scholarly journals Critical Role of MicroRNA-155 in Herpes Simplex Encephalitis

2014 ◽  
Vol 192 (6) ◽  
pp. 2734-2743 ◽  
Author(s):  
Siddheshvar Bhela ◽  
Sachin Mulik ◽  
Pradeep B. J. Reddy ◽  
Raphael L. Richardson ◽  
Fernanda Gimenez ◽  
...  
2015 ◽  
Vol 31 (3) ◽  
pp. 345-350 ◽  
Author(s):  
Murat Sutcu ◽  
Hacer Akturk ◽  
Ayper Somer ◽  
Burak Tatli ◽  
Selda Hancerli Torun ◽  
...  

2003 ◽  
Vol 140 (1-2) ◽  
pp. 13-27 ◽  
Author(s):  
Crystal S. Anglen ◽  
M.E. Truckenmiller ◽  
Todd D. Schell ◽  
Robert H. Bonneau

2016 ◽  
Vol 90 (23) ◽  
pp. 10535-10544 ◽  
Author(s):  
Doina Atanasiu ◽  
Wan Ting Saw ◽  
Roselyn J. Eisenberg ◽  
Gary H. Cohen

ABSTRACTReceptor-dependent herpes simplex virus (HSV)-induced cell-cell fusion requires glycoproteins gD, gH/gL, and gB. Our current model posits that during fusion, receptor-activated conformational changes in gD activate gH/gL, which subsequently triggers the transformation of the prefusion form of gB into a fusogenic state. To examine the role of each glycoprotein in receptor-dependent cell-cell fusion, we took advantage of our discovery that fusion by wild-type herpes simplex virus 2 (HSV-2) glycoproteins occurs twice as fast as that achieved by HSV-1 glycoproteins. By sequentially swapping each glycoprotein between the two serotypes, we established that fusion speed was governed by gH/gL, with gH being the main contributor. While the mutant forms of gB fuse at distinct rates that are dictated by their molecular structure, these restrictions can be overcome by gH/gL of HSV-2 (gH2/gL2), thereby enhancing their activity. We also found that deregulated forms of gD of HSV-1 (gD1) and gH2/gL2can alter the fusogenic potential of gB, promoting cell fusion in the absence of a cellular receptor, and that deregulated forms of gB can drive the fusion machinery to even higher levels. Low pH enhanced fusion by affecting the structure of both gB and gH/gL mutants. Together, our data highlight the complexity of the fusion machinery, the impact of the activation state of each glycoprotein on the fusion process, and the critical role of gH/gL in regulating HSV-induced fusion.IMPORTANCECell-cell fusion mediated by HSV glycoproteins requires gD, gH/gL, gB, and a gD receptor. Here, we show that fusion by wild-type HSV-2 glycoproteins occurs twice as fast as that achieved by HSV-1 glycoproteins. By sequentially swapping each glycoprotein between the two serotypes, we found that the fusion process was controlled by gH/gL. Restrictions imposed on the gB structure by mutations could be overcome by gH2/gL2, enhancing the activity of the mutants. Under low-pH conditions or when using deregulated forms of gD1and gH2/gL2, the fusogenic potential of gB could only be increased in the absence of receptor, underlining the exquisite regulation that occurs in the presence of receptor. Our data highlight the complexity of the fusion machinery, the impact of the activation state of each glycoprotein on the fusion process, and the critical role of gH/gL in regulating HSV-induced fusion.


1991 ◽  
Vol 4 (4) ◽  
pp. 211-224 ◽  
Author(s):  
B. Laurent ◽  
R. F. Allegri ◽  
C. Thomas-Anterion ◽  
N. Foyatier ◽  
B. Naegele-Faure ◽  
...  

Five patients with predominantly dominant cerebral hemisphere lesions due to herpes simplex encephalitis are described. Verbal amnesia was the main deficit but amnesic aphasia sometimes associated with impairment of remote memory also occurred. Semantic and episodic memory deficits were also explored in one case and the role of the right cerebral hemisphere in facilitating recovery of learning is discussed.


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