STRUCTURAL AND BIOCHEMICAL ELUCIDATION OF MOSQUITO HEAT SHOCK PROTEIN 70
Intro: Heat Shock Proteins function as molecular chaperones and found present in almost all living organism. Furthermore, HSPs are divided into many different classes based on their molecular mass, amino acid composition, and physiological function. Among different insects, mosquito is unique mainly...
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| Format: | Article |
| Language: | English |
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Elsevier
2023-05-01
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| Series: | International Journal of Infectious Diseases |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S1201971223002072 |
| _version_ | 1797824594883641344 |
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| author | S. Chakraborti |
| author_facet | S. Chakraborti |
| author_sort | S. Chakraborti |
| collection | DOAJ |
| description | Intro: Heat Shock Proteins function as molecular chaperones and found present in almost all living organism. Furthermore, HSPs are divided into many different classes based on their molecular mass, amino acid composition, and physiological function. Among different insects, mosquito is unique mainly because of three factors; first its blood sucking abilities, second its disease spreading nature and third, its unique adoptability against any stress condition. For any organism, adaptation against extremities HSP family of proteins plays a crucial role as they are the key molecular chaperones and folding catalysts. However, very little information is available on how HSPs proteins are associated with mosquito's stress response and protein folding. Methods: Catalogue of heat shock protein of Anopheles culicifacies and Anopheles stephensi (malaria causing vectors of India) was prepared using extensive BLASTP, tBLASTn and Pfam based domain search analysis. Evolutionary relationship of Hsp was determined by performing syntenic and phylogenetic relationship. Catalogue was experimentally validated by extensive q-pcr analysis. Furthermore, recombinant Hsp70 protein was expressed and purified in E.coli and characterized using different biophysical technique, finally activity of the Hsp70 was determined using various biochemical assay. Findings: Result shows that there are seven different isoforms of Hsp70; among seven isoforms four are localized in cytoplasm, two are localized in ER and one in mitochondria. We also determined tissue specific expression of different Hsp70 isoforms in adult female mosquitoes. Also we measured the activity and compared it with other organism and also determined the residues responsible for the activity. Conclusion: We have explored Hsp70 using a multi-disciplinary approach, and this study provides us many novel insight regarding Hsp70 expression, conformation, folding and its interaction partner and helps us in developing Hsp70 specific inhibitors. In my presentation I will show our recent findings related to heat shock proteins and discuss successful inhibitor screening against heat shock proteins. |
| first_indexed | 2024-03-13T10:41:16Z |
| format | Article |
| id | doaj.art-b11cf7d2630b41019ea013a9f9d47ee9 |
| institution | Directory Open Access Journal |
| issn | 1201-9712 |
| language | English |
| last_indexed | 2024-03-13T10:41:16Z |
| publishDate | 2023-05-01 |
| publisher | Elsevier |
| record_format | Article |
| series | International Journal of Infectious Diseases |
| spelling | doaj.art-b11cf7d2630b41019ea013a9f9d47ee92023-05-18T04:38:11ZengElsevierInternational Journal of Infectious Diseases1201-97122023-05-01130S34STRUCTURAL AND BIOCHEMICAL ELUCIDATION OF MOSQUITO HEAT SHOCK PROTEIN 70S. Chakraborti0ICMR-National Institute of Malaria Research, Vector Biology, New Delhi, IndiaIntro: Heat Shock Proteins function as molecular chaperones and found present in almost all living organism. Furthermore, HSPs are divided into many different classes based on their molecular mass, amino acid composition, and physiological function. Among different insects, mosquito is unique mainly because of three factors; first its blood sucking abilities, second its disease spreading nature and third, its unique adoptability against any stress condition. For any organism, adaptation against extremities HSP family of proteins plays a crucial role as they are the key molecular chaperones and folding catalysts. However, very little information is available on how HSPs proteins are associated with mosquito's stress response and protein folding. Methods: Catalogue of heat shock protein of Anopheles culicifacies and Anopheles stephensi (malaria causing vectors of India) was prepared using extensive BLASTP, tBLASTn and Pfam based domain search analysis. Evolutionary relationship of Hsp was determined by performing syntenic and phylogenetic relationship. Catalogue was experimentally validated by extensive q-pcr analysis. Furthermore, recombinant Hsp70 protein was expressed and purified in E.coli and characterized using different biophysical technique, finally activity of the Hsp70 was determined using various biochemical assay. Findings: Result shows that there are seven different isoforms of Hsp70; among seven isoforms four are localized in cytoplasm, two are localized in ER and one in mitochondria. We also determined tissue specific expression of different Hsp70 isoforms in adult female mosquitoes. Also we measured the activity and compared it with other organism and also determined the residues responsible for the activity. Conclusion: We have explored Hsp70 using a multi-disciplinary approach, and this study provides us many novel insight regarding Hsp70 expression, conformation, folding and its interaction partner and helps us in developing Hsp70 specific inhibitors. In my presentation I will show our recent findings related to heat shock proteins and discuss successful inhibitor screening against heat shock proteins.http://www.sciencedirect.com/science/article/pii/S1201971223002072 |
| spellingShingle | S. Chakraborti STRUCTURAL AND BIOCHEMICAL ELUCIDATION OF MOSQUITO HEAT SHOCK PROTEIN 70 International Journal of Infectious Diseases |
| title | STRUCTURAL AND BIOCHEMICAL ELUCIDATION OF MOSQUITO HEAT SHOCK PROTEIN 70 |
| title_full | STRUCTURAL AND BIOCHEMICAL ELUCIDATION OF MOSQUITO HEAT SHOCK PROTEIN 70 |
| title_fullStr | STRUCTURAL AND BIOCHEMICAL ELUCIDATION OF MOSQUITO HEAT SHOCK PROTEIN 70 |
| title_full_unstemmed | STRUCTURAL AND BIOCHEMICAL ELUCIDATION OF MOSQUITO HEAT SHOCK PROTEIN 70 |
| title_short | STRUCTURAL AND BIOCHEMICAL ELUCIDATION OF MOSQUITO HEAT SHOCK PROTEIN 70 |
| title_sort | structural and biochemical elucidation of mosquito heat shock protein 70 |
| url | http://www.sciencedirect.com/science/article/pii/S1201971223002072 |
| work_keys_str_mv | AT schakraborti structuralandbiochemicalelucidationofmosquitoheatshockprotein70 |