Deaminase-independent inhibition of parvoviruses by the APOBEC3A cytidine deaminase.

The APOBEC3 proteins form a multigene family of cytidine deaminases with inhibitory activity against viruses and retrotransposons. In contrast to APOBEC3G (A3G), APOBEC3A (A3A) has no effect on lentiviruses but dramatically inhibits replication of the parvovirus adeno-associated virus (AAV). To stud...

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Autores principales:	Iñigo Narvaiza, Daniel C Linfesty, Benjamin N Greener, Yoshiyuki Hakata, David J Pintel, Eric Logue, Nathaniel R Landau, Matthew D Weitzman
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2009
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/c9be6e30441e4dc4b3b23d56c804e04b
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spelling	oai:doaj.org-article:c9be6e30441e4dc4b3b23d56c804e04b2021-11-25T05:47:54ZDeaminase-independent inhibition of parvoviruses by the APOBEC3A cytidine deaminase.1553-73661553-737410.1371/journal.ppat.1000439https://doaj.org/article/c9be6e30441e4dc4b3b23d56c804e04b2009-05-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/19461882/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374The APOBEC3 proteins form a multigene family of cytidine deaminases with inhibitory activity against viruses and retrotransposons. In contrast to APOBEC3G (A3G), APOBEC3A (A3A) has no effect on lentiviruses but dramatically inhibits replication of the parvovirus adeno-associated virus (AAV). To study the contribution of deaminase activity to the antiviral activity of A3A, we performed a comprehensive mutational analysis of A3A. By mutation of non-conserved residues, we found that regions outside of the catalytic active site contribute to both deaminase and antiviral activities. Using A3A point mutants and A3A/A3G chimeras, we show that deaminase activity is not required for inhibition of recombinant AAV production. We also found that deaminase-deficient A3A mutants block replication of both wild-type AAV and the autonomous parvovirus minute virus of mice (MVM). In addition, we identify specific residues of A3A that confer activity against AAV when substituted into A3G. In summary, our results demonstrate that deaminase activity is not necessary for the antiviral activity of A3A against parvoviruses.Iñigo NarvaizaDaniel C LinfestyBenjamin N GreenerYoshiyuki HakataDavid J PintelEric LogueNathaniel R LandauMatthew D WeitzmanPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 5, Iss 5, p e1000439 (2009)
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 Iñigo Narvaiza Daniel C Linfesty Benjamin N Greener Yoshiyuki Hakata David J Pintel Eric Logue Nathaniel R Landau Matthew D Weitzman Deaminase-independent inhibition of parvoviruses by the APOBEC3A cytidine deaminase.
description	The APOBEC3 proteins form a multigene family of cytidine deaminases with inhibitory activity against viruses and retrotransposons. In contrast to APOBEC3G (A3G), APOBEC3A (A3A) has no effect on lentiviruses but dramatically inhibits replication of the parvovirus adeno-associated virus (AAV). To study the contribution of deaminase activity to the antiviral activity of A3A, we performed a comprehensive mutational analysis of A3A. By mutation of non-conserved residues, we found that regions outside of the catalytic active site contribute to both deaminase and antiviral activities. Using A3A point mutants and A3A/A3G chimeras, we show that deaminase activity is not required for inhibition of recombinant AAV production. We also found that deaminase-deficient A3A mutants block replication of both wild-type AAV and the autonomous parvovirus minute virus of mice (MVM). In addition, we identify specific residues of A3A that confer activity against AAV when substituted into A3G. In summary, our results demonstrate that deaminase activity is not necessary for the antiviral activity of A3A against parvoviruses.
format	article
author	Iñigo Narvaiza Daniel C Linfesty Benjamin N Greener Yoshiyuki Hakata David J Pintel Eric Logue Nathaniel R Landau Matthew D Weitzman
author_facet	Iñigo Narvaiza Daniel C Linfesty Benjamin N Greener Yoshiyuki Hakata David J Pintel Eric Logue Nathaniel R Landau Matthew D Weitzman
author_sort	Iñigo Narvaiza
title	Deaminase-independent inhibition of parvoviruses by the APOBEC3A cytidine deaminase.
title_short	Deaminase-independent inhibition of parvoviruses by the APOBEC3A cytidine deaminase.
title_full	Deaminase-independent inhibition of parvoviruses by the APOBEC3A cytidine deaminase.
title_fullStr	Deaminase-independent inhibition of parvoviruses by the APOBEC3A cytidine deaminase.
title_full_unstemmed	Deaminase-independent inhibition of parvoviruses by the APOBEC3A cytidine deaminase.
title_sort	deaminase-independent inhibition of parvoviruses by the apobec3a cytidine deaminase.
publisher	Public Library of Science (PLoS)
publishDate	2009
url	https://doaj.org/article/c9be6e30441e4dc4b3b23d56c804e04b
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Deaminase-independent inhibition of parvoviruses by the APOBEC3A cytidine deaminase.

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