![Open Access](https://i-scholar.in/lib/pkp/templates/images/icons/fulltextgreen.png)
![Restricted Access](https://i-scholar.in/lib/pkp/templates/images/icons/fulltextred.png)
Modulation of Midgut Peritrophins' Expression during Plasmodium Infection in Anopheles stephensi (Diptera:Culicidae)
The peritrophic matrix (PM) serves as a barrier to pathogens in many disease vectors including mosquitoes. The Plasmodium ookinete has to cross the PM barrier for its successful establishment in the mosquito midgut and subsequent transmission. It is conceived that alterations to PM may lead to a block in infection. Peritrophins which are the major constituents of PM are yet to be elucidated at molecular level. The present study demonstrates Anopheles stephensi midgut peritrophins' expression during Plasmodium berghei infection. Eight peritrophin genes (Per 10, Per 16, Per 22, Per 25, Per 26, Per 28, Per 30 & Per 43) of A. stephensi were identified from vectorbase, isolated from the adult midgut, and expression pattern monitored in real-time, in normal and infected blood meal conditions. Temporal expression of peritrophins in the midgut was monitored every 6 h till 24 h post blood meal. Results showed that the Per 10, Per 16, Per 22, Per 25 and Per 26 expression was significantly downregulated during Plasmodium infection whereas Per 30 and Per 43 expression was markedly up-regulated. The Per 28 expression was low initially but elevated later. This data clearly indicates that peritrophins are differentially modulated in infected midgut. The significance of differential expression of peritrophins' in parasite transmission is discussed further.
Keywords
Anopheles stephensi, Malaria, Peritrophins, Plasmodium berghei, Transmission.
User
Font Size
Information
- Peters, W., Peritrophic membranes. In Zoophysiology, SpringerVerlag, Berlin, 1992, vol. 30, pp. 1–238.
- Lehane, M. J., Peritrophic matrix structure and function. Annu. Rev. Entomol., 1997, 42, 525–550.
- Hegedus, D., Erlandson, M., Gillott, C. and Toprak, U., New insights into peritrophic matrix synthesis, architecture, and function. Annu. Rev. Entomol., 2009, 54, 285–302.
- Tellam, R. L., Wijffels, G. and Willadsen, P., Peritrophic matrix proteins. Insect Biochem. Mol. Biol., 1999, 29, 87–101.
- Tetreau, G. et al., Analysis of chitin-binding proteins from Manduca sexta provides new insights into evolution of peritrophin A-type chitin-binding domains in insects. Insect Biochem. Mol. Biol., 2014, 62, 127–141.
- Toprak, U. et al., Identification of the Mamestra configurata (Lepidoptera: Noctuidae) peritrophic matrix proteins and enzymes involved in peritrophic matrix chitin metabolism. Insect Sci., 2016, 23, 656–674.
- Yin, J., Wei, Z. J., Li, K. B., Cao, Y. Z. and Guo, W., Identification and molecular characterization of a new member of the peritrophic membrane proteins from the meadow moth, Loxostege sticticalis. Int. J. Biol. Sci., 2010, 6, 491–498.
- Gaines, P. J., Walmsley, S. J. and Wisnewski, N., Cloning and characterization of five cDNAs encoding peritrophin-A domains from the cat flea, Ctenocephalides felis. Insect Biochem. Mol. Biol., 2003, 33, 1061–1073.
- Vuocolo, T., Eisemann, C. H., Pearson, R. D., Willadsen, P. and Tellam, R. L., Identification and molecular characterization of a peritrophin gene, Peritrophin-48, from the myiasis fly Chrysomya bezziana. Insect Biochem. Mol. Biol., 2001, 31, 919–932.
- Elvin, C. M., Vuocolo, T., Pearson, R. D., East, I. J. and Riding, G. A., Characterization of a major peritrophic membrane protein, Peritrophin-44, from the larvae of Lucilia cuprina. J. Biol. Chem., 1996, 271, 8925–8935.
- Weiss, B. L., Savage, A. F., Griffith, B. C., Wu, Y. and Aksoy, S., The peritrophic matrix mediates differential infection outcomes in the tsetse fly gut following challenge with commensal, pathogenic, and parasitic microbes. J. Immunol., 2014, 193, 773–782.
- Shen, Z. and Jacobs-Lorena, M., A Type I peritrophic matrix protein from the malaria vector Anopheles gambiae binds to chitin: cloning, expression, and characterization. J. Biol. Chem., 1998, 273, 17665–17670.
- Cazares-Raga, F. E., Chavez-Munguia, B., Gonzolez-Calixto, C., Ochoa-Frarco, A. P., Gawinowicz, M. A., Rodriguez, M. H. and Hernandez-Hernandez, F. C., Morphological and proteomic characterization of midgut of the malaria vector Anopheles albimanus at early time after a blood feeding. J. Proteomics, 2014, 111, 100–112.
- Devenport, M., Alvarenga, P. H., Shao, L., Fujioka, H., Bianconi, M. L., Oliveira, P. L. and Jacobs-Lorena, M., Identification of the Aedes aegypti peritrophic matrix protein AeIMUCI as a hemebinding protein. Biochemistry, 2006, 45, 9540–9549.
- Huber, M., Cabib, E. and Miller, L. H., Malaria parasite chitinase and penetration of the mosquito peritrophic membrane. Proc. Natl. Acad. Sci. USA, 1991, 88, 2807–2810.
- Tsai, Y. L., Hayward, R. E., Langer, R. C., Fidock, D. A. and Vinetz, J. M., Disruption of Plasmodium falciparum chitinase markedly impairs parasite invasion of mosquito midgut. Infect. Immun., 2001, 69, 4048–4054.
- Shahabuddin, M., Toyoshima, T., Aikawa, M. and Kaslow, D. C., Transmission-blocking activity of a chitinase inhibitor and activation of malarial parasite chitinase by mosquito protease. Proc. Natl. Acad. Sci. USA, 1993, 90, 4266–4270.
- Shahabuddin, M., Lemos, F. J., Kaslow, D. C. and Jacobs-Lorena, M., Antibody-mediated inhibition of Aedes aegypti midgut trypsin blocks sporogonic development of Plasmodium gallinaceum. Infect. Immun., 1996, 64, 739–743.
- Dinglasan, R. R. et al., The Anopheles gambiae adult midgut peritrophic matrix proteome. Insect Biochem. Mol. Biol., 2009, 39, 125–134.
- Shen, Z. and Jacobs-Lorena, M., Evolution of chitin-binding proteins in invertebrates. J. Mol. Evol., 1999, 48, 341–347.
- He, N. et al., Proteomic analysis of cast cuticles from Anopheles gambiae by tandem mass spectrometry. Insect Biochem. Mol. Biol., 2007, 37, 135–146.
- Tellam, R. L. and Eisemann, C., Chitin is only a minor component of the peritrophic matrix from larvae of Lucilia cuprina. Insect Biochem. Mol. Biol., 2000, 30, 1189–1120.
- Dana, A. N. et al., Gene expression patterns associated with blood feeding in the malaria mosquito Anopheles gambiae. BMC Genomics, 2005, 6, 5.
- Staubli, W., Freyvogel, T. A. and Suter, J., Structural modification of the endoplasmic epithelial cells of mosquitoes in relation to blood intake. J. Microsc., 1966, 85, 189–204.
- Okuda, K., Caroci, A., Ribolla, P., Marinotti, O., De Bianchi, A. G. and Bijovsky, A. T., Morphological and enzymatic analysis of the midgut of Anopheles darlingi during blood digestion. J. Insect Physiol., 2005, 51, 769–776.
- Berner, R., Rudin, W. and Hecker, H., Peritrophic membranes and protease activity in the midgut of the malaria mosquito, Anopheles stephensi (Liston) (Insecta: Diptera) under normal and experimental conditions. J. Ultrastruct. Res., 1983, 83, 195–204.
- Becker, B., Effects of 20-hydroxyecdysone, juvenile hormone, Dimilin, and Captan on in vitro synthesis of peritrophic membrane in Calliphora erythrocephala. J. Insect Physiol., 1978, 24, 699–705.
- Billingsley, P. F. and Rudin, W., The role of the mosquito peritrophic membrane in blood meal digestion and infectivity of Plasmodium species. J. Parasitol., 1992, 78, 430–440.
![](https://i-scholar.in/public/site/images/abstractview.png)
Abstract Views: 274
![](https://i-scholar.in/public/site/images/pdfview.png)
PDF Views: 88