Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành y học dành cho các bạn tham khảo đề tài: Reversible conformational change in herpes simplex virus glycoprotein B with fusion-fromwithout activity is triggered by mildly acidic pH | Siekavizza-Robles et al. Virology Journal 2010 7 352 http content 7 1 352 VIROLOGY JOURNAL RESEARCH Open Access Reversible conformational change in herpes simplex virus glycoprotein B with fusion-from-without activity is triggered by mildly acidic pH Carlos R Siekavizza-Robles Stephen J Dollery Anthony V Nicola Abstract Background The pre-fusion form of the herpes simplex virus HSV fusion protein gB undergoes pH-triggered conformational change in vitro and during viral entry Dollery et al. J. Virol. 84 3759-3766 2010 . The antigenic structure of gB from the fusion-from-without FFWO strain of HSV-1 ANG path resembles wild type gB that has undergone pH-triggered changes. Together changes in the antigenic and oligomeric conformation of gB correlate with fusion activity. We tested whether the pre-fusion form of FFWO gB undergoes altered conformational change in response to low pH. Results A pH of - altered the conformation of Domains I and V of FFWO gB which together comprise the functional region containing the hydrophobic fusion loops. The ANG path gB oligomer was altered at a similar pH. All changes were reversible. In wild type HSV lacking the UL45 protein which has been implicated in gB-mediated fusion gB still underwent pH-triggered changes. ANG path entry was inactivated by pretreatment of virions with low pH. Conclusion The pre-fusion conformation of gB with enhanced fusion activity undergoes alteration in antigenic structure and oligomeric conformation in response to acidic pH. We propose that endosomal pH triggers conformational change in mutant gB with FFWO activity in a manner similar to wild type. Differences apart from this trigger may account for the increased fusion activity of FFWO gB. Introduction Membrane fusion during enveloped virus entry is mediated by conformational change in viral fusion proteins. Herpesviruses are a paradigm for viral entry mediated by a multi-component fusion machinery. Herpesviral fusion and entry is
