Structure of an Odorant-Vinding Protein form the Mosquito Aedes aegypti Suggests a Binding Pocket Covered by a pH-Sensitive

Leite, N; Krogh, R; Xu, W; Ishida, Y; Iulek, J; Leal, W; Oliva, G

Title: Structure of an Odorant-Vinding Protein form the Mosquito Aedes aegypti Suggests a Binding Pocket Covered by a pH-Sensitive

Full Record
Other Related Research

Abstract

The yellow fever mosquito, Aedes aegypti, is the primary vector for the viruses that cause yellow fever, mostly in tropical regions of Africa and in parts of South America, and human dengue, which infects 100 million people yearly in the tropics and subtropics. A better understanding of the structural biology of olfactory proteins may pave the way for the development of environmentally-friendly mosquito attractants and repellents, which may ultimately contribute to reduction of mosquito biting and disease transmission. Previously, we isolated and cloned a major, female-enriched odorant-binding protein (OBP) from the yellow fever mosquito, AaegOBP1, which was later inadvertently renamed AaegOBP39. We prepared recombinant samples of AaegOBP1 by using an expression system that allows proper formation of disulfide bridges and generates functional OBPs, which are indistinguishable from native OBPs. We crystallized AaegOBP1 and determined its three-dimensional structure at 1.85 {angstrom} resolution by molecular replacement based on the structure of the malaria mosquito OBP, AgamOBP1, the only mosquito OBP structure known to date. The structure of AaegOBP1 (= AaegOBP39) shares the common fold of insect OBPs with six {alpha}-helices knitted by three disulfide bonds. A long molecule of polyethylene glycol (PEG) was built into the electron-density maps identified in a longmore »« less

Authors:: Leite, N; Krogh, R; Xu, W; Ishida, Y; Iulek, J; Leal, W; Oliva, G

Publication Date:: Sat Dec 31 00:00:00 EST 2011

Research Org.:: Brookhaven National Lab. (BNL), Upton, NY (United States)

Sponsoring Org.:: USDOE SC OFFICE OF SCIENCE (SC)

OSTI Identifier:: 1042254

Report Number(s):: BNL-97932-2012-JA
Journal ID: ISSN 1932-6203; TRN: US201212%%665

DOE Contract Number:: DE-AC02-98CH10886

Resource Type:: Journal Article

Journal Name:: PLoS One

Additional Journal Information:: Journal Volume: 4; Journal Issue: 11; Journal ID: ISSN 1932-6203

Country of Publication:: United States

Language:: English

Subject:: 59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES; AFFINITY; AFRICA; CONFORMATIONAL CHANGES; DICHROISM; DIMERS; DISEASES; DISULFIDES; ELECTRON DENSITY; FEVER; HUMAN POPULATIONS; HYDROGEN; INSECTS; MALARIA; MOLECULES; MOSQUITOES; ODORANTS; POLYETHYLENE GLYCOLS; PH VALUE; PROTEINS; PROTEIN STRUCTURE; RECEPTORS; REDUCTION; RESOLUTION; SOUTH AMERICA; TRANSMISSION; TROPICAL REGIONS; TUNNELS; DISEASE VECTORS; VIRUSES

Citation Formats


                    Leite, N, Krogh, R, Xu, W, Ishida, Y, Iulek, J, Leal, W, and Oliva, G. Structure of an Odorant-Vinding Protein form the Mosquito Aedes aegypti Suggests a Binding Pocket Covered by a pH-Sensitive.  United States: N. p., 2011. 
        Web.

Copy to clipboard


                    Leite, N, Krogh, R, Xu, W, Ishida, Y, Iulek, J, Leal, W, & Oliva, G. Structure of an Odorant-Vinding Protein form the Mosquito Aedes aegypti Suggests a Binding Pocket Covered by a pH-Sensitive.  United States.

Copy to clipboard


                    Leite, N, Krogh, R, Xu, W, Ishida, Y, Iulek, J, Leal, W, and Oliva, G. 2011.  
        "Structure of an Odorant-Vinding Protein form the Mosquito Aedes aegypti Suggests a Binding Pocket Covered by a pH-Sensitive".  United States.

Copy to clipboard


                    
@article{osti_1042254,

  title        = {Structure of an Odorant-Vinding Protein form the Mosquito Aedes aegypti Suggests a Binding Pocket Covered by a pH-Sensitive},

  author       = {Leite, N and Krogh, R and Xu, W and Ishida, Y and Iulek, J and Leal, W and Oliva, G},

  abstractNote = {The yellow fever mosquito, Aedes aegypti, is the primary vector for the viruses that cause yellow fever, mostly in tropical regions of Africa and in parts of South America, and human dengue, which infects 100 million people yearly in the tropics and subtropics. A better understanding of the structural biology of olfactory proteins may pave the way for the development of environmentally-friendly mosquito attractants and repellents, which may ultimately contribute to reduction of mosquito biting and disease transmission. Previously, we isolated and cloned a major, female-enriched odorant-binding protein (OBP) from the yellow fever mosquito, AaegOBP1, which was later inadvertently renamed AaegOBP39. We prepared recombinant samples of AaegOBP1 by using an expression system that allows proper formation of disulfide bridges and generates functional OBPs, which are indistinguishable from native OBPs. We crystallized AaegOBP1 and determined its three-dimensional structure at 1.85 {angstrom} resolution by molecular replacement based on the structure of the malaria mosquito OBP, AgamOBP1, the only mosquito OBP structure known to date. The structure of AaegOBP1 (= AaegOBP39) shares the common fold of insect OBPs with six {alpha}-helices knitted by three disulfide bonds. A long molecule of polyethylene glycol (PEG) was built into the electron-density maps identified in a long tunnel formed by a crystallographic dimer of AaegOBP1. Circular dichroism analysis indicated that delipidated AaegOBP1 undergoes a pH-dependent conformational change, which may lead to release of odorant at low pH (as in the environment in the vicinity of odorant receptors). A C-terminal loop covers the binding cavity and this 'lid' may be opened by disruption of an array of acid-labile hydrogen bonds thus explaining reduced or no binding affinity at low pH.},

  doi          = {},

  url          = {https://www.osti.gov/biblio/1042254},
  journal      = {PLoS One},

  issn         = {1932-6203},

  number       = 11,

  volume       = 4,

  place        = {United States},

  year         = {Sat Dec 31 00:00:00 EST 2011},

  month        = {Sat Dec 31 00:00:00 EST 2011}

}

Copy to clipboard

Journal Article:

Other availability

Find in Google Scholar

Search WorldCat to find libraries that may hold this journal

Save / Share:

Export Metadata

Save to My Library

Similar records in OSTI.GOV collections:

Aedes aegypti Odorant Binding Protein 22 selectively binds fatty acids through a conformational change in its C-terminal tail

Journal Article Wang, Jing; Murphy, Emma; Nix, Jay; ... - Scientific Reports

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,more »« less
https://doi.org/10.1038/s41598-020-60242-9

Full Text Available
High Rate of Non-Human Feeding by Aedes aegypti Reduces Zika Virus Transmission in South Texas

Journal Article Olson, Mark; Ndeffo-Mbah, Martial; Juarez, Jose; ... - Viruses

Mosquito-borne viruses are emerging or re-emerging globally, afflicting millions of people around the world. Aedes aegypti, the yellow fever mosquito, is the principal vector of dengue, Zika, and chikungunya viruses, and has well-established populations across tropical and subtropical urban areas of the Americas, including the southern United States. While intense arboviral epidemics have occurred in Mexico and further south in the Americas, local transmission in the United States has been minimal. Here, we study Ae. aegypti and Culex quinquefasciatus host feeding patterns and vertebrate host communities in residential environments of South Texas to identify host-utilization relative to availability. Only 31%more »« less
Cited by 21
https://doi.org/10.3390/v12040453
A mosquito hemolymph odorant-binding protein family member specifically binds juvenile hormone

Journal Article Kim, Il; Pham, Van; Jablonka, Willy; ... - Journal of Biological Chemistry

Juvenile hormone (JH) is a key regulator of insect development and reproduction. In adult mosquitoes, it is essential for maturation of the ovary and normal male reproductive behavior, but how JH distribution and activity is regulated after secretion is unclear. Here, we report a new type of specific JH-binding protein, given the name mosquito juvenile hormone-binding protein (mJHBP), which circulates in the hemolymph of pupal and adult Aedes aegypti males and females. mJHBP is a member of the odorant-binding protein (OBP) family, and orthologs are present in the genomes of Aedes, Culex, and Anopheles mosquito species. Using isothermal titration calorimetry,more »« less
Cited by 32
https://doi.org/10.1074/jbc.m117.802009

Full Text Available
Surveillance of Aedes aegypti indoors and outdoors using Autocidal Gravid Ovitraps in South Texas during local transmission of Zika virus, 2016 to 2018

Journal Article Martin, Estelle; Medeiros, Matthew; Carbajal, Ester; ... - Acta Tropica

The yellow fever mosquito, Aedes aegypti, has facilitated the re-emergence of dengue virus (DENV) and emergence of chikungunya virus (CHIKV) and Zika virus (ZIKV) in the Americas and the Caribbean. The recent transmission of these arboviruses in the continental United States has been limited, to date, to South Florida and South Texas despite Ae. aegypti occurring over a much larger geographical region within the country. The main goal of our study was to provide the first long term longitudinal study of Ae. aegypti and enhance the knowledge about the indoor and outdoor relative abundance of Ae. aegypti as a proxymore »« less
Cited by 18
https://doi.org/10.1016/j.actatropica.2019.02.006

Full Text Available
Restriction fragment length polymorphism mapping of quantitative trait loci for malaria parasite susceptibility in the mosquito Aedes aegypti

Journal Article Severson, D; Thathy, V; Mori, A - Genetics

Susceptibility of the mosquito Aedes aegypti to the malarial parasite Plasmodium gallinaceum was investigated as a quantitative trait using restriction fragment length polymorphisms (RFLP). Two F{sub 2} populations of mosquitoes were independently prepared from pairwise matings between a highly susceptible and a refractory strain of A. aegypti. RFLP were tested for association with oocyst development on the mosquito midgut. Two putative quantitative trait loci (QTL) were identified that significantly affect susceptibility. One QTL, pgs [2,LF98], is located on chromosome 2 and accounted for 65 and 49% of the observed phenotypic variance in the two populations, respectively. A second QTL, pgs[3,MalI],more »« less

Similar Records