence: 91%

Peritrophic membrane structure of Aedes aegypti (Diptera: Culicidae) mosquitoes after infection with dengue virus type 2 (D2-16681)

Suwanmanee¹,

Chaisri²,

Wasinpiyamongkol

et al. 2009

Appl. Entomol. Zool.

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The peritrophic membrane (PM) is a non-cellular tissue involved in the protection of midgut epithelium from mechanical damage and insults from pathogens. This study was carried out to determine the involvement of PM in mosquitoes after infection with dengue virus. Aedes aegypti (Diptera: Culicidae) mosquitoes were fed sucrose and human blood with and without dengue virus type 2 (D2-16681), and collected at 0.5, 1, 6, and 12 h, respectively. Specimens were prepared for examination under light and electron microscopy. The results showed that PM was produced only in the blood-fed mosquitoes. The infected blood meal induced the mosquitoes to produce PM in their midgut earlier and thicker than in mosquitoes with blood alone. The initial evidence of PM occurred at 1 h post-blood meal (PBM) as a matrix-like structure. By 6 h PBM, PM had become a layer, which persisted at 12 h. Among mosquitoes fed with blood alone, this structure was found only from 6 and 12 h PBM. Dengue virus type 2 induced different modifications of mosquito PM construction and structures, confirmed under an electron microscope.

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“…Based on these reports and the temporal expression pattern of peritrophins obtained in the current study, it can be presumed that the early peritrophin genes may be transcribed in response to the blood meal and their corresponding proteins are used immediately in the formation of the peritrophic matrix whereas the middle and late peritrophin gene products may be packaged into vesicles in preparation for a subsequent blood meal. Temporal regulation of secretory vesicular appearance process where PM precursors are accumulated was also demonstrated in the midgut of A. darlingi 25 , A. albimanus 13 and A. stephensi 26 . In contrast, in A. aegypti, the vesicles are formed de novo after blood feeding 19 .…”

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confidence: 72%

Modulation of Midgut Peritrophins' Expression during <i>Plasmodium Infection</i> in <i>Anopheles stephensi</i> (Diptera:Culicidae)

et al. 2017

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Morphological and enzymatic analysis of the midgut of Anopheles darlingi during blood digestion

Cited by 35 publications

References 33 publications

Serine protease activities in Oxysarcodexia thornax (Walker) (Diptera: Sarcophagidae) first instar larva

Serine protease activities in Oxysarcodexia thornax (Walker) (Diptera: Sarcophagidae) first instar larva

Peritrophic membrane structure of Aedes aegypti (Diptera: Culicidae) mosquitoes after infection with dengue virus type 2 (D2-16681)

Modulation of Midgut Peritrophins' Expression during <i>Plasmodium Infection</i> in <i>Anopheles stephensi</i> (Diptera:Culicidae)

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