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GP1 of Lassa Virus

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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="PMID: 25972533" />. The <scene name='76/761695/Lamp1bindingsite/4'>histidine triad</scene> is critical in forming a <scene name='76/761695/Lamp1bindingsite/3'>binding site</scene> for LAMP1.
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="PMID: 25972533" />. The <scene name='76/761695/Lamp1bindingsite/4'>histidine triad</scene> is critical in forming a <scene name='76/761695/Lamp1bindingsite/3'>binding site</scene> for LAMP1.
===LAMP1 Binding Site===
===LAMP1 Binding Site===
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The primary cellular receptor of LASV 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 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.
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The primary cellular receptor of LASV 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 [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.
<scene name='76/761695/4zjf_chaina_hisandlampsite/1'>LAMP1 Binding sites with Histidine Triad</scene>
<scene name='76/761695/4zjf_chaina_hisandlampsite/1'>LAMP1 Binding sites with Histidine Triad</scene>
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Revision as of 08:43, 5 July 2017

4ZJF structure

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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. ↑ Cao W, Henry MD, Borrow P, Yamada H, Elder JH, Ravkov EV, Nichol ST, Compans RW, Campbell KP, Oldstone MB. Identification of alpha-dystroglycan as a receptor for lymphocytic choriomeningitis virus and Lassa fever virus. Science. 1998 Dec 11;282(5396):2079-81. PMID:9851928
  3. ↑ Kunz S, Rojek JM, Perez M, Spiropoulou CF, Oldstone MB. Characterization of the interaction of lassa fever virus with its cellular receptor alpha-dystroglycan. J Virol. 2005 May;79(10):5979-87. PMID:15857984 doi:http://dx.doi.org/10.1128/JVI.79.10.5979-5987.2005
  4. ↑ Eschli B, Quirin K, Wepf A, Weber J, Zinkernagel R, Hengartner H. Identification of an N-terminal trimeric coiled-coil core within arenavirus glycoprotein 2 permits assignment to class I viral fusion proteins. J Virol. 2006 Jun;80(12):5897-907. PMID:16731928 doi:http://dx.doi.org/10.1128/JVI.00008-06
  5. ↑ Li S, Sun Z, Pryce R, Parsy ML, Fehling SK, Schlie K, Siebert CA, Garten W, Bowden TA, Strecker T, Huiskonen JT. Acidic pH-Induced Conformations and LAMP1 Binding of the Lassa Virus Glycoprotein Spike. PLoS Pathog. 2016 Feb 5;12(2):e1005418. doi: 10.1371/journal.ppat.1005418., eCollection 2016 Feb. PMID:26849049 doi:http://dx.doi.org/10.1371/journal.ppat.1005418

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