The dengue vector Aedes aegypti contains a functional high mobility group box 1 (HMGB1) protein with a unique regulatory C-terminus.
The mosquito Aedes aegypti can spread the dengue, chikungunya and yellow fever viruses. Thus, the search for key molecules involved in the mosquito survival represents today a promising vector control strategy. High Mobility Group Box (HMGB) proteins are essential nuclear factors that maintain the h...
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2012
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oai:doaj.org-article:4bc086d502824e8ca762341eb7f4bf2b2021-11-18T07:13:26ZThe dengue vector Aedes aegypti contains a functional high mobility group box 1 (HMGB1) protein with a unique regulatory C-terminus.1932-620310.1371/journal.pone.0040192https://doaj.org/article/4bc086d502824e8ca762341eb7f4bf2b2012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22802955/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203The mosquito Aedes aegypti can spread the dengue, chikungunya and yellow fever viruses. Thus, the search for key molecules involved in the mosquito survival represents today a promising vector control strategy. High Mobility Group Box (HMGB) proteins are essential nuclear factors that maintain the high-order structure of chromatin, keeping eukaryotic cells viable. Outside the nucleus, secreted HMGB proteins could alert the innate immune system to foreign antigens and trigger the initiation of host defenses. In this work, we cloned and functionally characterized the HMGB1 protein from Aedes aegypti (AaHMGB1). The AaHMGB1 protein typically consists of two HMG-box DNA binding domains and an acidic C-terminus. Interestingly, AaHMGB1 contains a unique alanine/glutamine-rich (AQ-rich) C-terminal region that seems to be exclusive of dipteran HMGB proteins. AaHMGB1 is localized to the cell nucleus, mainly associated with heterochromatin. Circular dichroism analyses of AaHMGB1 or the C-terminal truncated proteins revealed α-helical structures. We showed that AaHMGB1 can effectively bind and change the topology of DNA, and that the AQ-rich and the C-terminal acidic regions can modulate its ability to promote DNA supercoiling, as well as its preference to bind supercoiled DNA. AaHMGB1 is phosphorylated by PKA and PKC, but not by CK2. Importantly, phosphorylation of AaHMGB1 by PKA or PKC completely abolishes its DNA bending activity. Thus, our study shows that a functional HMGB1 protein occurs in Aedes aegypt and we provide the first description of a HMGB1 protein containing an AQ-rich regulatory C-terminus.Fabio Schneider RibeiroIsabel Caetano de Abreu da SilvaVitor Coutinho CarneiroFabrício dos Santos BelgranoRonaldo Mohana-BorgesIvone de Andrade RosaMarlene BenchimolNathalia Rocha Quintino SouzaRafael Dias MesquitaMarcos Henrique Ferreira SorgineFelipe Gazos-LopesAmanda Roberta Revoredo VicentinoWenjie WuRenata de Moraes MacielMario Alberto Cardoso da Silva-NetoMarcelo Rosado FantappiéPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 7, p e40192 (2012) |
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| spellingShingle |
Medicine R Science Q Fabio Schneider Ribeiro Isabel Caetano de Abreu da Silva Vitor Coutinho Carneiro Fabrício dos Santos Belgrano Ronaldo Mohana-Borges Ivone de Andrade Rosa Marlene Benchimol Nathalia Rocha Quintino Souza Rafael Dias Mesquita Marcos Henrique Ferreira Sorgine Felipe Gazos-Lopes Amanda Roberta Revoredo Vicentino Wenjie Wu Renata de Moraes Maciel Mario Alberto Cardoso da Silva-Neto Marcelo Rosado Fantappié The dengue vector Aedes aegypti contains a functional high mobility group box 1 (HMGB1) protein with a unique regulatory C-terminus. |
| description |
The mosquito Aedes aegypti can spread the dengue, chikungunya and yellow fever viruses. Thus, the search for key molecules involved in the mosquito survival represents today a promising vector control strategy. High Mobility Group Box (HMGB) proteins are essential nuclear factors that maintain the high-order structure of chromatin, keeping eukaryotic cells viable. Outside the nucleus, secreted HMGB proteins could alert the innate immune system to foreign antigens and trigger the initiation of host defenses. In this work, we cloned and functionally characterized the HMGB1 protein from Aedes aegypti (AaHMGB1). The AaHMGB1 protein typically consists of two HMG-box DNA binding domains and an acidic C-terminus. Interestingly, AaHMGB1 contains a unique alanine/glutamine-rich (AQ-rich) C-terminal region that seems to be exclusive of dipteran HMGB proteins. AaHMGB1 is localized to the cell nucleus, mainly associated with heterochromatin. Circular dichroism analyses of AaHMGB1 or the C-terminal truncated proteins revealed α-helical structures. We showed that AaHMGB1 can effectively bind and change the topology of DNA, and that the AQ-rich and the C-terminal acidic regions can modulate its ability to promote DNA supercoiling, as well as its preference to bind supercoiled DNA. AaHMGB1 is phosphorylated by PKA and PKC, but not by CK2. Importantly, phosphorylation of AaHMGB1 by PKA or PKC completely abolishes its DNA bending activity. Thus, our study shows that a functional HMGB1 protein occurs in Aedes aegypt and we provide the first description of a HMGB1 protein containing an AQ-rich regulatory C-terminus. |
| format |
article |
| author |
Fabio Schneider Ribeiro Isabel Caetano de Abreu da Silva Vitor Coutinho Carneiro Fabrício dos Santos Belgrano Ronaldo Mohana-Borges Ivone de Andrade Rosa Marlene Benchimol Nathalia Rocha Quintino Souza Rafael Dias Mesquita Marcos Henrique Ferreira Sorgine Felipe Gazos-Lopes Amanda Roberta Revoredo Vicentino Wenjie Wu Renata de Moraes Maciel Mario Alberto Cardoso da Silva-Neto Marcelo Rosado Fantappié |
| author_facet |
Fabio Schneider Ribeiro Isabel Caetano de Abreu da Silva Vitor Coutinho Carneiro Fabrício dos Santos Belgrano Ronaldo Mohana-Borges Ivone de Andrade Rosa Marlene Benchimol Nathalia Rocha Quintino Souza Rafael Dias Mesquita Marcos Henrique Ferreira Sorgine Felipe Gazos-Lopes Amanda Roberta Revoredo Vicentino Wenjie Wu Renata de Moraes Maciel Mario Alberto Cardoso da Silva-Neto Marcelo Rosado Fantappié |
| author_sort |
Fabio Schneider Ribeiro |
| title |
The dengue vector Aedes aegypti contains a functional high mobility group box 1 (HMGB1) protein with a unique regulatory C-terminus. |
| title_short |
The dengue vector Aedes aegypti contains a functional high mobility group box 1 (HMGB1) protein with a unique regulatory C-terminus. |
| title_full |
The dengue vector Aedes aegypti contains a functional high mobility group box 1 (HMGB1) protein with a unique regulatory C-terminus. |
| title_fullStr |
The dengue vector Aedes aegypti contains a functional high mobility group box 1 (HMGB1) protein with a unique regulatory C-terminus. |
| title_full_unstemmed |
The dengue vector Aedes aegypti contains a functional high mobility group box 1 (HMGB1) protein with a unique regulatory C-terminus. |
| title_sort |
dengue vector aedes aegypti contains a functional high mobility group box 1 (hmgb1) protein with a unique regulatory c-terminus. |
| publisher |
Public Library of Science (PLoS) |
| publishDate |
2012 |
| url |
https://doaj.org/article/4bc086d502824e8ca762341eb7f4bf2b |
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