Receptor-induced thiolate couples Env activation to retrovirus fusion and infection.

According to current models of retrovirus infection, receptor binding to the surface subunit (SU) of the envelope glycoprotein (Env) triggers a conformational change in the transmembrane subunit (TM) that mediates virus fusion to cell membranes. To understand how this occurs, we investigated the rol...

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Autores principales:	Jason G Smith, James M Cunningham
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2007
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/83a121dcb80b48e1a8ee66bebac040c0
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spelling	oai:doaj.org-article:83a121dcb80b48e1a8ee66bebac040c02021-11-25T05:46:47ZReceptor-induced thiolate couples Env activation to retrovirus fusion and infection.1553-73661553-737410.1371/journal.ppat.0030198https://doaj.org/article/83a121dcb80b48e1a8ee66bebac040c02007-12-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/18260686/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374According to current models of retrovirus infection, receptor binding to the surface subunit (SU) of the envelope glycoprotein (Env) triggers a conformational change in the transmembrane subunit (TM) that mediates virus fusion to cell membranes. To understand how this occurs, we investigated the role of the receptor Tva in avian leukosis virus-A (ALV-A) infection. We find that Tva binding induced the formation of a reactive thiolate on Cys38 (Cys38-S- in SU. Both chemical and genetic inactivation of Cys38-S- completely abrogated ALV fusion and infection. Remarkably, Cys38-S- does not mediate isomerization of the SU-TM disulfide bond and is not required for Tva-induced activation of TM, including pre-hairpin association with membranes and low pH assembly of helical bundles. These findings indicate that, contrary to current models, receptor activation of TM is not sufficient for ALV fusion and infection and that formation of a reactive thiolate is an additional receptor-dependent step.Jason G SmithJames M CunninghamPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 3, Iss 12, p e198 (2007)
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 Jason G Smith James M Cunningham Receptor-induced thiolate couples Env activation to retrovirus fusion and infection.
description	According to current models of retrovirus infection, receptor binding to the surface subunit (SU) of the envelope glycoprotein (Env) triggers a conformational change in the transmembrane subunit (TM) that mediates virus fusion to cell membranes. To understand how this occurs, we investigated the role of the receptor Tva in avian leukosis virus-A (ALV-A) infection. We find that Tva binding induced the formation of a reactive thiolate on Cys38 (Cys38-S- in SU. Both chemical and genetic inactivation of Cys38-S- completely abrogated ALV fusion and infection. Remarkably, Cys38-S- does not mediate isomerization of the SU-TM disulfide bond and is not required for Tva-induced activation of TM, including pre-hairpin association with membranes and low pH assembly of helical bundles. These findings indicate that, contrary to current models, receptor activation of TM is not sufficient for ALV fusion and infection and that formation of a reactive thiolate is an additional receptor-dependent step.
format	article
author	Jason G Smith James M Cunningham
author_facet	Jason G Smith James M Cunningham
author_sort	Jason G Smith
title	Receptor-induced thiolate couples Env activation to retrovirus fusion and infection.
title_short	Receptor-induced thiolate couples Env activation to retrovirus fusion and infection.
title_full	Receptor-induced thiolate couples Env activation to retrovirus fusion and infection.
title_fullStr	Receptor-induced thiolate couples Env activation to retrovirus fusion and infection.
title_full_unstemmed	Receptor-induced thiolate couples Env activation to retrovirus fusion and infection.
title_sort	receptor-induced thiolate couples env activation to retrovirus fusion and infection.
publisher	Public Library of Science (PLoS)
publishDate	2007
url	https://doaj.org/article/83a121dcb80b48e1a8ee66bebac040c0
work_keys_str_mv	AT jasongsmith receptorinducedthiolatecouplesenvactivationtoretrovirusfusionandinfection AT jamesmcunningham receptorinducedthiolatecouplesenvactivationtoretrovirusfusionandinfection
_version_	1718414466528313344

Receptor-induced thiolate couples Env activation to retrovirus fusion and infection.

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