TY - JOUR
T1 - Degrees of maturity
T2 - The complex structure and biology of flaviviruses
AU - Pierson, Theodore C.
AU - Diamond, Michael S.
N1 - Funding Information:
This work was supported by the Intramural Research Program of the NIH , National Institutes of Allergy and Infectious Diseases (NIAID) , R01-AI077955 and U01-AI061373 . The authors thank Mr. Ethan Tyler and Phong Lee for preparation of the figures. We are grateful to Drs. Kimberly Dowd and Swati Mukherjee for their thoughtful comments on our manuscript. We thank members of our laboratory for useful discussions.
PY - 2012/4
Y1 - 2012/4
N2 - Flaviviruses are small enveloped virions that enter target cells in a pH-dependent fashion. Virus attachment, entry, and membrane fusion are orchestrated by the envelope (E) and pre-membrane (prM) proteins, the two structural proteins displayed on the surface of virions. Flaviviruses assemble as an immature non-infectious form onto which prM and E form trimeric spikes. During egress from infected cells, flaviviruses undergo dramatic structural changes characterized by the formation of a herringbone arrangement of E proteins that lie flat against the surface of the virion and cleavage of the prM protein by the cellular protease furin. The result is a relatively smooth, infectious mature virion. This dynamic process is now understood in structural detail at the atomic level. However, recent studies indicate that many of the virions released from cells share structural features of both immature and mature virus particles. These mosaic partially mature virions are infectious and interact uniquely with target cells and the host immune response. Here, we will discuss recent advances in our understanding of the biology and significance of partially mature flaviviruses.
AB - Flaviviruses are small enveloped virions that enter target cells in a pH-dependent fashion. Virus attachment, entry, and membrane fusion are orchestrated by the envelope (E) and pre-membrane (prM) proteins, the two structural proteins displayed on the surface of virions. Flaviviruses assemble as an immature non-infectious form onto which prM and E form trimeric spikes. During egress from infected cells, flaviviruses undergo dramatic structural changes characterized by the formation of a herringbone arrangement of E proteins that lie flat against the surface of the virion and cleavage of the prM protein by the cellular protease furin. The result is a relatively smooth, infectious mature virion. This dynamic process is now understood in structural detail at the atomic level. However, recent studies indicate that many of the virions released from cells share structural features of both immature and mature virus particles. These mosaic partially mature virions are infectious and interact uniquely with target cells and the host immune response. Here, we will discuss recent advances in our understanding of the biology and significance of partially mature flaviviruses.
UR - http://www.scopus.com/inward/record.url?scp=84859500348&partnerID=8YFLogxK
U2 - 10.1016/j.coviro.2012.02.011
DO - 10.1016/j.coviro.2012.02.011
M3 - Review article
C2 - 22445964
AN - SCOPUS:84859500348
SN - 1879-6257
VL - 2
SP - 168
EP - 175
JO - Current Opinion in Virology
JF - Current Opinion in Virology
IS - 2
ER -