Chemical Communication: A Visit with Insects

Mohanty, Smita; Ring, Joshua R.; Prusti, Rabi K.

doi:10.2174/187231308783334153

Cited by 3 publications

(4 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Lepidopteran PBPs are reported to undergo a well-defined dramatic conformational switch when the pH is changed from 6.0 or above to 5.0 or below 7 – 17 . This pH-driven conformational change has been shown to be associated with ligand binding (at high pH) and release at low pH 6 – 17 . To investigate the effect of pH on OfurPBP2 conformation at high and low pH levels, we used far-UV CD and high-resolution solution NMR analysis.…”

Section: Discussionmentioning

confidence: 98%

“…PBPs comprise a subfamily of OBPs in insects, which were first identified in the giant silk moth Antheraea polyphemus 4 , 5 . These acidic proteins have molecular masses between 14–16 kDa with six conserved cysteine residues 6 . Based on studies carried out on both recombinant PBPs 7 – 17 as well as native PBPs isolated from moth antennae 4 , 15 , it is widely accepted that these carrier proteins pick up the hydrophobic pheromone molecules at pH above 6.0 (pH of sensillar lymph) 7 – 12 and transport them across the sensillar lymph releasing at acidic pH near the membrane-bound olfactory receptor by undergoing a dramatic conformational switch 7 , 8 , 13 – 16 .…”

Section: Introductionmentioning

confidence: 99%

“…Based on studies carried out on both recombinant PBPs 7 – 17 as well as native PBPs isolated from moth antennae 4 , 15 , it is widely accepted that these carrier proteins pick up the hydrophobic pheromone molecules at pH above 6.0 (pH of sensillar lymph) 7 – 12 and transport them across the sensillar lymph releasing at acidic pH near the membrane-bound olfactory receptor by undergoing a dramatic conformational switch 7 , 8 , 13 – 16 . Based on extensive structure-function studies on Antheraea polyphemus pheromone-binding protein1 (ApolPBP1), Bombyx mori PBP (BmorPBP), Amyelois transitella PBP1 (AtraPBP1) and Lymantria dispar PBP2 (LdisPBP2), it is clear that the proteins exist in lipid-bound or open or PBP B conformation at neutral pH, and lipid-free or closed or PBP A conformation at acidic pH 6 – 17 . In the bound or PBP B conformation, the lipid molecule occupies the binding pocket while the unstructured C-terminus is exposed to the solvent 7 – 12 .…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Structure and Function Studies of Asian Corn Borer Ostrinia furnacalis Pheromone Binding Protein2

Mazumder

Dahal

Chaudhary

et al. 2018

Sci Rep

Self Cite

View full text Add to dashboard Cite

Lepidopteran male moths have an extraordinarily sensitive olfactory system that is capable of detecting and responding to minute amounts of female-secreted pheromones over great distances. Pheromone-binding proteins (PBPs) in male antennae ferry the hydrophobic ligand across the aqueous lymph to the olfactory receptor neuron triggering the response. PBPs bind ligands at physiological pH of the lymph and release them at acidic pH near the receptor while undergoing a conformational change. In Anthereae polyphemus PBP1, ligand binding to the hydrophobic pocket and its release is regulated by two biological gates: His70 and His95 at one end of the pocket and C-terminus tail at the other end. Interestingly, in Asian corn borer Ostrinia furnacalis PBP2 (OfurPBP2), critical residues for ligand binding and release are substituted in both biological gates. The impact of these substitutions on the ligand binding and release mechanism in OfurPBP2 is not known. We report here overexpression of soluble OfurPBP2 and structural characterization at high and low pH by circular dichroism (CD) and NMR. Ligand binding and ab initio model development were carried out with fluorescence and small-angle X-ray scattering (SAXS) respectively. OfurPBP2 in solution at pH 6.5 is homogeneous, well-folded and has a compact globular shape.

show abstract

Section: Discussionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Structure and Function Studies of Asian Corn Borer Ostrinia furnacalis Pheromone Binding Protein2

Mazumder

Dahal

Chaudhary

et al. 2018

Sci Rep

Self Cite

View full text Add to dashboard Cite

show abstract

“…They are small (molecular weights of ∼14−16 kDa) acidic, highly water soluble proteins. PBPs found in different moth species exhibit a high degree of sequence similarity with six conserved cysteine residues that are involved in the formation of three disulfide bonds 3 (Figure 1A).…”

mentioning

confidence: 99%

Pheromone Perception: Mechanism of the Reversible Coil–Helix Transition in Antheraea polyphemus Pheromone-Binding Protein 1

et al. 2019

Self Cite

View full text Add to dashboard Cite

Pheromone-binding protein (PBP) in male moth antennae transports pheromone to the olfactory receptor neuron by undergoing a pH-dependent conformational switch, from PBP B at higher pH to PBP A at lower pH, associated with ligand binding and release, respectively. The characteristic feature of the dramatic protein switch is the pH-dependent reversible coil−helix transition of the C-terminus. In the PBP B conformation at pH >6.0, the C-terminus is exposed to the solvent as a coil while the ligand occupies the hydrophobic pocket. However, in the PBP A conformation at acidic pH, the C-terminus switches to a helix and releases the ligand by outcompeting it for the hydrophobic pocket. In Antheraea polyphemus PBP1 (ApolPBP1), the C-terminus (P 129 −V 142 ) is composed predominantly of hydrophobic residues except for three strategically located acidic residues: Asp 132 , Glu 137 , and Glu 141 . Here, we report for the first time on the consequences of the mutation of one or more acidic residues in the pH-driven reversible coil−helix transition of the ApolPBP1 C-terminus through biophysical characterization. Mutation of any single acidic residue in the C-terminus to its neutral counterpart destabilizes the helix formation at lower pH; these mutants exist as a mixture of both conformations. However, mutation of the two terminal acidic residues together knocks out the protein switch and adversely affects both ligand binding and release functions. Thus, these mutant proteins remain in the open (PBP B ) conformation at all pH levels.

show abstract

Sensilla on the labial palps of the cave species Tachycines plumiopedella Li, Feng & Luo, 2021 (Orthoptera: Rhaphidophoridae)

2023

View full text Add to dashboard Cite

Chemical Communication: A Visit with Insects

Cited by 3 publications

References 0 publications

Structure and Function Studies of Asian Corn Borer Ostrinia furnacalis Pheromone Binding Protein2

Structure and Function Studies of Asian Corn Borer Ostrinia furnacalis Pheromone Binding Protein2

Pheromone Perception: Mechanism of the Reversible Coil–Helix Transition in Antheraea polyphemus Pheromone-Binding Protein 1

Sensilla on the labial palps of the cave species Tachycines plumiopedella Li, Feng & Luo, 2021 (Orthoptera: Rhaphidophoridae)

Contact Info

Product

Resources

About