Blood digestion in the mosquito,Anopheles stephensi liston (diptera: Culicidae): Partial characterization and post-feeding activity of midgut aminopeptidases (original) (raw)
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Medical and Veterinary Entomology, 1997
Present understanding of the development of sexual stages of the human malaria parasites Plasmodium vivax and Pfalciparum in the Anopheles vector is reviewed, with particular reference to the role of the mosquito midgut in establishing an infection. The sexual stages of the parasite, the gametocytes, are formed in human erythrocytes. The changes in temperature and pH encountered by the gametocyte induce gametogenesis in the lumen of the midgut. Macromolecules derived from mosquito tissue and second messenger pathways regulate events leading to fertilization. In An.tessellatus the movement of the ookinete from the lumen to the midgut epithelium is linked to the release of trypsin in the midgut and the peritrophic matrix is not a firm barrier to this movement, The passage of the Rvivax ookinete through the peritrophic matrix may take place before the latter is fully formed. The late ookinete development in Pfalciparurn requires chitinase to facilitate penetration of the peritrophic matrix. Recognition sites for the ookinetes are present on the midgut epithelial cells. N-acetyl glucosamine residues in the oligosaccharide side chains of An.tessellarus midgut glycoproteins and peritrophic matrix proteoglycan may function as recognition sites for Pvivax and Pfalciparum ookinetes. It is possible that ookinetes penetrating epithelial cells produce stress in the vector. Mosquito molecules may be involved in oocyst development in the basal lamina, and encapsulation of the parasite occurs in vectors that are refractory to the parasite. Detailed knowledge of vector-parasite interactions, particularly in the midgut and the identification of critical mosquito molecules offers prospects for manipulating the vector for the control of malaria.
Archives of Insect Biochemistry and Physiology, 2012
Understanding specific gene regulation during responses to malaria infection is key to dissecting the mosquito defense mechanisms and host/parasite interactions. A full-length serine protease cDNA was isolated from the fat body of female Anopheles dirus, a major malaria vector in Thailand. The predicted amino acid sequence of SERF4 identifies it as a member of the serine protease family containing a single trypsin-like protease domain. Digestive trypsins function in the female mosquito midgut and are inducible in two phases in this tissue upon blood intake. However, the gene was highly upregulated in the midgut at day 3 postinfection by Plasmodium falciparum. In situ hybridization confirmed that SERF4 transcripts were located in the midgut epithelial cells rather than hemocytes or other tissues associated with the midgut. SERF4 was also strongly downregulated in the whole insects at day 16 after infection in comparison with the blood-fed control. Changes in the expression of the SERF4 gene in response to infection with this human malaria parasite suggest a role in parasite-specific innate immunity.
Insect Biochemistry and Molecular Biology, 2010
The main vector for transmission of malaria in Mexico is the Anopheles albimanus mosquito. The midgut of disease-transmitting mosquitoes carries out a variety of functions that are related to blood feeding. We analyzed the midgut of A. albimanus infected with Plasmodium berghei (resistant mosquito) using a proteomic approach to identify putative short peptides that are enriched in the midgut after blood feeding. Mosquito midguts were analyzed by two-dimensional electrophoresis to determine the changes in protein profiles. We identified 21 spot proteins that are differentially expressed in the blood of mosquitoes during the immune challenge. Molecular weight of the spots varied from 13 to 36 kDa, with a broad isoelectric point range of 3.92e8.90. We identified the differentially expressed proteins using mass spectrometry and constructed a proteomic data base of the A. albimanus midgut with diverse functions, some of them proteins with digestive and immunologic functions. Identification of these proteins may have important implications for understanding the blood meal digestion process, as well as developing novel vector control strategies and understanding parasite vector interactions.
Study and comparison of mosquito (Diptera) aminopeptidase N protein with other order of insects
International Journal of Mosquito Research, 2019
The Aminopeptidase N group of exopeptidases are abundant proteins on the midgut brush border of mosquitoes. It belongs to a group of membrane-bound zinc metalloproteases. It is a ubiquitous enzyme that is found in a wide range of organisms from insects to mammals. Studies carried out on mosquitoes APNs are proteolytic enzymes that are involved in a wide range of functions, including digestion, involved in defense responses receptors for Bacillus thuringiensis (Bt) Cry1 insecticidal toxins and very important to play a role in parasite-vector interactions. Mosquito based Malaria Transmission Blocking Vaccines (TBV) target midgut surface antigens of Anopheles mosquitoes, the obligate vector of malaria parasite. Aminopeptidase N 1 is one of the most potent immunogenic protein involved in parasite infection and development in mosquitoes.
Journal of the National Science Foundation of Sri Lanka, 2010
Intake of an infective bloodmeal containing Plasmodium uiuax gametocytes, by Anop heles tesselLatus mosquitoes, ieads to the detection of zygotes and ookinetes in the midgut 3-8 h after the bloodmeal. An intact peritrophic matrix, frrst observed approximately 18 h after a bloodmeal, is formed irrespective ofthe body size and age ofthe mosquito, but only in a proportion ofmosquitoes. Unlike in the case of P. falciparurn where ookinetes develop at about 24 h, the peritrophic matrix would therefore not be a signifrcant banier to the infectivity of P. uiuat dre to the relatively rapid formation of P. uiuox ookinetes. The rate oftrypsin production was the same in An. tessellatus of different sizes, with the activity peaking about 21 h post bloodmeal. At this time the majority of P. uiuax ookinetes would have exited the midgut. A tendency for An. tesselLolus of intermediate size to be more susceptible to infection with P. uiuor than large or small mosquitoes was observed. However this difference was statistically significant in only one of two experiments.
PLoS ONE, 2014
Malaria sporozoites must invade the salivary glands of mosquitoes for maturation before transmission to vertebrate hosts. The duration of the sporogonic cycle within the mosquitoes ranges from 10 to 21 days depending on the parasite species and temperature. During blood feeding salivary gland proteins are injected into the vertebrate host, along with malaria sporozoites in the case of an infected mosquito. To identify salivary gland proteins depleted after blood feeding of female Anopheles campestris-like, a potential malaria vector of Plasmodium vivax in Thailand, two-dimensional gel electrophoresis and nano-liquid chromatography-mass spectrometry techniques were used. Results showed that 19 major proteins were significantly depleted in three to four day-old mosquitoes fed on a first blood meal. For the mosquitoes fed the second blood meal on day 14 after the first blood meal, 14 major proteins were significantly decreased in amount. The significantly depleted proteins in both groups included apyrase, 59-nucleotidase/apyrase, D7, D7-related 1, short form D7r1, gSG6, antiplatelet protein, serine/threonine-protein kinase rio3, putative sil1, cyclophilin A, hypothetical protein Phum_PHUM512530, AGAP007618-PA, and two non-significant hit proteins. To our knowledge, this study presents for the first time the salivary gland proteins that are involved in the second blood feeding on the day corresponding to the transmission period of the sporozoites to new mammalian hosts. This information serves as a basis for future work concerning the possible role of these proteins in the parasite transmission and the physiological processes that occur during the blood feeding.
PLoS ONE, 2012
Background: Plasmodium parasites need to cross the midgut and salivary gland epithelia to complete their life cycle in the mosquito. However, our understanding of the molecular mechanism and the mosquito genes that participate in this process is still very limited. Methodology/Principal Findings: We identified an Anopheles gambiae epithelial serine protease (AgESP) that is constitutively expressed in the submicrovillar region of mosquito midgut epithelial cells and in the basal side of the salivary glands that is critical for Plasmodium parasites to cross these two epithelial barriers. AgESP silencing greatly reduces Plasmodium berghei and Plasmodium falciparum midgut invasion and prevents the transcriptional activation of gelsolin, a key regulator of actin remodeling and a reported Plasmodium agonist. AgESP expression is highly induced in midgut cells invaded by Plasmodium, suggesting that this protease also participates in the apoptotic response to invasion. In salivary gland epithelial cells, AgESP is localized on the basal side-the surface with which sporozoites interact. AgESP expression in the salivary gland is also induced in response to P. berghei and P. falciparum sporozoite invasion, and AgESP silencing significantly reduces the number of sporozoites that invade this organ. Conclusion: Our findings indicate that AgESP is required for Plasmodium parasites to effectively traverse the midgut and salivary gland epithelial barriers. Plasmodium parasites need to modify the actin cytoskeleton of mosquito epithelial cells to successfully complete their life cycle in the mosquito and AgESP appears to be a major player in the regulation of this process.