Host Cell Chaperones Hsp70/Hsp90 and Peptidyl-Prolyl Cis/Trans Isomerases Are Required for the Membrane Translocation of Bacterial ADP-Ribosylating Toxins

Author(s):  
Katharina Ernst ◽  
Leonie Schnell ◽  
Holger Barth

2010 ◽  
Vol 78 (7) ◽  
pp. 2927-2936 ◽  
Author(s):  
Steven P. O'Hara ◽  
Gabriella B. Gajdos ◽  
Christy E. Trussoni ◽  
Patrick L. Splinter ◽  
Nicholas F. LaRusso

ABSTRACT Internalization of the obligate intracellular apicomplexan parasite, Cryptosporidium parvum, results in the formation of a unique intramembranous yet extracytoplasmic niche on the apical surfaces of host epithelial cells, a process that depends on host cell membrane extension. We previously demonstrated that efficient C. parvum invasion of biliary epithelial cells (cholangiocytes) requires host cell actin polymerization and localized membrane translocation/insertion of Na+/glucose cotransporter 1 (SGLT1) and of aquaporin 1 (Aqp1), a water channel, at the attachment site. The resultant localized water influx facilitates parasite cellular invasion by promoting host-cell membrane protrusion. However, the molecular mechanisms by which C. parvum induces membrane translocation/insertion of SGLT1/Aqp1 are obscure. We report here that cultured human cholangiocytes express several nonmuscle myosins, including myosins IIA and IIB. Moreover, C. parvum infection of cultured cholangiocytes results in the localized selective aggregation of myosin IIB but not myosin IIA at the region of parasite attachment, as assessed by dual-label immunofluorescence confocal microscopy. Concordantly, treatment of cells with the myosin light chain kinase inhibitor ML-7 or the myosin II-specific inhibitor blebbistatin or selective RNA-mediated repression of myosin IIB significantly inhibits (P < 0.05) C. parvum cellular invasion (by 60 to 80%). Furthermore ML-7 and blebbistatin significantly decrease (P < 0.02) C. parvum-induced accumulation of SGLT1 at infection sites (by approximately 80%). Thus, localized actomyosin-dependent membrane translocation of transporters/channels initiated by C. parvum is essential for membrane extension and parasite internalization, a phenomenon that may also be relevant to the mechanisms of cell membrane protrusion in general.



Author(s):  
A. E. Ritchie

The cause of bluecomb disease in turkeys is unknown. Filtration of infective intestinal contents suggests a viral origin. To date, it has not been possible to isolate the etiologic agent in various cell cultures. The purpose of this work was to characterize as many virus-like entities as were recognizable in intestines of both healthy and bluecomb-infected turkeys. By a comparison of the viral populations it was hoped that some insight might be gained into the cause of this disease. Studies of turkey hemorraghic enteritis by Gross and Moore (Avian Dis. 11: 296-307, 1967) have suggested that a bacteriophage-host cell interaction may bear some causal relationship to that disease.



Author(s):  
Frederick A. Murphy ◽  
Alyne K. Harrison ◽  
Sylvia G. Whitfield

The bullet-shaped viruses are currently classified together on the basis of similarities in virion morphology and physical properties. Biologically and ecologically the member viruses are extremely diverse. In searching for further bases for making comparisons of these agents, the nature of host cell infection, both in vivo and in cultured cells, has been explored by thin-section electron microscopy.





2009 ◽  
Vol 47 (05) ◽  
Author(s):  
Z Varga ◽  
Z Greff ◽  
J Pató ◽  
P Bánhegyi ◽  
L Őrfi ◽  
...  


2020 ◽  
Vol 5 (Special) ◽  

The coronavirus illness (COVID-19) is caused by a new recombinant SARS-CoV (SARS-CoV) virus (SARS-CoV-2). Target cell infection by SARS-CoV is mediated by the prickly protein of the coronavirus and host cell receptor, enzyme 2 converting angiotensin (ACE2) [3]. Similarly, a recent study suggests that cellular entry by SARS-CoV-2 is dependent on both ACE2 as well as type II transmembrane axial protease (TMPRSS2) [4]. This means that detection of ACE2 and PRSS2 expression in human tissues can predict potential infected cells and their respective effects in COVID-19 patients [1].



2007 ◽  
Vol 42 (2) ◽  
pp. 273-277
Author(s):  
J. Szarka ◽  
Eszter Szarka ◽  
G. Csilléry




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