Baculovirus Expression of the Respiratory Syncytial Virus Fusion Protein using Trichoplusia ni Insect Cells View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1997-01

AUTHORS

ELLEN Snell, SONIA Sanhueza, LUCY Gisonni, MARK Parrington, MICHEL Klein, PHILIP Wang, RUN-PAN Du, STEPHEN Cockle, WEI-YAO Yan, MARY Ewasyshyn, PHILIP Wyde

ABSTRACT

Respiratory syncytial virus (RSV) is a major viral pathogen responsible for severe respiratory tract infections in infants, young children, and the elderly. The RSV fusion (F) protein is highly conserved among RSV subgroups A and B and is the major protective immunogen. A genetically-engineered version of the RSV F protein was produced in insect cells using the baculovirus expression system. To express a secreted form of this protein, the transmembrane domain was eliminated by removing the region of the gene encoding 48 amino acids at the C-terminus. Production of the truncated RSV F protein (RSV-Fs) was compared in two different insect cell lines, Spodoptera frugiperda (Sf9) and Trichoplusia ni (High Five). The yield of RSV-Fs secreted from High Five insect cells was over 7-fold higher than that from Sf9 insect cells. Processing of the RSV-Fs protein was also different in the two insect cell lines. N-terminal sequencing demonstrated that while most of the RSV-Fs protein secreted by High Five cells was correctly processed at the F2-F1 proteolytic cleavage site, most of the RSV-Fs protein secreted by Sf9 cells was unprocessed or incorrectly processed. Antigenicity of the major RSV F neutralization epitopes was maintained in the RSV-Fs protein secreted from High Five cells. The RSV-specific neutralizing antibody titres in the sera of cotton rats immunized with the RSV-Fs protein were equivalent to those in the sera of animals intranasally inoculated with live RSV. Animals immunized with either live RSV or the immunoaffinity purified RSV-Fs protein from High Five cells were completely protected against live virus challenge. More... »

PAGES

63-72

Identifiers

URI

http://scigraph.springernature.com/pub.10.1023/a:1007939524088

DOI

http://dx.doi.org/10.1023/a:1007939524088

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1038895914

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/9208456


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Download the RDF metadata as:  json-ld nt turtle xml License info

HOW TO GET THIS DATA PROGRAMMATICALLY:

JSON-LD is a popular format for linked data which is fully compatible with JSON.

curl -H 'Accept: application/ld+json' 'https://scigraph.springernature.com/pub.10.1023/a:1007939524088'

N-Triples is a line-based linked data format ideal for batch operations.

curl -H 'Accept: application/n-triples' 'https://scigraph.springernature.com/pub.10.1023/a:1007939524088'

Turtle is a human-readable linked data format.

curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/pub.10.1023/a:1007939524088'

RDF/XML is a standard XML format for linked data.

curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1023/a:1007939524088'


 

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319 schema:name Connaught Centre for Biotechnology Research, Connaught Laboratories Ltd., 1755 Steeles Ave. West, M2R 3T4, North York, Ontario, Canada
320 rdf:type schema:Organization
 




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