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@article{1376815, author = {Battisti, Anthony J. and Meng, Geng and Winkler, Dennis C. and McGinnes, Lori W. and Plevka, Pavel and Steven, Alasdair C. and Morrison, Trudy G. and Rossmann, Michael G.}, article_location = {WASHINGTON}, article_number = {35}, doi = {http://dx.doi.org/10.1073/pnas.1210275109}, keywords = {NEWCASTLE-DISEASE VIRUS; RESPIRATORY SYNCYTIAL VIRUS; CRYSTAL-STRUCTURE; SENDAI-VIRUS; PARTICLES; REVEALS; NUCLEOCAPSIDS; GLYCOPROTEINS; ECTODOMAIN; EVOLUTION}, language = {eng}, issn = {0027-8424}, journal = {Proceedings of the National Academy of Sciences of the United States of America}, title = {Structure and assembly of a paramyxovirus matrix protein}, volume = {109}, year = {2012} }
TY - JOUR ID - 1376815 AU - Battisti, Anthony J. - Meng, Geng - Winkler, Dennis C. - McGinnes, Lori W. - Plevka, Pavel - Steven, Alasdair C. - Morrison, Trudy G. - Rossmann, Michael G. PY - 2012 TI - Structure and assembly of a paramyxovirus matrix protein JF - Proceedings of the National Academy of Sciences of the United States of America VL - 109 IS - 35 SP - 13996-14000 EP - 13996-14000 PB - National Academy of Sciences SN - 00278424 KW - NEWCASTLE-DISEASE VIRUS KW - RESPIRATORY SYNCYTIAL VIRUS KW - CRYSTAL-STRUCTURE KW - SENDAI-VIRUS KW - PARTICLES KW - REVEALS KW - NUCLEOCAPSIDS KW - GLYCOPROTEINS KW - ECTODOMAIN KW - EVOLUTION N2 - Many pleomorphic, lipid-enveloped viruses encode matrix proteins that direct their assembly and budding, but the mechanism of this process is unclear. We have combined X-ray crystallography and cryoelectron tomography to show that the matrix protein of Newcastle disease virus, a paramyxovirus and relative of measles virus, forms dimers that assemble into pseudotetrameric arrays that generate the membrane curvature necessary for virus budding. We show that the glycoproteins are anchored in the gaps between the matrix proteins and that the helical nucleocapsids are associated in register with the matrix arrays. About 90% of virions lack matrix arrays, suggesting that, in agreement with previous biological observations, the matrix protein needs to dissociate from the viral membrane during maturation, as is required for fusion and release of the nucleocapsid into the host's cytoplasm. Structure and sequence conservation imply that other paramyxovirus matrix proteins function similarly. ER -
BATTISTI, Anthony J., Geng MENG, Dennis C. WINKLER, Lori W. MCGINNES, Pavel PLEVKA, Alasdair C. STEVEN, Trudy G. MORRISON and Michael G. ROSSMANN. Structure and assembly of a paramyxovirus matrix protein. \textit{Proceedings of the National Academy of Sciences of the United States of America}. WASHINGTON: National Academy of Sciences, 2012, vol.~109, No~35, p.~13996-14000. ISSN~0027-8424. Available from: https://dx.doi.org/10.1073/pnas.1210275109.
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