Full-length, glycosylated NSP4 is localized to plasma membrane caveolae by a novel raft isolation technique.

Full-length, glycosylated NSP4 is localized to plasma membrane caveolae by a novel raft isolation technique. Research Abstract Details 

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Full-length, glycosylated NSP4 is localized to plasma membrane caveolae by a novel raft isolation technique. Abstract Text:

Stephen M Storey,Thomas F Gibbons,Cecelia V Williams,Rebecca D Parr,Friedhelm Schroeder,Judith M Ball,

Rotavirus NSP4, initially characterized as an endoplasmic reticulum intracellular receptor, is a multifunctional viral enterotoxin that induces diarrhea in murine pups. There have been recent reports of the secretion of a cleaved NSP4 fragment (residues 112 to 175) and of the association of NSP4 with LC3-positive autophagosomes, raft membranes, and microtubules. To determine if NSP4 traffics to a specific subset of rafts at the plasma membrane, we isolated caveolae from plasma membrane-enriched material that yielded caveola membranes free of endoplasmic reticulum and nonraft plasma membrane markers. Analyses of the newly isolated caveolae from rotavirus-infected MDCK cells revealed full-length, high-mannose glycosylated NSP4. The lack of Golgi network-specific processing of the caveolar NSP4 glycans supports studies showing that NSP4 bypasses the Golgi apparatus. Confocal imaging showed the colocalization of NSP4 with caveolin-1 early and late in infection, elucidating the temporal and spatial NSP4-caveolin-1 association during infection. These data were extended with fluorescent resonance energy transfer analyses that confirmed the NSP4 and caveolin-1 interaction in that the specific fluorescently tagged antibodies were within 10 nm of each other during infection. Cells transfected with NSP4 showed patterns of staining and colocalization with caveolin-1 similar to those of infected cells. This study presents an endoplasmic reticulum contaminant-free caveola isolation protocol; describes the presence of full-length, endoglycosidase H-sensitive NSP4 in plasma membrane caveolae; provides confirmation of the NSP4-caveolin interaction in the presence and absence of other viral proteins; and provides a final plasma membrane destination for Golgi network-bypassing NSP4 transport.

Full-length, glycosylated NSP4 is localized to plasma membrane caveolae by a novel raft isolation technique. Publishing Authors By Initials

SM Storey,TF Gibbons,CV Williams,RD Parr,F Schroeder,JM Ball,

For similar proteins: viral proteins: viral nonstructural proteins research abstracts see: proteins: viral proteins: viral nonstructural proteins research

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Full-length, glycosylated NSP4 is localized to plasma membrane caveolae by a novel raft isolation technique. Journal Published:

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

Journal: Journal of virology

VOLUME: 81

Page Numbers: 5472-83

Journal Abbreviation: J. Virol.

ISSN: 0022-538X

DAY: 21

MONTH: 03

YEAR: 2007

Full-length, glycosylated NSP4 is localized to plasma membrane caveolae by a novel raft isolation technique. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 113724

Full-length, glycosylated NSP4 is localized to plasma membrane caveolae by a novel raft isolation technique. Keywords Mesh Terms:

KEYWORDS: Viral Nonstructural Proteins

MESH TERMS: metabolism

Chemical & Substance for Abstract: Full-length, glycosylated NSP4 is localized to plasma membrane caveolae by a novel raft isolation technique. Information

Substance Name: Octoxynol

Registry Number: 9002-93-1

Grant and Affiliation Information for Full-length, glycosylated NSP4 is localized to plasma membrane caveolae by a novel raft isolation technique.

AFFILIATION: Department of Pathobiology, TVMC, Texas A and M University, TAMU 4467, College Station, TX 77843-4467, USA.

Country: United States

AGENCY: United States NIAID

GRANT: T32 AI 572072-01A1

ACRONYM: AI

MEDLINETA: J Virol

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