Theileria parvaSporozoite Entry into Bovine Lymphocytes Involves both Parasite and Host Cell Signal Transduction Processes

1996 ◽  
Vol 84 (3) ◽  
pp. 344-354 ◽  
Author(s):  
Michael K. Shaw
Keyword(s):  
Signal Transduction ◽  
Host Cell ◽  
Cell Signal ◽  
Cell Signal Transduction ◽  
Bovine Lymphocytes

Host Cell Signal Transduction during Listeria monocytogenes Infection

1999 ◽  
Vol 372 (1) ◽  
pp. 166-172 ◽  
Author(s):  
Michael Kuhn ◽  
Thilo Pfeuffer ◽  
Lars Greiffenberg ◽  
Werner Goebel
Keyword(s):  
Signal Transduction ◽  
Listeria Monocytogenes ◽  
Host Cell ◽  
Cell Signal ◽  
Listeria Monocytogenes Infection ◽  
Cell Signal Transduction

scholarly journals Dissection of Host Cell Signal Transduction during Acinetobacter baumannii – Triggered Inflammatory Response

PLoS ONE ◽  
2010 ◽  
Vol 5 (4) ◽  
pp. e10033 ◽  
Author(s):  
Catalina March ◽  
Verónica Regueiro ◽  
Enrique Llobet ◽  
David Moranta ◽  
Pau Morey ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Inflammatory Response ◽  
Acinetobacter Baumannii ◽  
Host Cell ◽  
Cell Signal ◽  
Cell Signal Transduction

scholarly journals Modulation of Host Cell Signal Transduction Pathways by Helicobacter Pylori Infection

2005 ◽  
Vol 19 (7) ◽  
pp. 415-420 ◽  
Author(s):  
Peter JM Ceponis ◽  
Nicola L Jones
Keyword(s):  
Signal Transduction ◽  
Helicobacter Pylori ◽  
Host Cell ◽  
Current Knowledge ◽  
Vacuolating Cytotoxin ◽  
Cell Signal ◽  
Cytotoxin Associated Gene A ◽  
Cell Signal Transduction ◽  
Present Summary ◽  
Study Group Meeting

Bacterial pathogens modulate host cell signal transduction responses to establish infection and cause disease. The purpose of the present summary, first presented at the Canadian Helicobacter Study Group meeting, is to discuss current knowledge of specific Helicobacter pylori factors, including the vacuolating cytotoxin, cytotoxin-associated gene A and the type four secretion system encoded by the cytotoxin-associated gene pathogenicity island and review the host cell signal transduction cascades that they modulate.

Hijacking host cell signal transduction mechanisms during infection with enteropathogenic Escherichia coli

1996 ◽  
Vol 24 (2) ◽  
pp. 552-558 ◽  
Author(s):  
T. J. Baldwin ◽  
S. Knutton ◽  
R. Haigh ◽  
P. H. Williams ◽  
H. M. Palmer ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Signal Transduction ◽  
Host Cell ◽  
Enteropathogenic Escherichia Coli ◽  
Cell Signal ◽  
Transduction Mechanisms ◽  
Cell Signal Transduction

scholarly journals Polyunsaturated Fatty Acids Inhibit T Cell Signal Transduction by Modification of Detergent-insoluble Membrane Domains

1998 ◽  
Vol 143 (3) ◽  
pp. 637-644 ◽  
Author(s):  
Thomas M. Stulnig ◽  
Markus Berger ◽  
Thomas Sigmund ◽  
Daniel Raederstorff ◽  
Hannes Stockinger ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Fatty Acids ◽  
T Cells ◽  
T Cell ◽  
Polyunsaturated Fatty Acids ◽  
Membrane Domains ◽  
Protein Tyrosine ◽  
Cell Signal ◽  
Family Protein ◽  
Cell Signal Transduction

Polyunsaturated fatty acids (PUFAs) exert immunosuppressive effects, but the molecular alterations leading to T cell inhibition are not yet elucidated. Signal transduction seems to involve detergent-resistant membrane domains (DRMs) acting as functional rafts within the plasma membrane bilayer with Src family protein tyrosine kinases being attached to their cytoplasmic leaflet. Since DRMs include predominantly saturated fatty acyl moieties, we investigated whether PUFAs could affect T cell signaling by remodeling of DRMs. Jurkat T cells cultured in PUFA-supplemented medium showed a markedly diminished calcium response when stimulated via the transmembrane CD3 complex or glycosyl phosphatidylinositol (GPI)- anchored CD59. Immunofluorescence studies indicated that CD59 but not Src family protein tyrosine kinase Lck remained in a punctate pattern after PUFA enrichment. Analysis of DRMs revealed a marked displacement of Src family kinases (Lck, Fyn) from DRMs derived from PUFA-enriched T cells compared with controls, and the presence of Lck in DRMs strictly correlated with calcium signaling. In contrast, GPI-anchored proteins (CD59, CD48) and ganglioside GM1, both residing in the outer membrane leaflet, remained in the DRM fraction. In conclusion, PUFA enrichment selectively modifies the cytoplasmic layer of DRMs and this alteration could underlie the inhibition of T cell signal transduction by PUFAs.

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