NADPH Oxidase Activity and Cytochromeb558Content of Human Epstein-Barr-Virus-Transformed B Lymphocytes Correlate with Expression of Genes Encoding Components of the Oxidase System

1998 ◽  
Vol 360 (2) ◽  
pp. 158-164 ◽  
Author(s):  
Antonio Condino-Neto ◽  
Peter E. Newburger
2001 ◽  
Vol 268 (19) ◽  
pp. 5197-5208 ◽  
Author(s):  
Marie-Hélène Paclet ◽  
Anthony W. Coleman ◽  
James Burritt ◽  
Françoise Morel

1995 ◽  
Vol 306 (1) ◽  
pp. 141-145 ◽  
Author(s):  
M Chetty ◽  
A J Thrasher ◽  
A Abo ◽  
C M Casimir

The NADPH oxidase of phagocytes is known to be expressed in Epstein-Barr-virus-transformed B-lymphocytes, albeit at levels only approx. 5% of those found in neutrophils. We have investigated the basis of this low level of expression and find that all four specific components of the NADPH oxidase are expressed in B-lymphocytes, but only p47-phox protein attains levels equivalent with those found in neutrophils. This component was shown to phosphorylate and translocate to the membrane normally on activation. The other cytosolic component, p67-phox, did show a deficit, and by supplementing a B-cell cytosol extract with recombinant p67-phox, this was shown to account for the somewhat reduced activity of B-cell cytosol in a cell-free oxidase system. The cell-free analysis also clearly located the major deficiency in superoxide-generating capacity of B-lymphocytes to the membrane. Western blotting of membrane proteins revealed major reductions in the amount of cytochrome b558. Analysis of the levels of mRNA for both subunits of cytochrome b558, however, showed levels greater than expected. Significantly more mRNA for gp91-phox was present in B-cells than in undifferentiated HL60 cells, although it was not quite as abundant as in differentiated HL60 cells, which are capable of producing large amounts of superoxide. We conclude that the failure of B-lymphocytes to generate amounts of superoxide equivalent to those generated by neutrophils is primarily due to a post-transcriptionally determined block to the accumulation of cytochrome b558.


2014 ◽  
Vol 10 (8) ◽  
pp. e1004307 ◽  
Author(s):  
Ayman El-Guindy ◽  
Francesc Lopez-Giraldez ◽  
Henri-Jacques Delecluse ◽  
Jessica McKenzie ◽  
George Miller

Vaccines ◽  
2021 ◽  
Vol 9 (3) ◽  
pp. 285
Author(s):  
Xinle Cui ◽  
Zhouhong Cao ◽  
Yuriko Ishikawa ◽  
Sara Cui ◽  
Ken-Ichi Imadome ◽  
...  

Epstein–Barr virus (EBV) is the primary cause of infectious mononucleosis and is strongly implicated in the etiology of multiple lymphoid and epithelial cancers. EBV core fusion machinery envelope proteins gH/gL and gB coordinately mediate EBV fusion and entry into its target cells, B lymphocytes and epithelial cells, suggesting these proteins could induce antibodies that prevent EBV infection. We previously reported that the immunization of rabbits with recombinant EBV gH/gL or trimeric gB each induced markedly higher serum EBV-neutralizing titers for B lymphocytes than that of the leading EBV vaccine candidate gp350. In this study, we demonstrated that immunization of rabbits with EBV core fusion machinery proteins induced high titer EBV neutralizing antibodies for both B lymphocytes and epithelial cells, and EBV gH/gL in combination with EBV trimeric gB elicited strong synergistic EBV neutralizing activities. Furthermore, the immune sera from rabbits immunized with EBV gH/gL or trimeric gB demonstrated strong passive immune protection of humanized mice from lethal dose EBV challenge, partially or completely prevented death respectively, and markedly decreased the EBV load in peripheral blood of humanized mice. These data strongly suggest the combination of EBV core fusion machinery envelope proteins gH/gL and trimeric gB is a promising EBV prophylactic vaccine.


1994 ◽  
Vol 269 (29) ◽  
pp. 18743-18746 ◽  
Author(s):  
F.E. Maly ◽  
L.A. Quilliam ◽  
O. Dorseuil ◽  
C.J. Der ◽  
G.M. Bokoch

2014 ◽  
Vol 58 (2-3) ◽  
pp. 268-276 ◽  
Author(s):  
Olivia L. Hatton ◽  
Aleishia Harris-Arnold ◽  
Steven Schaffert ◽  
Sheri M. Krams ◽  
Olivia M. Martinez

Author(s):  
David Liebowitz ◽  
Elliott Kieff ◽  
Jeffery Sample ◽  
Mark Birkenbach ◽  
Fred Wang

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