GP1 of Lassa Virus: Difference between revisions
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The primary cellular receptor of LASV is α-dystroglycan (α-DG)<ref name="PMID: 9851928">PMID: 9851928</ref><ref name="PMID: 15857984">PMID: 15857984</ref>, which is recognized by a trimeric class 1 viral GPC (spike complex) on the viral surface<ref name="PMID: 16731928">PMID: 16731928</ref><ref name="PMID: 26849049">PMID: 26849049</ref>. Following successful attachment to α-DG on cells, LASV is internalized via [http://en.wikipedia.org/wiki/Pinocytosis macropinocytosis]<ref name="PMID: 27147735">PMID: 27147735</ref>, and the GPC facilitates membrane fusion at the acidic environment of a late endosomal compartment<ref name="PMID: 16731928"><ref name="PMID: 21931550">PMID: 21931550 </ref>. Recent studies have shown that successful infection by LASV requires it to switch in a pH-dependent manner from α-DG to LAMP1<ref name="PMID: 27605678" /><ref name="PMID:24970085">PMID:24970085</ref>. Binding of the <scene name='76/761695/Lamp1bindingsite/14'>LAMP1</scene> endosomal compartment triggers the spikes. | The primary cellular receptor of LASV is α-dystroglycan (α-DG)<ref name="PMID: 9851928">PMID: 9851928</ref><ref name="PMID: 15857984">PMID: 15857984</ref>, which is recognized by a trimeric class 1 viral GPC (spike complex) on the viral surface<ref name="PMID: 16731928">PMID: 16731928</ref><ref name="PMID: 26849049">PMID: 26849049</ref>. Following successful attachment to α-DG on cells, LASV is internalized via [http://en.wikipedia.org/wiki/Pinocytosis macropinocytosis]<ref name="PMID: 27147735">PMID: 27147735</ref>, and the GPC facilitates membrane fusion at the acidic environment of a late endosomal compartment<ref name="PMID: 16731928"><ref name="PMID: 21931550">PMID: 21931550 </ref>. Recent studies have shown that successful infection by LASV requires it to switch in a pH-dependent manner from α-DG to LAMP1<ref name="PMID: 27605678" /><ref name="PMID:24970085">PMID:24970085</ref>. Binding of the <scene name='76/761695/Lamp1bindingsite/14'>LAMP1</scene> endosomal compartment triggers the spikes. | ||
=== Histidine Triad=== | === Histidine Triad=== | ||
Included in this structure is a unique <scene name='76/761695/Histriad/ | Included in this structure is a unique <scene name='76/761695/Histriad/9'>triad of histidines</scene> that is highly conserved among OW arenaviruses. Located on the β-sheet face of GP1, the histidine triad is a structural element that directly interacts with LAMP1 and helps stabilize a LAMP1-"compatible" conformation by providing a molecular mechanism for the pH-dependent receptor switching<ref name="PMID: 25972533" />. The <scene name='76/761695/Lamp1bindingsite/5'>histidine triad</scene> is critical in forming a <scene name='76/761695/Lamp1bindingsite/9'>binding site</scene> for LAMP1<ref name="PMID: 28448640">PMID: 28448640 </ref><ref name="PMID: 27605678">PMID: 27605678 </ref>. | ||
==Resources== | ==Resources== | ||
For more information on this protein structure visit the following sites: [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4zjf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zjf OCA], [http://pdbe.org/4zjf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zjf RCSB], [http://www.ebi.ac.uk/pdbsum/4zjf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zjf ProSAT] | For more information on this protein structure visit the following sites: [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4zjf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zjf OCA], [http://pdbe.org/4zjf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zjf RCSB], [http://www.ebi.ac.uk/pdbsum/4zjf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zjf ProSAT] | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category: Cohen, N]] | [[Category: Cohen, N]] | ||