About: A Protective and Safe Intranasal RSV Vaccine Based on a Recombinant Prefusion-Like Form of the F Protein Bound to Bacterium-Like Particles

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About: A Protective and Safe Intranasal RSV Vaccine Based on a Recombinant Prefusion-Like Form of the F Protein Bound to Bacterium-Like Particles Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	A Protective and Safe Intranasal RSV Vaccine Based on a Recombinant Prefusion-Like Form of the F Protein Bound to Bacterium-Like Particles
Creator	Rottier, Peter Widjaja, Ivy Rigter, Alan Leenhouts, Kees Versantvoort, Hanneke Coenjaerts, Frank Cornelis, A De Haan, Haijema, Bert Van Roosmalen, Maarten
Source	PMC
abstract	Respiratory syncytial virus (RSV) is an important cause of respiratory tract disease in infants and the elderly. Currently, no licensed vaccine against RSV is available. Here we describe the development of a safe and effective intranasal subunit vaccine that is based on recombinant fusion (F) protein bound to the surface of immunostimulatory bacterium-like particles (BLPs) derived from the food-grade bacterium Lactococcus lactis. Different variants of F were analyzed with respect to their conformation and reactivity with neutralizing antibodies, assuming that F proteins mimicking the metastable prefusion form of RSV F expose a more extensive and relevant epitope repertoire than F proteins corresponding to the postfusion structure. Our results indicate that the recombinant soluble ectodomain of RSV F readily adopts a postfusion conformation, generation of which cannot be prevented by C-terminal addition of a trimerization motif, but whose formation is prevented by mutation of the two furin cleavage sites in F. While the putative postfusion form of F is recognized well by the monoclonal antibody Palivizumab, this is much less so for the more potently neutralizing, prefusion-specific antibodies D25 and AM22. Both addition of the trimerization motif and mutation of the furin cleavage sites increased the reactivity of F with D25 and AM22, with the highest reactivity being observed for F proteins in which both these features were combined. Intranasal vaccination of mice or cotton rats with BLPs loaded with this latter prefusion-like F protein (BLP-F), resulted in the potent induction of F-specific immunoglobulins and in significantly decreased virus titers in the lungs upon RSV challenge. Moreover, and in contrast to animals vaccinated with formalin-inactivated RSV, animals that received BLP-F exhibited high levels of F-specific secretory IgA in the nose and RSV-neutralizing antibodies in sera, but did not show symptoms of enhanced disease after challenge with RSV.
has issue date	2013-08-12(xsd:dateTime)
bibo:doi	10.1371/journal.pone.0071072
bibo:pmid	23951084
has license	cc-by
sha1sum (hex)	c61f5c4971f07156d3c1d9dd76de4b158855ecc1
schema:url	https://doi.org/10.1371/journal.pone.0071072
resource representing a document's title	A Protective and Safe Intranasal RSV Vaccine Based on a Recombinant Prefusion-Like Form of the F Protein Bound to Bacterium-Like Particles
has PubMed Central identifier	PMC3741363
has PubMed identifier	23951084
schema:publication	PLoS One
resource representing a document's body	covid:c61f5c4971f07156d3c1d9dd76de4b158855ecc1#body_text
is schema:about of	named entity 'high' named entity 'antibodies' named entity 'virus' named entity 'neutralizing' named entity 'reactivity' named entity 'features' named entity 'reactivity' named entity 'BACTERIUM' named entity 'RECOMBINANT' named entity 'NOSE' named entity 'BUT' named entity 'INDUCTION' named entity 'FOOD' named entity 'CHALLENGE' named entity 'STRUCTURE' named entity 'FORMALIN' named entity 'F PROTEIN' named entity 'D25' named entity 'SPECIFIC' named entity 'SPECIFIC IMMUNOGLOBULINS' named entity 'HIGH' named entity 'DESCRIBE' named entity 'SOLUBLE' named entity 'BASED' named entity 'LICENSED VACCINE' named entity 'COMBINED' named entity 'IMPORTANT' named entity 'GENERATION' named entity 'DECREASED' named entity 'VACCINATED' named entity 'ANALYZED' named entity 'INCREASED' named entity 'ENHANCED' named entity 'THE LUNGS' named entity 'SURFACE' named entity 'AVAILABLE' named entity 'RECOMBINANT' named entity 'RESPIRATORY SYNCYTIAL VIRUS' named entity 'DID' named entity 'LEVELS' named entity 'MONOCLONAL ANTIBODY' named entity 'DEVELOPMENT' named entity 'RESULTS' named entity 'RECEIVED' named entity 'EPITOPE' named entity 'SECRETORY IGA' named entity 'ELDERLY' named entity 'CAUSE' named entity 'GRADE' named entity 'EXTENSIVE' named entity 'EXPOSE' named entity 'ADDITION' named entity 'RESPIRATORY TRACT DISEASE' named entity 'NEUTRALIZING ANTIBODIES' named entity 'EFFECTIVE' named entity 'REACTIVITY' named entity 'SUBUNIT VACCINE' named entity 'DERIVED' named entity 'LOADED' named entity 'FORM' named entity 'RSV VACCINE' named entity 'RESPECT' named entity 'PROTEIN ' named entity 'OBSERVED' named entity 'SAFE' named entity 'FUSION' named entity 'BEING' named entity 'SERA' named entity 'MICE' named entity 'MOTIF' named entity 'LACTOCOCCUS LACTIS' named entity 'PROTEIN BOUND'

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