994 Combination therapy for hepatitis C: positive selection pressure at baseline is associated with virologic response to therapy

Hepatology ◽  
2003 ◽  
Vol 38 ◽  
pp. 634-635
Author(s):  
V PARK ◽  
S MENON ◽  
B MASON ◽  
R LI ◽  
J KRUSHKAL ◽  
...  
PLoS ONE ◽  
2014 ◽  
Vol 9 (5) ◽  
pp. e97078 ◽  
Author(s):  
Akihito Tsubota ◽  
Kaoru Mogushi ◽  
Hideki Aizaki ◽  
Ken Miyaguchi ◽  
Keisuke Nagatsuma ◽  
...  

2019 ◽  
Vol 7 ◽  
pp. 232470961985812
Author(s):  
Clara Y. Tow ◽  
John F. Reinus

In this era of direct-acting antiviral (DAA) therapy for chronic hepatitis C virus (HCV) infection, treated patients have extremely high rates of sustained virologic response to short courses of therapy regardless of stage of fibrosis. Treatment failure is uncommon and often attributed to medication noncompliance or viral resistance to drug. This report describes 2 Child-Pugh-A cirrhotic patients who failed to clear HCV in response to therapy with DAAs. Each patient had Roux-en-Y gastric bypass (RYGB) surgery preceding DAA therapy. RYGB may create multiple barriers to adequate DAA absorption as a result of changes in gastrointestinal physiology. Treatment monitoring and duration should be carefully considered in this unique patient population.


2020 ◽  
Author(s):  
Franco D. Fernández ◽  
Luis R. Conci

AbstractPhytoplasmas are plant pathogenic bacteria transmitted by insects. As endosymbiotic bacteria that lack a cell wall, their membrane proteins are in direct contact with host cytoplasm. In phytoplasmas the immunodominant membrane proteins (IDPs), are the most abundant proteins of the cell membrane. The antigenic membrane protein (Amp), one of the three types of IDPs, is characterized by a positive selection pressure acting in their extracellular domain. In South America, the ‘Candidatus Phytoplasma meliae’ has been associated to chinaberry yellows disease. In the present work, we describe for the first time the structure, phylogeny and selection pressure of amp gene in sixteen ‘Candidatus Phytoplasma meliae’ isolates. Our results indicate that amp gene sequences preserve the structure, large extracellular domain flanked by to hydrophobic domains in the N- (signal peptide) and C-termini (transmembrane), previously described in its orthologues and high divergence in the amino acids residues from extracellular domain. Moreover, a positive selection pressure was detected predominantly in this region confirming previous reports.


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