Thiol/disulfide exchange is required for membrane fusion directed by the Newcastle disease virus fusion protein.

Thiol/disulfide exchange is required for membrane fusion directed by the Newcastle disease virus fusion protein. Research Abstract Details 

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Thiol/disulfide exchange is required for membrane fusion directed by the Newcastle disease virus fusion protein. Abstract Text:

Surbhi Jain,Lori W McGinnes,Trudy G Morrison,

Newcastle disease virus (NDV), an avian paramyxovirus, initiates infection with attachment of the viral hemagglutinin-neuraminidase (HN) protein to sialic acid-containing receptors, followed by fusion of viral and cell membranes, which is mediated by the fusion (F) protein. Like all class 1 viral fusion proteins, the paramyxovirus F protein is thought to undergo dramatic conformational changes upon activation. How the F protein accomplishes extensive conformational rearrangements is unclear. Since several viral fusion proteins undergo disulfide bond rearrangement during entry, we asked if similar rearrangements occur in NDV proteins during entry. We found that inhibitors of cell surface thiol/disulfide isomerase activity--5'5-dithio-bis(2-nitrobenzoic acid) (DTNB), bacitracin, and anti-protein disulfide isomerase antibody--inhibited cell-cell fusion and virus entry but had no effect on cell viability, glycoprotein surface expression, or HN protein attachment or neuraminidase activities. These inhibitors altered the conformation of surface-expressed F protein, as detected by conformation-sensitive antibodies. Using biotin maleimide (MPB), a reagent that binds to free thiols, free thiols were detected on surface-expressed F protein, but not HN protein. The inhibitors DTNB and bacitracin blocked the detection of these free thiols. Furthermore, MPB binding inhibited cell-cell fusion. Taken together, our results suggest that one or several disulfide bonds in cell surface F protein are reduced by the protein disulfide isomerase family of isomerases and that F protein exists as a mixture of oxidized and reduced forms. In the presence of HN protein, only the reduced form may proceed to refold into additional intermediates, leading to the fusion of membranes.

Thiol/disulfide exchange is required for membrane fusion directed by the Newcastle disease virus fusion protein. Publishing Authors By Initials

S Jain,LW McGinnes,TG Morrison,

For similar biological phenomena, cell phenomena, and immunity: biological phenomena: microbiologic phenomena: viral physiology: virus attachment research abstracts see: biological phenomena, cell phenomena, and immunity: biological phenomena: microbiologic phenomena: viral physiology: virus attachment research

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Thiol/disulfide exchange is required for membrane fusion directed by the Newcastle disease virus fusion protein. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Journal of virology

VOLUME: 81

Page Numbers: 2328-39

Journal Abbreviation: J. Virol.

ISSN: 0022-538X

DAY: 6

MONTH: 12

YEAR: 2006

Thiol/disulfide exchange is required for membrane fusion directed by the Newcastle disease virus fusion protein. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 113724

Thiol/disulfide exchange is required for membrane fusion directed by the Newcastle disease virus fusion protein. Keywords Mesh Terms:

KEYWORDS: Virus Attachment

MESH TERMS: drug effects

Chemical & Substance for Abstract: Thiol/disulfide exchange is required for membrane fusion directed by the Newcastle disease virus fusion protein. Information

Substance Name: Protein Disulfide-Isomerase

Registry Number: EC 5.3.4.1

Grant and Affiliation Information for Thiol/disulfide exchange is required for membrane fusion directed by the Newcastle disease virus fusion protein.

AFFILIATION: Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655, USA.

Country: United States

AGENCY: United States NIAID

GRANT: AI 30572

ACRONYM: AI

MEDLINETA: J Virol

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