Structure of the Immature Dengue Virus at Low pH Primes Proteolytic Maturation Export

@article{citeulike:2604723, abstract = {Intracellular cleavage of immature flaviviruses is a critical step in assembly that generates the membrane fusion potential of the E glycoprotein. With cryoelectron microscopy we show that the immature dengue particles undergo a reversible conformational change at low pH that renders them accessible to furin cleavage. At a pH of 6.0, the E proteins are arranged in a herringbone pattern with the pr peptides docked onto the fusion loops, a configuration similar to that of the mature virion. After cleavage, the dissociation of pr is pH-dependent, suggesting that in the acidic environment of the trans-Golgi network pr is retained on the virion to prevent membrane fusion. These results suggest a mechanism by which flaviviruses are processed and stabilized in the host cell secretory pathway. 10.1126/science.1153264}, author = {Yu, I-Mei and Zhang, Wei and Holdaway, Heather A. and Li, Long and Kostyuchenko, Victor A. and Chipman, Paul R. and Kuhn, Richard J. and Rossmann, Michael G. and Chen, Jue}, citeulike-article-id = {2604723}, citeulike-linkout-0 = {http://dx.doi.org/10.1126/science.1153264}, citeulike-linkout-1 = {http://www.sciencemag.org/cgi/content/abstract/319/5871/1834}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/18369148}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=18369148}, day = {28}, doi = {10.1126/science.1153264}, journal = {Science}, keywords = {dengue, proteolytic, structure}, month = {March}, number = {5871}, pages = {1834--1837}, posted-at = {2009-06-16 03:05:22}, priority = {2}, title = {Structure of the Immature Dengue Virus at Low pH Primes Proteolytic Maturation}, url = {http://dx.doi.org/10.1126/science.1153264}, volume = {319}, year = {2008} }

TY - JOUR ID - citeulike:2604723 L3 - citeulike-article-id:2604723 N2 - Intracellular cleavage of immature flaviviruses is a critical step in assembly that generates the membrane fusion potential of the E glycoprotein. With cryoelectron microscopy we show that the immature dengue particles undergo a reversible conformational change at low pH that renders them accessible to furin cleavage. At a pH of 6.0, the E proteins are arranged in a herringbone pattern with the pr peptides docked onto the fusion loops, a configuration similar to that of the mature virion. After cleavage, the dissociation of pr is pH-dependent, suggesting that in the acidic environment of the trans-Golgi network pr is retained on the virion to prevent membrane fusion. These results suggest a mechanism by which flaviviruses are processed and stabilized in the host cell secretory pathway. 10.1126/science.1153264 IS - 5871 JF - Science EP - 1837 TI - Structure of the Immature Dengue Virus at Low pH Primes Proteolytic Maturation VL - 319 SP - 1834 KW - dengue KW - proteolytic KW - structure AU - Yu, I-Mei AU - Zhang, Wei AU - Holdaway, Heather AU - Li, Long AU - Kostyuchenko, Victor AU - Chipman, Paul AU - Kuhn, Richard AU - Rossmann, Michael AU - Chen, Jue PY - 2008/03/28/ UR - http://dx.doi.org/10.1126/science.1153264 ER -