Triatoma Virus Recombinant VP4 Protein Induces Membrane Permeability through Dynamic Pores
نویسندگان
چکیده
منابع مشابه
Triatoma virus recombinant VP 4 protein induces membrane 2 permeability through dynamic pores 3 4 5
4 5 Rubén Sánchez-Eugenia, Julen Goikolea, David Gil-Cartón, Lissete 6 Sánchez-Magraner, Diego M. A. Guérin 7 8 9 1 Unidad de Biofísica (CSIC, UPV/EHU), Bo Sarriena S/N, 48940 Leioa, 10 Bizkaia, Spain. 11 2 CIC bioGUNE, Structural Biology Unit, Parque Tecnológico Zamudio, 12 48160 Derio, Bizkaia, Spain. 13 3 Departamento de Bioquímica y Biología Molecular, Facultad de Ciencia y 14 Tecnología, U...
متن کاملRecombinant VP4 of human rhinovirus induces permeability in model membranes.
In common with all nonenveloped viruses, the mechanism of picornavirus membrane penetration during cell entry is poorly understood. The small, myristylated capsid protein VP4 has been implicated in this process. Here we show that recombinant VP4 of human rhinovirus 16 has the ability to associate with and induce membrane permeability in otherwise intact liposomes. This provides further evidence...
متن کاملCapsid Protein VP4 of Human Rhinovirus Induces Membrane Permeability by the Formation of a Size-Selective Multimeric Pore
Non-enveloped viruses must deliver their viral genome across a cell membrane without the advantage of membrane fusion. The mechanisms used to achieve this remain poorly understood. Human rhinovirus, a frequent cause of the common cold, is a non-enveloped virus of the picornavirus family, which includes other significant pathogens such as poliovirus and foot-and-mouth disease virus. During picor...
متن کاملCapping and methylation of mRNA by purified recombinant VP4 protein of bluetongue virus.
The core of bluetongue virus (BTV) is a multienzyme complex composed of two major proteins (VP7 and VP3) and three minor proteins (VP1, VP4, and VP6) in addition to the viral genome. The core is transcriptionally active and produces capped mRNA from which all BTV proteins are translated, but the relative role of each core component in the overall reaction process remains unclear. Previously we ...
متن کاملSV40 late protein VP4 forms toroidal pores to disrupt membranes for viral release.
Nonenveloped viruses are generally released from the cell by the timely lysis of host cell membranes. SV40 has been used as a model virus for the study of the lytic nonenveloped virus life cycle. The expression of SV40 VP4 at later times during infection is concomitant with cell lysis. To investigate the role of VP4 in viral release and its mechanism of action, VP4 was expressed and purified fr...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Virology
سال: 2015
ISSN: 0022-538X,1098-5514
DOI: 10.1128/jvi.00011-15