LoГЇc maurin full#

В© 2014 by the American Association for the Study of Liver Diseases. Find the latest news, pictures, and opinions about LoГЇc Maurin. Our study highlights the role of E1 as a modulator of HCV binding to receptors and membrane fusion, underlining its potential as an antiviral target. These results reveal a multifunctional and crucial interaction between E1 and E2 for HCV entry into cells. Finally, we demonstrated that this crosstalk is involved in membrane fusion.

These results highlight the critical role of E1 in the modulation of HCV binding to receptors. In addition, we found for the first time that E1E2 complexes can interact with the first extracellular loop of Claudin-1, whereas soluble E2 did not. Interestingly, we found that this crosstalk modulates E1E2 binding to HCV entry receptors SR-BI and CD81.

LoГЇc maurin full#

Its modulation leads to either a full restoration of the functionality of the suboptimal heterodimer or a destabilization of the functional heterodimer. By mutagenesis analysis, we identified a particular crosstalk between three amino acids of E1 and the domain III of E2. Using HCV pseudoparticle assays, we confirmed the opposing entry phenotypes of these heterodimers. Join Facebook to connect with Loc Maurin La Puenta and others you may know. Loc Maurin Pontificia Universidad Catlica de Chile). We found an E1E2 combination that drastically impaired the infectivity of cell culture-derived HCV particles, whereas the reciprocal E1E2 combination led to increased infectivity. View the profiles of people named Loc Maurin La Puenta. Looking for the first light of the Universe from the Atcama desert (Dr. For this purpose we generated chimeric E1E2 heterodimers derived from two HCV 1a strains to identify and characterize crosstalk between their domains. Simone Aiola, Erminia Calabrese, Loc Maurin, Sigurd Naess, Benjamin L Schmitt, Maximilian H Abitbol, Graeme E Addison, Peter AR Ade, David Alonso. Here we sought to investigate how certain domains of E1 and E2 have coevolved to optimize their interactions to promote efficient HCV entry. However, knowledge about their structure, intra- or intermolecular dialogs, and conformational changes is scarce, limiting the design of therapeutic strategies targeting E1E2. Hepatitis C virus (HCV) envelope glycoproteins E1 and E2 are important mediators for productive cell entry.