3iya | pdb_00003iya

Association of the pr peptides with dengue virus blocks membrane fusion at acidic pH

Loading... Status: waiting for Mol* initialization Structural highlights 3iya is a 6 chain structure with sequence from Dengue virus 2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 22Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function E7FLK7_9FLAV Publication Abstract from PubMed Flavivirus assembles into an inert particle that requires proteolytic activation by furin to enable transmission to other hosts. We previously showed that immature virus undergoes a conformational change at low pH that renders it accessible to furin (I. M. Yu, W. Zhang, H. A. Holdaway, L. Li, V. A. Kostyuchenko, P. R. Chipman, R. J. Kuhn, M. G. Rossmann, and J. Chen, Science 319:1834-1837, 2008). Here we show, using cryoelectron microscopy, that the structure of immature dengue virus at pH 6.0 is essentially the same before and after the cleavage of prM. The structure shows that after cleavage, the proteolytic product pr remains associated with the virion at acidic pH, and that furin cleavage by itself does not induce any major conformational changes. We also show by liposome cofloatation experiments that pr retention prevents membrane insertion, suggesting that pr is present on the virion in the trans-Golgi network to protect the progeny virus from fusion within the host cell. Association of the pr peptides with dengue virus at acidic pH blocks membrane fusion.,Yu IM, Holdaway HA, Chipman PR, Kuhn RJ, Rossmann MG, Chen J J Virol. 2009 Dec;83(23):12101-7. Epub 2009 Sep 16. PMID:19759134 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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