Proteome-wide analysis of Anopheles culicifacies mosquito midgut: new insights into the mechanism of refractoriness
Abstract Background Midgut invasion, a major bottleneck for malaria parasites transmission is considered as a potential target for vector-parasite interaction studies. New intervention strategies are required to explore the midgut proteins and their potential role in refractoriness for malaria contr...
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| Format: | Article |
| Language: | English |
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BMC
2018-05-01
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| Series: | BMC Genomics |
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| Online Access: | http://link.springer.com/article/10.1186/s12864-018-4729-3 |
| _version_ | 1819076401166286848 |
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| author | Sonam Vijay Ritu Rawal Kavita Kadian Jagbir Singh Tridibesh Adak Arun Sharma |
| author_facet | Sonam Vijay Ritu Rawal Kavita Kadian Jagbir Singh Tridibesh Adak Arun Sharma |
| author_sort | Sonam Vijay |
| collection | DOAJ |
| description | Abstract Background Midgut invasion, a major bottleneck for malaria parasites transmission is considered as a potential target for vector-parasite interaction studies. New intervention strategies are required to explore the midgut proteins and their potential role in refractoriness for malaria control in Anopheles mosquitoes. To better understand the midgut functional proteins of An. culicifacies susceptible and refractory species, proteomic approaches coupled with bioinformatics analysis is an effective means in order to understand the mechanism of refractoriness. In the present study, an integrated in solution- in gel trypsin digestion approach, along with Isobaric tag for relative and absolute quantitation (iTRAQ)–Liquid chromatography/Mass spectrometry (LC/MS/MS) and data mining were performed to identify the proteomic profile and differentially expressed proteins in Anopheles culicifacies susceptible species A and refractory species B. Results Shot gun proteomics approaches led to the identification of 80 proteins in An. culicifacies susceptible species A and 92 in refractory species B and catalogue was prepared. iTRAQ based proteomic analysis identified 48 differentially expressed proteins from total 130 proteins. Of these, 41 were downregulated and 7 were upregulated in refractory species B in comparison to susceptible species A. We report that the altered midgut proteins identified in naturally refractory mosquitoes are involved in oxidative phosphorylation, antioxidant and proteolysis process that may suggest their role in parasite growth inhibition. Furthermore, real time polymerase chain reaction (PCR) analysis of few proteins indicated higher expression of iTRAQ upregulated protein in refractory species than susceptible species. Conclusion This study elucidates the first proteome of the midguts of An. culicifacies sibling species that attempts to analyze unique proteogenomic interactions to provide insights for better understanding of the mechanism of refractoriness. Functional implications of these upregulated proteins in refractory species may reflect the phenotypic characteristics of the mosquitoes and will improve our understandings of blood meal digestion process, parasite vector interactions and proteomes of other vectors of human diseases for development of novel vector control strategies. |
| first_indexed | 2024-12-21T18:40:43Z |
| format | Article |
| id | doaj.art-5ef2173a908648198ff923c0041761a1 |
| institution | Directory Open Access Journal |
| issn | 1471-2164 |
| language | English |
| last_indexed | 2024-12-21T18:40:43Z |
| publishDate | 2018-05-01 |
| publisher | BMC |
| record_format | Article |
| series | BMC Genomics |
| spelling | doaj.art-5ef2173a908648198ff923c0041761a12022-12-21T18:54:01ZengBMCBMC Genomics1471-21642018-05-0119111610.1186/s12864-018-4729-3Proteome-wide analysis of Anopheles culicifacies mosquito midgut: new insights into the mechanism of refractorinessSonam Vijay0Ritu Rawal1Kavita Kadian2Jagbir Singh3Tridibesh Adak4Arun Sharma5Division of Protein Biochemistry and Structural Biology, National Institute of Malaria Research (ICMR)Division of Protein Biochemistry and Structural Biology, National Institute of Malaria Research (ICMR)Division of Protein Biochemistry and Structural Biology, National Institute of Malaria Research (ICMR)Division of Protein Biochemistry and Structural Biology, National Institute of Malaria Research (ICMR)Vector Biology Divisions, National Institute of Malaria Research (ICMR)Division of Protein Biochemistry and Structural Biology, National Institute of Malaria Research (ICMR)Abstract Background Midgut invasion, a major bottleneck for malaria parasites transmission is considered as a potential target for vector-parasite interaction studies. New intervention strategies are required to explore the midgut proteins and their potential role in refractoriness for malaria control in Anopheles mosquitoes. To better understand the midgut functional proteins of An. culicifacies susceptible and refractory species, proteomic approaches coupled with bioinformatics analysis is an effective means in order to understand the mechanism of refractoriness. In the present study, an integrated in solution- in gel trypsin digestion approach, along with Isobaric tag for relative and absolute quantitation (iTRAQ)–Liquid chromatography/Mass spectrometry (LC/MS/MS) and data mining were performed to identify the proteomic profile and differentially expressed proteins in Anopheles culicifacies susceptible species A and refractory species B. Results Shot gun proteomics approaches led to the identification of 80 proteins in An. culicifacies susceptible species A and 92 in refractory species B and catalogue was prepared. iTRAQ based proteomic analysis identified 48 differentially expressed proteins from total 130 proteins. Of these, 41 were downregulated and 7 were upregulated in refractory species B in comparison to susceptible species A. We report that the altered midgut proteins identified in naturally refractory mosquitoes are involved in oxidative phosphorylation, antioxidant and proteolysis process that may suggest their role in parasite growth inhibition. Furthermore, real time polymerase chain reaction (PCR) analysis of few proteins indicated higher expression of iTRAQ upregulated protein in refractory species than susceptible species. Conclusion This study elucidates the first proteome of the midguts of An. culicifacies sibling species that attempts to analyze unique proteogenomic interactions to provide insights for better understanding of the mechanism of refractoriness. Functional implications of these upregulated proteins in refractory species may reflect the phenotypic characteristics of the mosquitoes and will improve our understandings of blood meal digestion process, parasite vector interactions and proteomes of other vectors of human diseases for development of novel vector control strategies.http://link.springer.com/article/10.1186/s12864-018-4729-3Anopheles culicifaciesRefractoryMidgutShot gun proteomicsiTRAQRT-PCR |
| spellingShingle | Sonam Vijay Ritu Rawal Kavita Kadian Jagbir Singh Tridibesh Adak Arun Sharma Proteome-wide analysis of Anopheles culicifacies mosquito midgut: new insights into the mechanism of refractoriness BMC Genomics Anopheles culicifacies Refractory Midgut Shot gun proteomics iTRAQ RT-PCR |
| title | Proteome-wide analysis of Anopheles culicifacies mosquito midgut: new insights into the mechanism of refractoriness |
| title_full | Proteome-wide analysis of Anopheles culicifacies mosquito midgut: new insights into the mechanism of refractoriness |
| title_fullStr | Proteome-wide analysis of Anopheles culicifacies mosquito midgut: new insights into the mechanism of refractoriness |
| title_full_unstemmed | Proteome-wide analysis of Anopheles culicifacies mosquito midgut: new insights into the mechanism of refractoriness |
| title_short | Proteome-wide analysis of Anopheles culicifacies mosquito midgut: new insights into the mechanism of refractoriness |
| title_sort | proteome wide analysis of anopheles culicifacies mosquito midgut new insights into the mechanism of refractoriness |
| topic | Anopheles culicifacies Refractory Midgut Shot gun proteomics iTRAQ RT-PCR |
| url | http://link.springer.com/article/10.1186/s12864-018-4729-3 |
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