Linked Life Data

21179438

Source:http://linkedlifedata.com/resource/pubmed/id/21179438

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2010-12-23
pubmed:abstractText
Yersinia pestis, the causative agent of bubonic plague, employs its type III secretion system to inject toxins into target cells, a crucial step in infection establishment. LcrV is an essential component of the T3SS of Yersinia spp, and is able to associate at the tip of the secretion needle and take part in the translocation of anti-host effector proteins into the eukaryotic cell cytoplasm. Upon cell contact, LcrV is also released into the surrounding medium where it has been shown to block the normal inflammatory response, although details of this mechanism have remained elusive. In this work, we reveal a key aspect of the immunomodulatory function of LcrV by showing that it interacts directly and with nanomolar affinity with the inflammatory cytokine IFN?. In addition, we generate specific IFN? mutants that show decreased interaction capabilities towards LcrV, enabling us to map the interaction region to two basic C-terminal clusters of IFN?. Lastly, we show that the LcrV-IFN? interaction can be disrupted by a number of inhibitors, some of which display nanomolar affinity. This study thus not only identifies novel potential inhibitors that could be developed for the control of Yersinia-induced infection, but also highlights the diversity of the strategies used by Y. pestis to evade the immune system, with the hijacking of pleiotropic cytokines being a long-range mechanism that potentially plays a key role in the severity of plague.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1932-6203
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
5
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
e15242
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Hijacking of the pleiotropic cytokine interferon-? by the type III secretion system of Yersinia pestis.
pubmed:affiliation
Institut de Biologie Structurale, UMR 5075 (Comissariat à l'Enérgie Atomique/Centre National de la Recherche Scientifique/Université Grenoble I), Grenoble, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't