This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


GP1 of Lassa Virus

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 5: Line 5:
'''GP1''' (Glycoprotein 1) is the receptor binding domain of LASV that mediates receptor recognition. Research thus far indicates that GP1 from LASV may undergo irreversible conformational changes that could serve as an immunological decoy mechanism.
'''GP1''' (Glycoprotein 1) is the receptor binding domain of LASV that mediates receptor recognition. Research thus far indicates that GP1 from LASV may undergo irreversible conformational changes that could serve as an immunological decoy mechanism.
==Structural Highlights==
==Structural Highlights==
-
GP1 of LASV is a 4 chain structure with <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>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
+
GP1 of LASV is a 4 chain structure with <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>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]
-
[https://en.wikipedia.org/wiki/X-ray_crystallography X-ray diffraction]
+
=== Histidine Triad===
=== Histidine Triad===
-
Attached to this structure is a <scene name='76/761695/Histriad/5'>unique 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" />.
+
Attached to this structure is a <scene name='76/761695/Histriad/5'>unique 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 binding site for LAMP1 (insert scene).
===LAMP1 Binding Site===
===LAMP1 Binding Site===
-
To effectively infect cells, LASV needs to switch in an endosomal compartment from its primary receptor, [[α-dystroglycan]] (α-DG), to LAMP1<ref name="RoleofLAMP1BindingandpHsensing">DOI 10.1128/JVI.01624-16</ref>. Recent studies show that receptor switching is critical during cell entry of LASV. The binding of LAMP1 triggers the glycoprotein spike complex of LASV to catalyze [https://en.wikipedia.org/wiki/Lipid_bilayer_fusion membrane fusion] by potentiating its response to pH.
+
To effectively infect cells, LASV needs to switch from its primary receptor, [[α-dystroglycan]] (α-DG), to LAMP1<ref name="RoleofLAMP1BindingandpHsensing">DOI 10.1128/JVI.01624-16</ref>.
 +
 
 +
The binding of LAMP1 triggers the glycoprotein spike complex of LASV to catalyze [https://en.wikipedia.org/wiki/Lipid_bilayer_fusion membrane fusion] by potentiating its response to pH.....so....
Protein structure accession number: '''4ZJF'''
Protein structure accession number: '''4ZJF'''

Revision as of 08:21, 27 June 2017

4ZJF structure

Drag the structure with the mouse to rotate

References

  1. ↑ 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
  2. ↑ Cohen-Dvashi H, Israeli H, Shani O, Katz A, Diskin R. Role of LAMP1 Binding and pH Sensing by the Spike Complex of Lassa Virus. J Virol. 2016 Oct 28;90(22):10329-10338. Print 2016 Nov 15. PMID:27605678 doi:http://dx.doi.org/10.1128/JVI.01624-16

Proteopedia Page Contributors and Editors (what is this?)

Rebecca Holstein, Michal Harel

Retrieved from "http://52.214.119.220/wiki/index.php/GP1_of_Lassa_Virus"
Personal tools