3ixx

From Proteopedia

(Difference between revisions)

Revision as of 14:35, 25 December 2014

The pseudo-atomic structure of West Nile immature virus in complex with Fab fragments of the anti-fusion loop antibody E53

Structural highlights

3ixx is a 10 chain structure with sequence from Mus musculus and West nile virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[Q9Q6P4_WNV] Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes (By similarity).[SAAS:SAAS011998_004_099774] [Q9WHD2_WNV] Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes (By similarity).[SAAS:SAAS026470_004_099774]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Flaviviruses are a group of human pathogens causing severe encephalitic or hemorrhagic diseases that include West Nile, dengue and yellow fever viruses. Here, using X-ray crystallography we have defined the structure of the flavivirus cross-reactive antibody E53 that engages the highly conserved fusion loop of the West Nile virus envelope glycoprotein. Using cryo-electron microscopy, we also determined that E53 Fab binds preferentially to spikes in noninfectious, immature flavivirions but is unable to bind significantly to mature virions, consistent with the limited solvent exposure of the epitope. We conclude that the neutralizing impact of E53 and likely similar fusion-loop-specific antibodies depends on its binding to the frequently observed immature component of flavivirus particles. Our results elucidate how fusion-loop antibodies, which comprise a significant fraction of the humoral response against flaviviruses, can function to control infection without appreciably recognizing mature virions. As these highly cross-reactive antibodies are often weakly neutralizing they also may contribute to antibody-dependent enhancement and flavi virus pathogenesis thereby complicating development of safe and effective vaccines.

Structural basis for the preferential recognition of immature flaviviruses by a fusion-loop antibody.,Cherrier MV, Kaufmann B, Nybakken GE, Lok SM, Warren JT, Chen BR, Nelson CA, Kostyuchenko VA, Holdaway HA, Chipman PR, Kuhn RJ, Diamond MS, Rossmann MG, Fremont DH EMBO J. 2009 Oct 21;28(20):3269-76. Epub 2009 Aug 27. PMID:19713934^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Cherrier MV, Kaufmann B, Nybakken GE, Lok SM, Warren JT, Chen BR, Nelson CA, Kostyuchenko VA, Holdaway HA, Chipman PR, Kuhn RJ, Diamond MS, Rossmann MG, Fremont DH. Structural basis for the preferential recognition of immature flaviviruses by a fusion-loop antibody. EMBO J. 2009 Oct 21;28(20):3269-76. Epub 2009 Aug 27. PMID:19713934 doi:10.1038/emboj.2009.245

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3ixx"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[3ixx]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/West_nile_virus West nile virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IXX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3IXX FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ixx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ixx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ixx RCSB], [http://www.ebi.ac.uk/pdbsum/3ixx PDBsum]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ixx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ixx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ixx RCSB], [http://www.ebi.ac.uk/pdbsum/3ixx PDBsum]</span></td></tr>
-<table>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/Q9Q6P4_WNV Q9Q6P4_WNV]] Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes (By similarity).[SAAS:SAAS011998_004_099774] [[http://www.uniprot.org/uniprot/Q9WHD2_WNV Q9WHD2_WNV]] Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes (By similarity).[SAAS:SAAS026470_004_099774]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 34: @@
 [[Category: Mus musculus]]
 [[Category: West nile virus]]
-[[Category: Cherrier, M V.]]
+[[Category: Cherrier, M V]]
-[[Category: Chipman, P R.]]
+[[Category: Chipman, P R]]
-[[Category: Diamond, M S.]]
+[[Category: Diamond, M S]]
-[[Category: Fremont, D H.]]
+[[Category: Fremont, D H]]
-[[Category: Holdaway, H A.]]
+[[Category: Holdaway, H A]]
-[[Category: Kaufmann, B.]]
+[[Category: Kaufmann, B]]
-[[Category: Kostyuchenko, V A.]]
+[[Category: Kostyuchenko, V A]]
-[[Category: Kuhn, R J.]]
+[[Category: Kuhn, R J]]
-[[Category: Lok, S M.]]
+[[Category: Lok, S M]]
-[[Category: Nelson, C A.]]
+[[Category: Nelson, C A]]
-[[Category: Nybakken, G E.]]
+[[Category: Nybakken, G E]]
-[[Category: Rossmann, M G.]]
+[[Category: Rossmann, M G]]
-[[Category: Warren, J T.]]
+[[Category: Warren, J T]]
 [[Category: Atp-binding]]
 [[Category: E53]]
@@ Line 60: / Line 62: @@
 [[Category: Virion]]
 [[Category: Virus]]
-[[Category: West nile virus]]
 [[Category: Wnv]]

3ixx

From Proteopedia

Revision as of 14:35, 25 December 2014

The pseudo-atomic structure of West Nile immature virus in complex with Fab fragments of the anti-fusion loop antibody E53

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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