Polydnavirus Ank proteins bind NF-κB homodimers and inhibit processing of Relish.

Recent studies have greatly increased understanding of how the immune system of insects responds to infection, whereas much less is known about how pathogens subvert immune defenses. Key regulators of the insect immune system are Rel proteins that form Nuclear Factor-κB (NF-κB) transcription factors...

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Autores principales:	Kavita Bitra, Richard J Suderman, Michael R Strand
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/4737cc48bba848ae8cc0f831e8b3c7ea
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spelling	oai:doaj.org-article:4737cc48bba848ae8cc0f831e8b3c7ea2021-11-18T06:04:23ZPolydnavirus Ank proteins bind NF-κB homodimers and inhibit processing of Relish.1553-73661553-737410.1371/journal.ppat.1002722https://doaj.org/article/4737cc48bba848ae8cc0f831e8b3c7ea2012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22654665/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374Recent studies have greatly increased understanding of how the immune system of insects responds to infection, whereas much less is known about how pathogens subvert immune defenses. Key regulators of the insect immune system are Rel proteins that form Nuclear Factor-κB (NF-κB) transcription factors, and inhibitor κB (IκB) proteins that complex with and regulate NF-κBs. Major mortality agents of insects are parasitoid wasps that carry immunosuppressive polydnaviruses (PDVs). Most PDVs encode ank genes that share features with IκBs, while our own prior studies suggested that two ank family members from Microplitis demolitor bracovirus (MdBV) (Ank-H4 and Ank-N5) behave as IκB mimics. However, the binding affinities of these viral mimics for Rel proteins relative to endogenous IκBs remained unclear. Surface plasmon resonance (SPR) and co-immunoprecipitation assays showed that the IκB Cactus from Drosophila bound Dif and Dorsal homodimers more strongly than Relish homodimers. Ank-H4 and -N5 bound Dif, Dorsal and Relish homodimers with higher affinity than the IκB domain of Relish (Rel-49), and also bound Relish homodimers more strongly than Cactus. Ank-H4 and -N5 inhibited processing of compound Relish and reduced the expression of several antimicrobial peptide genes regulated by the Imd signaling pathway in Drosophila mbn2 cells. Studies conducted in the natural host Pseudoplusia includens suggested that parasitism by M. demolitor also activates NF-κB signaling and that MdBV inhibits this response. Overall, our data provide the first quantitative measures of insect and viral IκB binding affinities, while also showing that viral mimics disable Relish processing.Kavita BitraRichard J SudermanMichael R StrandPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 8, Iss 5, p e1002722 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
spellingShingle	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 Kavita Bitra Richard J Suderman Michael R Strand Polydnavirus Ank proteins bind NF-κB homodimers and inhibit processing of Relish.
description	Recent studies have greatly increased understanding of how the immune system of insects responds to infection, whereas much less is known about how pathogens subvert immune defenses. Key regulators of the insect immune system are Rel proteins that form Nuclear Factor-κB (NF-κB) transcription factors, and inhibitor κB (IκB) proteins that complex with and regulate NF-κBs. Major mortality agents of insects are parasitoid wasps that carry immunosuppressive polydnaviruses (PDVs). Most PDVs encode ank genes that share features with IκBs, while our own prior studies suggested that two ank family members from Microplitis demolitor bracovirus (MdBV) (Ank-H4 and Ank-N5) behave as IκB mimics. However, the binding affinities of these viral mimics for Rel proteins relative to endogenous IκBs remained unclear. Surface plasmon resonance (SPR) and co-immunoprecipitation assays showed that the IκB Cactus from Drosophila bound Dif and Dorsal homodimers more strongly than Relish homodimers. Ank-H4 and -N5 bound Dif, Dorsal and Relish homodimers with higher affinity than the IκB domain of Relish (Rel-49), and also bound Relish homodimers more strongly than Cactus. Ank-H4 and -N5 inhibited processing of compound Relish and reduced the expression of several antimicrobial peptide genes regulated by the Imd signaling pathway in Drosophila mbn2 cells. Studies conducted in the natural host Pseudoplusia includens suggested that parasitism by M. demolitor also activates NF-κB signaling and that MdBV inhibits this response. Overall, our data provide the first quantitative measures of insect and viral IκB binding affinities, while also showing that viral mimics disable Relish processing.
format	article
author	Kavita Bitra Richard J Suderman Michael R Strand
author_facet	Kavita Bitra Richard J Suderman Michael R Strand
author_sort	Kavita Bitra
title	Polydnavirus Ank proteins bind NF-κB homodimers and inhibit processing of Relish.
title_short	Polydnavirus Ank proteins bind NF-κB homodimers and inhibit processing of Relish.
title_full	Polydnavirus Ank proteins bind NF-κB homodimers and inhibit processing of Relish.
title_fullStr	Polydnavirus Ank proteins bind NF-κB homodimers and inhibit processing of Relish.
title_full_unstemmed	Polydnavirus Ank proteins bind NF-κB homodimers and inhibit processing of Relish.
title_sort	polydnavirus ank proteins bind nf-κb homodimers and inhibit processing of relish.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/4737cc48bba848ae8cc0f831e8b3c7ea
work_keys_str_mv	AT kavitabitra polydnavirusankproteinsbindnfkbhomodimersandinhibitprocessingofrelish AT richardjsuderman polydnavirusankproteinsbindnfkbhomodimersandinhibitprocessingofrelish AT michaelrstrand polydnavirusankproteinsbindnfkbhomodimersandinhibitprocessingofrelish
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Polydnavirus Ank proteins bind NF-κB homodimers and inhibit processing of Relish.

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