About: Immunogenetic Mechanisms Driving Norovirus GII.4 Antigenic Variation

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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	Immunogenetic Mechanisms Driving Norovirus GII.4 Antigenic Variation
Creator	Beltramello, M Corti, D Donaldson, E Swanstrom, J
Source	PMC
abstract	Noroviruses are the principal cause of epidemic gastroenteritis worldwide with GII.4 strains accounting for 80% of infections. The major capsid protein of GII.4 strains is evolving rapidly, resulting in new epidemic strains with altered antigenic potentials. To test if antigenic drift may contribute to GII.4 persistence, human memory B cells were immortalized and the resulting human monoclonal antibodies (mAbs) characterized for reactivity to a panel of time-ordered GII.4 virus-like particles (VLPs). Reflecting the complex exposure history of the volunteer, human anti-GII.4 mAbs grouped into three VLP reactivity patterns; ancestral (1987–1997), contemporary (2004–2009), and broad (1987–2009). NVB 114 reacted exclusively to the earliest GII.4 VLPs by EIA and blockade. NVB 97 specifically bound and blocked only contemporary GII.4 VLPs, while NBV 111 and 43.9 exclusively reacted with and blocked variants of the GII.4.2006 Minerva strain. Three mAbs had broad GII.4 reactivity. Two, NVB 37.10 and 61.3, also detected other genogroup II VLPs by EIA but did not block any VLP interactions with carbohydrate ligands. NVB 71.4 cross-neutralized the panel of time-ordered GII.4 VLPs, as measured by VLP-carbohydrate blockade assays. Using mutant VLPs designed to alter predicted antigenic epitopes, two evolving, GII.4-specific, blockade epitopes were mapped. Amino acids 294–298 and 368–372 were required for binding NVB 114, 111 and 43.9 mAbs. Amino acids 393–395 were essential for binding NVB 97, supporting earlier correlations between antibody blockade escape and carbohydrate binding variation. These data inform VLP vaccine design, provide a strategy for expanding the cross-blockade potential of chimeric VLP vaccines, and identify an antibody with broadly neutralizing therapeutic potential for the treatment of human disease. Moreover, these data support the hypothesis that GII.4 norovirus evolution is heavily influenced by antigenic variation of neutralizing epitopes and consequently, antibody-driven receptor switching; thus, protective herd immunity is a driving force in norovirus molecular evolution.
has issue date	2012-05-17(xsd:dateTime)
bibo:doi	10.1371/journal.ppat.1002705
bibo:pmid	22615565
has license	cc-by
sha1sum (hex)	dc6666eb8156bd4638809009f795ebd4a7843569
schema:url	https://doi.org/10.1371/journal.ppat.1002705
resource representing a document's title	Immunogenetic Mechanisms Driving Norovirus GII.4 Antigenic Variation
has PubMed Central identifier	PMC3355092
has PubMed identifier	22615565
schema:publication	PLoS Pathog
resource representing a document's body	covid:dc6666eb8156bd4638809009f795ebd4a7843569#body_text
is schema:about of	named entity 'norovirus' named entity 'rapidly' named entity 'escape' named entity 'reactivity' named entity 'capsid' named entity 'binding' named entity 'VLP' named entity 'neutralizing' named entity 'history' named entity 'human' named entity 'assays' named entity 'Driving' named entity 'DRIVING' named entity 'HERD IMMUNITY' named entity 'DID' named entity 'REFLECTING' named entity 'MAJOR CAPSID PROTEIN' named entity 'CAUSE' named entity 'NOROVIRUSES' named entity 'INTERACTIONS' named entity 'ANTIGENIC VARIATION' named entity 'EPIDEMIC' named entity 'INFECTIONS' named entity 'TREATMENT' named entity 'MINERVA' named entity 'TIME' named entity 'POTENTIALS' named entity '114' named entity 'PROVIDE' named entity 'VARIATION' named entity 'SUPPORT' named entity '111' named entity 'RAPIDLY' named entity 'BLOCKADE' named entity 'EVOLVING' named entity 'CONTRIBUTE ' named entity 'IS A' named entity 'THERAPEUTIC' named entity '368' named entity 'RESULTING' named entity 'ALTER' named entity 'STRAIN' named entity 'EVOLUTION' named entity 'ANTIBODY' named entity 'HUMAN DISEASE' named entity '372' named entity 'COMPLEX EXPOSURE' named entity 'VARIANTS' named entity '393' named entity 'NOROVIRUS' named entity 'BLOCK' named entity 'VACCINE DESIGN' named entity 'HUMAN' named entity 'LIGANDS' named entity 'BROAD' named entity 'STRAINS' named entity 'PANEL' named entity 'MUTANT' named entity 'EXPANDING' named entity 'EXPOSURE HISTORY' named entity 'ALTERED' named entity 'CHIMERIC' named entity 'HISTORY OF' named entity 'GROUPED' named entity 'THESE' named entity 'IMMUNOGENETIC' named entity 'EPITOPES' named entity 'IMMORTALIZED' named entity 'MONOCLONAL ANTIBODIES' named entity 'CHARACTERIZED' named entity 'CROSS' named entity 'ORDERED' named entity 'MAPPED' named entity 'VACCINES' named entity 'AMINO ACIDS' named entity 'ESCAPE' named entity 'VLPS' named entity 'RESULTING IN'

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