Alcohol Binding to the Odorant Binding Protein LUSH: Multiple Factors Affecting Binding Affinities

Ader, Lauren; Jones, David N. M.; Lin, Hai

doi:10.1021/bi100540k

Cited by 6 publications

(3 citation statements)

References 46 publications

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“…The subgroup of ABPIIs formed three clades. In one clade, the characterized OBP LUSH of D. melanogaster, crucial for binding pheromones and short-chain alcohols among other compounds (Ader, Jones, & Lin, 2010;Laughlin et al, 2008;Xu, Atkinson, Jones, & Smith, 2005), was localized together with ClapOBP01 and ClapOBP30 (Figure 3, bootstrap value of 84%). Another ABPII clade contained four C. lapponica minus-C OBPs.…”

Section: Identification Of Putative Soluble Proteins In Wfp and Bfpmentioning

confidence: 99%

A subset of chemosensory genes differs between two populations of a specialized leaf beetle after host plant shift

Wang

Pentzold

Kunert

et al. 2018

Ecology and Evolution

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Due to its fundamental role in shaping host selection behavior, we have analyzed the chemosensory repertoire of Chrysomela lapponica. This specialized leaf beetle evolved distinct populations which shifted from the ancestral host plant, willow (Salix sp., Salicaceae), to birch (Betula rotundifolia, Betulaceae). We identified 114 chemosensory candidate genes in adult C. lapponica: 41 olfactory receptors (ORs), eight gustatory receptors, 17 ionotropic receptors, four sensory neuron membrane proteins, 32 odorant binding proteins (OBPs), and 12 chemosensory proteins (CSP) by RNA‐seq. Differential expression analyses in the antennae revealed significant upregulation of one minus‐C OBP (Clap OBP27) and one CSP (Clap CSP12) in the willow feeders. In contrast, one OR (Clap OR17), four minus‐C OBPs (Clap OBP02, 07, 13, 20), and one plus‐C OBP (Clap OBP32) were significantly upregulated in birch feeders. The differential expression pattern in the legs was more complex. To narrow down putative ligands acting as cues for host discrimination, the relative abundance and diversity of volatiles of the two host plant species were analyzed. In addition to salicylaldehyde (willow‐specific), both plant species differed mainly in their emission rate of terpenoids such as (E,E)‐α‐farnesene (high in willow) or 4,8‐dimethylnona‐1,3,7‐triene (high in birch). Qualitatively, the volatiles were similar between willow and birch leaves constituting an “olfactory bridge” for the beetles. Subsequent structural modeling of the three most differentially expressed OBPs and docking studies using 22 host volatiles indicated that ligands bind with varying affinity. We suggest that the evolution of particularly minus‐C OBPs and ORs in C. lapponica facilitated its host plant shift via chemosensation of the phytochemicals from birch as novel host plant.

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Section: Identification Of Putative Soluble Proteins In Wfp and Bfpmentioning

confidence: 99%

A subset of chemosensory genes differs between two populations of a specialized leaf beetle after host plant shift

Wang

Pentzold

Kunert

et al. 2018

Ecology and Evolution

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“…These data may suggest, when combined with structural implications of L390, that ethanol interacts with the translocation pore in a conformation dependent manner. The odorant binding protein LUSH from Drosophila melanogaster has been previously shown to bind alcohol through a set of concerted hydrogen bonding interactions [ 45 ]. Hydrogen bonding networks coupled to substrate transport have also been previously observed in numerous MFS transporters, including LacY [ 46 ].…”

Section: Discussionmentioning

confidence: 99%

Functional Characterization of the Saccharomyces cerevisiae Equilibrative Nucleoside Transporter 1 (ScENT1)

2018

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Equilibrative nucleoside transporters (ENTs) are polytopic membrane transporters responsible for the translocation of nucleosides, nucleobases—to a lesser extent—and nucleoside analog therapeutics across cellular membranes. ENTs function in a diffusion controlled bidirectional manner and are thought to utilize an alternating access transport mechanism. However, a detailed understanding of ENT function at the molecular level has remained elusive. ScENT1 (formerly known as Function Unknown Now 26 or FUN26) is the only known ENT ortholog endogenously expressed in S. cerevisiae, and a proteoliposome assay system was used to study homogenously overexpressed and purified ScENT1 (wildtype relative to L390A and F249I mutants). L390 and F249 are highly conserved residues and were found to alter transporter function. L390A produced a reduction of mean transport activity while F249I increased mean substrate translocation relative to wildtype protein. However, both mutations resulted in transport of UTP—a novel gain of function for any ENT. These residues were then mapped onto an ab initio model of FUN26 which suggests they function in substrate translocation (L390) or cytoplasmic gating (F249). Furthermore, wildtype, L390A, and F249I were found to be sensitive to the presence of alcohols. Ethanol attenuated ScENT1-mediated transport of uridine by ~50%. These findings further demonstrate functional similarities between ScENT1 and human ENT isoforms and support identification of FUN26 as ScENT1, the first ENT isoform in S. cerevisiae.

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“…In this study, we developed an OBP-fused ISFET biosensor and demonstrated its feasibility for application as an olfactory sensor. To detect ethanol at various concentrations, a LUSH OBP, which is well-known to bind to various types of alcohols, − was used as a sensing substrate. We also used a dual-gate sensing system to enhance the signal produced by the molecular interaction between the LUSH and ethanol.…”

Section: Introductionmentioning

confidence: 99%

Field-Effect Transistor Biosensor Platform Fused with Drosophila Odorant-Binding Proteins for Instant Ethanol Detection

Lim

Kwon

Cho

2017

ACS Appl. Mater. Interfaces

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Odorant-binding proteins (OBPs) have attracted considerable attention as sensing substrates for the development of olfactory biosensors. The Drosophila LUSH protein is an OBP and is known to bind to various alcohols. Technology that uses the LUSH protein has great potential to provide crucial information through odorant detection. In this work, the LUSH protein was used as a sensing substrate to detect the ethanol concentration. Furthermore, we fused the LUSH protein with a silicon-on-insulator (SOI)-based ion-sensitive field-effect transistor (ISFET) to measure the electrical signals that arise from molecular interactions between the LUSH and ethanol. A dual-gate sensing system for self-amplification of the signal resulting from the molecular interaction between the LUSH and ethanol was then used to achieve a much higher sensitivity than a conventional ISFET. In the end, we successfully detected ethanol at concentrations ranging between 0.001 and 1% using the LUSH OBP-fused ISFET olfactory sensor. The OBP-fused SOI-based olfactory ISFET sensor can lead to the development of handheld sensors for various purposes such as detecting toxic chemicals, narcotics control, testing for food freshness, and noninvasive diagnoses.

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Alcohol Binding to the Odorant Binding Protein LUSH: Multiple Factors Affecting Binding Affinities

Cited by 6 publications

References 46 publications

A subset of chemosensory genes differs between two populations of a specialized leaf beetle after host plant shift

A subset of chemosensory genes differs between two populations of a specialized leaf beetle after host plant shift

Functional Characterization of the Saccharomyces cerevisiae Equilibrative Nucleoside Transporter 1 (ScENT1)

Field-Effect Transistor Biosensor Platform Fused with Drosophila Odorant-Binding Proteins for Instant Ethanol Detection

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