About: The “sweet” side of a long pentraxin: how glycosylation affects PTX3 functions in innate immunity and inflammation

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About: The “sweet” side of a long pentraxin: how glycosylation affects PTX3 functions in innate immunity and inflammation 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	The “sweet” side of a long pentraxin: how glycosylation affects PTX3 functions in innate immunity and inflammation
Creator	Mantovani, Alberto Garlanda, Cecilia Reading, Patrick Bottazzi, Barbara Inforzato, Antonio Barbati, Elisa Hutchinson, Andrew Moseley, Gregory
Source	Medline; PMC
abstract	Innate immunity represents the first line of defense against pathogens and plays key roles in activation and orientation of the adaptive immune response. The innate immune system comprises both a cellular and a humoral arm. Components of the humoral arm include soluble pattern recognition molecules (PRMs) that recognize pathogen-associated molecular patterns and initiate the immune response in coordination with the cellular arm, therefore acting as functional ancestors of antibodies. The long pentraxin PTX3 is a prototypic soluble PRM that is produced at sites of infection and inflammation by both somatic and immune cells. Gene targeting of this evolutionarily conserved protein has revealed a non-redundant role in resistance to selected pathogens. Moreover, PTX3 exerts important functions at the crossroad between innate immunity, inflammation, and female fertility. The human PTX3 protein contains a single N-glycosylation site that is fully occupied by complex type oligosaccharides, mainly fucosylated and sialylated biantennary glycans. Glycosylation has been implicated in a number of PTX3 activities, including neutralization of influenza viruses, modulation of the complement system, and attenuation of leukocyte recruitment. Therefore, this post translational modification might act as a fine tuner of PTX3 functions in native immunity and inflammation. Here we review the studies on PTX3, with emphasis on the glycan-dependent mechanisms underlying pathogen recognition and crosstalk with other components of the innate immune system.
has issue date	2013-01-07(xsd:dateTime)
bibo:doi	10.3389/fimmu.2012.00407
bibo:pmid	23316195
has license	cc-by
sha1sum (hex)	16eb672447620efa83aa59f913d690a95240f488
schema:url	https://doi.org/10.3389/fimmu.2012.00407
resource representing a document's title	The “sweet” side of a long pentraxin: how glycosylation affects PTX3 functions in innate immunity and inflammation
has PubMed Central identifier	PMC3539679
has PubMed identifier	23316195
schema:publication	Front Immunol
resource representing a document's body	covid:16eb672447620efa83aa59f913d690a95240f488#body_text
is schema:about of	named entity 'PATTERNS' named entity 'LEUKOCYTE RECRUITMENT' named entity 'ACT' named entity 'INFECTION' named entity 'CROSSTALK' named entity 'IMMUNE RESPONSE' named entity 'FUNCTIONAL' named entity 'COORDINATION' named entity 'PTX3 PROTEIN' named entity 'LONG' named entity 'INNATE IMMUNE SYSTEM' named entity 'REVIEW' named entity 'IMPORTANT' named entity 'PLAYS' named entity 'SELECTED' named entity 'GLYCAN' named entity 'MOLECULAR' named entity 'FULLY' named entity 'IMMUNE CELLS' named entity 'PTX3' named entity 'HUMAN' named entity 'MECHANISMS' named entity 'SOLUBLE' named entity 'NUMBER OF' named entity 'DEFENSE' named entity 'COMPONENTS' named entity 'ANCESTORS' named entity 'FUCOSYLATED' named entity 'INNATE IMMUNITY' named entity 'antibodies' named entity 'native' named entity 'fine' named entity 'immunity' named entity 'Gene targeting' named entity 'inflammation' named entity 'pentraxin' named entity 'INFLAMMATION' named entity 'FINE' named entity 'IS A' named entity 'CONSERVED' named entity 'STUDIES' named entity 'UNDERLYING' named entity 'REVEALED' named entity 'RESISTANCE TO' named entity 'MOLECULES' named entity 'EXERTS' named entity 'PATTERN RECOGNITION' named entity 'ARM' named entity 'ORIENTATION' named entity 'ACTIVITIES' named entity 'ROLE' named entity 'TUNER' named entity 'POST TRANSLATIONAL MODIFICATION' named entity 'ROLES' named entity 'NON-' named entity 'FUNCTIONS' named entity 'LONG' named entity 'GLYCOSYLATION' named entity 'ASSOCIATED' named entity 'COMPLEX TYPE' named entity 'ACTIVATION' named entity 'INITIATE' named entity 'CONTAINS' named entity 'OLIGOSACCHARIDES' named entity 'N-GLYCOSYLATION SITE' named entity 'GENE TARGETING' named entity 'PATHOGEN' named entity 'SITES' named entity 'BIANTENNARY' named entity 'PRM' named entity 'INCLUDING' named entity 'INNATE IMMUNITY' named entity 'COMPLEMENT SYSTEM' named entity 'SOMATIC'

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