4wat

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of PfRh5, an essential P. falciparum ligand for invasion of human erythrocytes

Structural highlights

4wat is a 1 chain structure with sequence from Plasmodium falciparum 3D7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.18Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RH5_PLAF7 Essential for the invasion of host erythrocytes by blood stage merozoites (PubMed:18827878, PubMed:19000690, PubMed:22080952, PubMed:25296023, PubMed:25583518, PubMed:27374406, PubMed:28186186, PubMed:28409866, PubMed:31204103). By binding P113 at the surface of the merozoite and human BSG/basigin on the erythrocyte membrane, leads to the establishment of a tight junction between the merozoite and host erythrocyte membranes (PubMed:22080952, PubMed:25296023, PubMed:25583518, PubMed:27374406, PubMed:28186186). In addition, the interaction with BSG results in BSG dimerization which triggers an increase in intracellular Ca(2+) in the erythrocyte (PubMed:27374406, PubMed:28409866). This essential step leads to a rearrangement of the erythrocyte cytoskeleton required for the merozoite invasion (PubMed:28409866).^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8] ^[9]

Publication Abstract from PubMed

Plasmodium falciparum causes the most severe form of malaria in humans and is responsible for over 700,000 deaths annually. It is an obligate intracellular parasite and invades erythrocytes where it grows in a relatively protected niche. Invasion of erythrocytes is essential for parasite survival and this involves interplay of multiple protein-protein interactions. One of the most important interactions is binding of parasite invasion ligand families EBLs and PfRhs to host receptors on the surface of erythrocytes. PfRh5 is the only essential invasion ligand within the PfRh family and is an important vaccine candidate. PfRh5 binds the host receptor basigin. In this study, we have determined the crystal structure of PfRh5 using diffraction data to 2.18 A resolution. PfRh5 exhibits a novel fold, comprising nine mostly anti-parallel alpha-helices encasing an N-terminal beta-hairpin, with the overall shape being an elliptical disk. This is the first three-dimensional structure determined for the PfRh family of proteins. DOI: http://dx.doi.org/10.7554/eLife.04187.001

Crystal structure of PfRh5, an essential P. falciparum ligand for invasion of human erythrocytes.,Chen L, Xu Y, Healer J, Thompson JK, Smith BJ, Lawrence MC, Cowman AF Elife. 2014 Oct 8;3:e04187. doi: 10.7554/eLife.04187. PMID:25296023^[10]

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

References

↑ Rodriguez M, Lustigman S, Montero E, Oksov Y, Lobo CA. PfRH5: a novel reticulocyte-binding family homolog of plasmodium falciparum that binds to the erythrocyte, and an investigation of its receptor. PLoS One. 2008 Oct 1;3(10):e3300. PMID:18827878 doi:10.1371/journal.pone.0003300
↑ Baum J, Chen L, Healer J, Lopaticki S, Boyle M, Triglia T, Ehlgen F, Ralph SA, Beeson JG, Cowman AF. Reticulocyte-binding protein homologue 5 invasion of human erythrocytes by Plasmodium falciparum. Int J Parasitol. 2009 Feb;39(3):371-80. PMID:19000690 doi:10.1016/j.ijpara.2008.10.006
↑ Crosnier C, Bustamante LY, Bartholdson SJ, Bei AK, Theron M, Uchikawa M, Mboup S, Ndir O, Kwiatkowski DP, Duraisingh MT, Rayner JC, Wright GJ. Basigin is a receptor essential for erythrocyte invasion by Plasmodium falciparum. Nature. 2011 Nov 9;480(7378):534-7. PMID:22080952 doi:10.1038/nature10606
↑ Chen L, Xu Y, Healer J, Thompson JK, Smith BJ, Lawrence MC, Cowman AF. Crystal structure of PfRh5, an essential P. falciparum ligand for invasion of human erythrocytes. Elife. 2014 Oct 8;3:e04187. PMID:25296023 doi:10.7554/eLife.04187
↑ Reddy KS, Amlabu E, Pandey AK, Mitra P, Chauhan VS, Gaur D. Multiprotein complex between the GPI-anchored CyRPA with PfRH5 and PfRipr is crucial for Plasmodium falciparum erythrocyte invasion. Proc Natl Acad Sci U S A. 2015 Jan 27;112(4):1179-84. PMID:25583518 doi:10.1073/pnas.1415466112
↑ Volz JC, Yap A, Sisquella X, Thompson JK, Lim NT, Whitehead LW, Chen L, Lampe M, Tham WH, Wilson D, Nebl T, Marapana D, Triglia T, Wong W, Rogers KL, Cowman AF. Essential Role of the PfRh5/PfRipr/CyRPA Complex during Plasmodium falciparum Invasion of Erythrocytes. Cell Host Microbe. 2016 Jul 13;20(1):60-71. PMID:27374406 doi:10.1016/j.chom.2016.06.004
↑ Galaway F, Drought LG, Fala M, Cross N, Kemp AC, Rayner JC, Wright GJ. P113 is a merozoite surface protein that binds the N terminus of Plasmodium falciparum RH5. Nat Commun. 2017 Feb 10;8:14333. PMID:28186186 doi:10.1038/ncomms14333
↑ Aniweh Y, Gao X, Hao P, Meng W, Lai SK, Gunalan K, Chu TT, Sinha A, Lescar J, Chandramohanadas R, Li HY, Sze SK, Preiser PR. P. falciparum RH5-Basigin interaction induces changes in the cytoskeleton of the host RBC. Cell Microbiol. 2017 Sep;19(9). PMID:28409866 doi:10.1111/cmi.12747
↑ Alanine DGW, Quinkert D, Kumarasingha R, Mehmood S, Donnellan FR, Minkah NK, Dadonaite B, Diouf A, Galaway F, Silk SE, Jamwal A, Marshall JM, Miura K, Foquet L, Elias SC, Labbe GM, Douglas AD, Jin J, Payne RO, Illingworth JJ, Pattinson DJ, Pulido D, Williams BG, de Jongh WA, Wright GJ, Kappe SHI, Robinson CV, Long CA, Crabb BS, Gilson PR, Higgins MK, Draper SJ. Human Antibodies that Slow Erythrocyte Invasion Potentiate Malaria-Neutralizing Antibodies. Cell. 2019 Jun 13. pii: S0092-8674(19)30553-7. doi: 10.1016/j.cell.2019.05.025. PMID:31204103 doi:http://dx.doi.org/10.1016/j.cell.2019.05.025
↑ Chen L, Xu Y, Healer J, Thompson JK, Smith BJ, Lawrence MC, Cowman AF. Crystal structure of PfRh5, an essential P. falciparum ligand for invasion of human erythrocytes. Elife. 2014 Oct 8;3:e04187. PMID:25296023 doi:10.7554/eLife.04187

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4wat"

Categories: Large Structures | Plasmodium falciparum 3D7 | Chen L

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[4wat]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum_3D7 Plasmodium falciparum 3D7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WAT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WAT FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.18&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4wat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wat OCA], [https://pdbe.org/4wat PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wat RCSB], [https://www.ebi.ac.uk/pdbsum/4wat PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wat ProSAT]</span></td></tr>
 </table>
 == Function ==
-[https://www.uniprot.org/uniprot/RH5_PLAF7 RH5_PLAF7] Essential for the invasion of host erythrocytes by blood stage merozoites (PubMed:25583518, PubMed:27374406, PubMed:25296023, PubMed:22080952, PubMed:18827878, PubMed:19000690, PubMed:31204103, PubMed:28186186, PubMed:28409866). By binding P113 at the surface of the merozoite and human BSG/basigin on the erythrocyte membrane, leads to the establishment of a tight junction between the merozoite and host erythrocyte membranes (PubMed:25583518, PubMed:27374406, PubMed:25296023, PubMed:22080952, PubMed:28186186). In addition, the interaction with BSG results in BSG dimerization which triggers an increase in intracellular Ca(2+) in the erythrocyte (PubMed:27374406, PubMed:28409866). This essential step leads to a rearrangement of the erythrocyte cytoskeleton required for the merozoite invasion (PubMed:28409866).<ref>PMID:18827878</ref> <ref>PMID:19000690</ref> <ref>PMID:22080952</ref> <ref>PMID:25296023</ref> <ref>PMID:25583518</ref> <ref>PMID:27374406</ref> <ref>PMID:28186186</ref> <ref>PMID:28409866</ref> <ref>PMID:31204103</ref>
+[https://www.uniprot.org/uniprot/RH5_PLAF7 RH5_PLAF7] Essential for the invasion of host erythrocytes by blood stage merozoites (PubMed:18827878, PubMed:19000690, PubMed:22080952, PubMed:25296023, PubMed:25583518, PubMed:27374406, PubMed:28186186, PubMed:28409866, PubMed:31204103). By binding P113 at the surface of the merozoite and human BSG/basigin on the erythrocyte membrane, leads to the establishment of a tight junction between the merozoite and host erythrocyte membranes (PubMed:22080952, PubMed:25296023, PubMed:25583518, PubMed:27374406, PubMed:28186186). In addition, the interaction with BSG results in BSG dimerization which triggers an increase in intracellular Ca(2+) in the erythrocyte (PubMed:27374406, PubMed:28409866). This essential step leads to a rearrangement of the erythrocyte cytoskeleton required for the merozoite invasion (PubMed:28409866).<ref>PMID:18827878</ref> <ref>PMID:19000690</ref> <ref>PMID:22080952</ref> <ref>PMID:25296023</ref> <ref>PMID:25583518</ref> <ref>PMID:27374406</ref> <ref>PMID:28186186</ref> <ref>PMID:28409866</ref> <ref>PMID:31204103</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

4wat

From Proteopedia

Current revision

Crystal structure of PfRh5, an essential P. falciparum ligand for invasion of human erythrocytes

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox