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| | <StructureSection load='6omw' size='340' side='right'caption='[[6omw]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='6omw' size='340' side='right'caption='[[6omw]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6omw]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Aedae Aedae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OMW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6OMW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6omw]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Aedes_aegypti Aedes aegypti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OMW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OMW FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene>, <scene name='pdbligand=PAM:PALMITOLEIC+ACID'>PAM</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]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6og0|6og0]], [[6ogh|6ogh]], [[6oii|6oii]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene>, <scene name='pdbligand=PAM:PALMITOLEIC+ACID'>PAM</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">5567053, AAEL005772 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7159 AEDAE])</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=6omw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6omw OCA], [https://pdbe.org/6omw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6omw RCSB], [https://www.ebi.ac.uk/pdbsum/6omw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6omw ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6omw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6omw OCA], [http://pdbe.org/6omw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6omw RCSB], [http://www.ebi.ac.uk/pdbsum/6omw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6omw ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/OBP22_AEDAE OBP22_AEDAE] Involved in modulation of blood-feeding behavior and capacity in female mosquitoes (PubMed:22479185, PubMed:34634943). Required for normal oviposition (PubMed:34634943). Required for normal fecundity and fertility of female and male mosquitoes (PubMed:34634943). Required for normal expression of VGA1 gene, which encodes the egg yolk protein vitellogenin-A1 (PubMed:34634943). Involved in regulation of spermatozoa development (PubMed:34634943). Required for normal female longevity when mosquitoes are maintained on regular sugar meal (PubMed:34634943). Binds long chain fatty acids (PubMed:32094450).<ref>PMID:22479185</ref> <ref>PMID:32094450</ref> <ref>PMID:34634943</ref> (Microbial infection) Facilitates shedding of dengue virus type 2 particles into mosquito saliva (PubMed:34634943). Does not affect dengue virus type 2 replication or infection prevalence in midgut and salivary glands at 14 days after blood feeding (PubMed:34634943).<ref>PMID:34634943</ref> (Microbial infection) Facilitates shedding of Zika virus particles into mosquito saliva (PubMed:34634943). Does not affect Zika virus replication or infection prevalence in midgut and salivary glands at 14 days after blood feeding (PubMed:34634943).<ref>PMID:34634943</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aedae]] | + | [[Category: Aedes aegypti]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Jones, D N]] | + | [[Category: Jones DN]] |
| - | [[Category: Wang, J]] | + | [[Category: Wang J]] |
| - | [[Category: Chemo-sensory signaling]]
| + | |
| - | [[Category: Lipid binding]]
| + | |
| - | [[Category: Odorant-binding protein]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
OBP22_AEDAE Involved in modulation of blood-feeding behavior and capacity in female mosquitoes (PubMed:22479185, PubMed:34634943). Required for normal oviposition (PubMed:34634943). Required for normal fecundity and fertility of female and male mosquitoes (PubMed:34634943). Required for normal expression of VGA1 gene, which encodes the egg yolk protein vitellogenin-A1 (PubMed:34634943). Involved in regulation of spermatozoa development (PubMed:34634943). Required for normal female longevity when mosquitoes are maintained on regular sugar meal (PubMed:34634943). Binds long chain fatty acids (PubMed:32094450).[1] [2] [3] (Microbial infection) Facilitates shedding of dengue virus type 2 particles into mosquito saliva (PubMed:34634943). Does not affect dengue virus type 2 replication or infection prevalence in midgut and salivary glands at 14 days after blood feeding (PubMed:34634943).[4] (Microbial infection) Facilitates shedding of Zika virus particles into mosquito saliva (PubMed:34634943). Does not affect Zika virus replication or infection prevalence in midgut and salivary glands at 14 days after blood feeding (PubMed:34634943).[5]
Publication Abstract from PubMed
Aedes aegypti is the primary vector for transmission of Dengue, Zika and chikungunya viruses. Previously it was shown that Dengue virus infection of the mosquito led to an in increased expression of the odorant binding protein 22 (AeOBP22) within the mosquito salivary gland and that siRNA mediated knockdown of AeOBP22 led to reduced mosquito feeding behaviors. Insect OBPs are implicated in the perception, storage and transport of chemosensory signaling molecules including air-borne odorants and pheromones. AeOBP22 is unusual as it is additionally expressed in multiple tissues, including the antenna, the male reproductive glands and is transferred to females during reproduction, indicating multiple roles in the mosquito life cycle. However, it is unclear what role it plays in these tissues and what ligands it interacts with. Here we present solution and X-ray crystallographic studies that indicate a potential role of AeOBP22 binding to fatty acids, and that the specificity for longer chain fatty acids is regulated by a conformational change in the C-terminal tail that leads to creation of an enlarged binding cavity that enhances binding affinity. This study sheds light onto the native ligands for AeOBP22 and provides insight into its potential functions in different tissues.
Aedes aegypti Odorant Binding Protein 22 selectively binds fatty acids through a conformational change in its C-terminal tail.,Wang J, Murphy EJ, Nix JC, Jones DNM Sci Rep. 2020 Feb 24;10(1):3300. doi: 10.1038/s41598-020-60242-9. PMID:32094450[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sim S, Ramirez JL, Dimopoulos G. Dengue virus infection of the Aedes aegypti salivary gland and chemosensory apparatus induces genes that modulate infection and blood-feeding behavior. PLoS Pathog. 2012;8(3):e1002631. PMID:22479185 doi:10.1371/journal.ppat.1002631
- ↑ Wang J, Murphy EJ, Nix JC, Jones DNM. Aedes aegypti Odorant Binding Protein 22 selectively binds fatty acids through a conformational change in its C-terminal tail. Sci Rep. 2020 Feb 24;10(1):3300. doi: 10.1038/s41598-020-60242-9. PMID:32094450 doi:http://dx.doi.org/10.1038/s41598-020-60242-9
- ↑ Dong S, Ye Z, Tikhe CV, Tu ZJ, Zwiebel LJ, Dimopoulos G. Pleiotropic Odorant-Binding Proteins Promote Aedes aegypti Reproduction and Flavivirus Transmission. mBio. 2021 Oct 26;12(5):e0253121. PMID:34634943 doi:10.1128/mBio.02531-21
- ↑ Dong S, Ye Z, Tikhe CV, Tu ZJ, Zwiebel LJ, Dimopoulos G. Pleiotropic Odorant-Binding Proteins Promote Aedes aegypti Reproduction and Flavivirus Transmission. mBio. 2021 Oct 26;12(5):e0253121. PMID:34634943 doi:10.1128/mBio.02531-21
- ↑ Dong S, Ye Z, Tikhe CV, Tu ZJ, Zwiebel LJ, Dimopoulos G. Pleiotropic Odorant-Binding Proteins Promote Aedes aegypti Reproduction and Flavivirus Transmission. mBio. 2021 Oct 26;12(5):e0253121. PMID:34634943 doi:10.1128/mBio.02531-21
- ↑ Wang J, Murphy EJ, Nix JC, Jones DNM. Aedes aegypti Odorant Binding Protein 22 selectively binds fatty acids through a conformational change in its C-terminal tail. Sci Rep. 2020 Feb 24;10(1):3300. doi: 10.1038/s41598-020-60242-9. PMID:32094450 doi:http://dx.doi.org/10.1038/s41598-020-60242-9
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