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GP1 of Lassa Virus
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GP1 of LASV is a 4 chain structure with <scene name='76/761695/Nag/1'>NAG</scene> ligands attached to each chain. The overall architecture of GP1 features a central β-sheet and two distinct halves: a glycosylated half containing the receptor-binding site that is made mostly by the central β-sheet and surrounding loops and a half that contains mostly helices and most likely faces the trimer axis<ref name="MolMechforLAMP1">DOI 10.1128/JVI.00651-15</ref>. The method used to determine this structure was [https://en.wikipedia.org/wiki/X-ray_crystallography X-ray diffraction] | GP1 of LASV is a 4 chain structure with <scene name='76/761695/Nag/1'>NAG</scene> ligands attached to each chain. The overall architecture of GP1 features a central β-sheet and two distinct halves: a glycosylated half containing the receptor-binding site that is made mostly by the central β-sheet and surrounding loops and a half that contains mostly helices and most likely faces the trimer axis<ref name="MolMechforLAMP1">DOI 10.1128/JVI.00651-15</ref>. The method used to determine this structure was [https://en.wikipedia.org/wiki/X-ray_crystallography X-ray diffraction] | ||
=== Histidine Triad=== | === Histidine Triad=== | ||
| - | Attached to this structure is a unique <scene name='76/761695/Histriad/ | + | Attached to this structure is a unique <scene name='76/761695/Histriad/6'>triad of histidines</scene> that is highly conserved among Old World arenaviruses. Located on the β-sheet face of GP1, the histidine triad is a structural element that directly interacts with [[LAMP1]] (Lysosome-associated membrane glycoprotein) and helps stabilize a LAMP1-"compatible" conformation by providing a molecular mechanism for the pH-dependent receptor switching<ref name="MolMechforLAMP1" />. The histidine triad is critical in forming a <scene name='76/761695/Lamp1bindingsite/3'>binding site</scene> for LAMP1. |
===LAMP1 Binding Site=== | ===LAMP1 Binding Site=== | ||
The primary cellular receptor of LASV α-dystroglycan (α-DG), which is recognized by a trimeric class 1 viral GPC on the surface of the virus. Following successful attachment to α-DG on cells, LASV is internalized via [https://en.wikipedia.org/wiki/Pinocytosis macropinocytosis], and the GPC facilitates membrane fusion at the acidic environment of a late endosomal compartment. Recent studies have shown that successful infection by LASV requires it to switch in a pH-dependent manner from α-DG to LAMP1. | The primary cellular receptor of LASV α-dystroglycan (α-DG), which is recognized by a trimeric class 1 viral GPC on the surface of the virus. Following successful attachment to α-DG on cells, LASV is internalized via [https://en.wikipedia.org/wiki/Pinocytosis macropinocytosis], and the GPC facilitates membrane fusion at the acidic environment of a late endosomal compartment. Recent studies have shown that successful infection by LASV requires it to switch in a pH-dependent manner from α-DG to LAMP1. | ||
Revision as of 10:10, 29 June 2017
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References
- ↑ 1.0 1.1 Cohen-Dvashi H, Cohen N, Israeli H, Diskin R. Molecular mechanism for LAMP1 recognition by Lassa Virus. J Virol. 2015 May 13. pii: JVI.00651-15. PMID:25972533 doi:http://dx.doi.org/10.1128/JVI.00651-15
Categories: Cohen, N | Cohen-Dvashi, H | Diskin, R | Israeli, H | Arenavirus | Glycoprotein | Lassa | LASV | Receptor binding | Viral protein | 4zjf | GP1
