About: Pseudomonas aeruginosa lectin LecB impairs keratinocyte fitness by abrogating growth factor signalling

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About: Pseudomonas aeruginosa lectin LecB impairs keratinocyte fitness by abrogating growth factor signalling 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	Pseudomonas aeruginosa lectin LecB impairs keratinocyte fitness by abrogating growth factor signalling
Creator	Reggiori, Fulvio Mari, Muriel Claudinon, Julie Geiger, Roger Gretzmeier, Christine Kiritsi, Dimitra Kleiser, Svenja Landi, Alessia Nyström, Alexander Römer, Winfried Thünauer, Roland Wilhelm, Isabel Wolf, Tobias
Source	PMC
abstract	Lectins are glycan-binding proteins with no catalytic activity and ubiquitously expressed in nature. Numerous bacteria use lectins to efficiently bind to epithelia, thus facilitating tissue colonisation. Wounded skin is one of the preferred niches for Pseudomonas aeruginosa, which has developed diverse strategies to impair tissue repair processes and promote infection. Here, we analyse the effect of the P. aeruginosa fucose-binding lectin LecB on human keratinocytes and demonstrate that it triggers events in the host, upon binding to fucosylated residues on cell membrane receptors, which extend beyond its role as an adhesion molecule. We found that LecB associates with insulin-like growth factor-1 receptor and dampens its signalling, leading to the arrest of cell cycle. In addition, we describe a novel LecB-triggered mechanism to down-regulate host cell receptors by showing that LecB leads to insulin-like growth factor-1 receptor internalisation and subsequent missorting towards intracellular endosomal compartments, without receptor activation. Overall, these data highlight that LecB is a multitask virulence factor that, through subversion of several host pathways, has a profound impact on keratinocyte proliferation and survival.
has issue date	2019-11-15(xsd:dateTime)
bibo:doi	10.26508/lsa.201900422
bibo:pmid	31732693
has license	cc-by
sha1sum (hex)	082892d44934e61adfef5cd6d5867439e30b183b
schema:url	https://doi.org/10.26508/lsa.201900422
resource representing a document's title	Pseudomonas aeruginosa lectin LecB impairs keratinocyte fitness by abrogating growth factor signalling
has PubMed Central identifier	PMC6858607
has PubMed identifier	31732693
schema:publication	Life Sci Alliance
resource representing a document's body	covid:082892d44934e61adfef5cd6d5867439e30b183b#body_text
is schema:about of	named entity 'growth factor' named entity 'P. aeruginosa' named entity 'P. AERUGINOSA' named entity 'LECTIN' named entity 'LECB' named entity 'FITNESS' named entity 'IMPAIRS' named entity 'SIGNALLING' named entity 'KERATINOCYTE' named entity 'GROWTH FACTOR' named entity 'ubiquitin' named entity 'IGF-1R' named entity 'GAPDH' named entity 'IGF1R' named entity 'biotinylation' named entity 'IGF-1R' named entity 'keratinocytes' named entity 'present tense' named entity 'western blot' named entity 'IGF-1R' named entity 'stratum corneum' named entity 'bafilomycin A1' named entity 'Life Science Alliance' named entity 'Lectin' named entity 'L-fucose' named entity 'FACS' named entity 'immunofluorescence' named entity 'plasma membrane' named entity 'ubiquitinated protein' named entity 'cell cycle' named entity 'endocytosis' named entity 'cytochalasin' named entity 'EGFR' named entity 'intracellular receptor' named entity 'growth factor' named entity 'biotinylation' named entity 'sorting signal' named entity 'IGF-1R' named entity 'receptor internalisation' named entity 'PDFs' named entity 'ubiquitin' named entity 'L-fucose' named entity 'IGF-1R' named entity 'ATG13' named entity 'chloroquine' named entity 'Rab9' named entity 'lectin' named entity 'PDF' named entity 'Ubiquitination' named entity 'siRNA' named entity 'Life Science Alliance' named entity 'text summarizing' named entity 'ATG13' named entity 'mTor' named entity 'autophagosome' named entity 'Vps34' named entity 'IGF-1R' named entity 'IGF-1R' named entity 'lectin' named entity 'sorting signal' named entity 'phagocytosis' named entity 'clathrin' named entity 'lysosome' named entity 'P. aeruginosa' named entity 'IGF-1R' named entity 'bafilomycin A1' named entity 'phagocytosis' named entity 'co-immunoprecipitated' named entity 'fucose'

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