Three amino acid residues of an odorant-binding protein are involved in binding odours inLoxostege sticticalisL.

2015 ◽  
Vol 24 (5) ◽  
pp. 528-538 ◽  
Author(s):  
J. Yin ◽  
X. Zhuang ◽  
Q. Wang ◽  
Y. Cao ◽  
S. Zhang ◽  
...  
Keyword(s):  
Amino Acid ◽  
Binding Protein ◽  
Odorant Binding Protein ◽  
Amino Acid Residues ◽  
Odorant Binding

scholarly journals Amino Acid Sequence, Post-translational Modifications, Binding and Labelling of Porcine Odorant-binding Protein

1998 ◽  
Vol 23 (6) ◽  
pp. 689-698 ◽  
Author(s):  
S. Paolini ◽  
A. Scaloni ◽  
A. Amoresano ◽  
S. Marchese ◽  
E. Napolitano ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Binding Protein ◽  
Odorant Binding Protein ◽  
Post Translational Modifications ◽  
Odorant Binding ◽  
Porcine Odorant Binding Protein

scholarly journals Odorant-binding protein. Characterization of ligand binding.

1990 ◽  
Vol 265 (11) ◽  
pp. 6118-6125
Author(s):  
J Pevsner ◽  
V Hou ◽  
A M Snowman ◽  
S H Snyder
Keyword(s):  
Ligand Binding ◽  
Binding Protein ◽  
Protein Characterization ◽  
Odorant Binding Protein ◽  
Odorant Binding

Molecular and Functional Characterization of One Odorant-Binding Protein Gene OBP3 in Bemisia tabaci (Hemiptera: Aleyrodidae)

2019 ◽  
Author(s):  
Ran Wang ◽  
Yuan Hu ◽  
Peiling Wei ◽  
Cheng Qu ◽  
Chen Luo
Keyword(s):  
Host Plant ◽  
Bemisia Tabaci ◽  
Binding Protein ◽  
Insect Pest ◽  
Critical Role ◽  
Functional Characterization ◽  
Odorant Binding Protein ◽  
Binding Characteristics ◽  
And Function ◽  
Odorant Binding

Abstract Odorant binding proteins (OBPs) of insects play a critical role in chemical perceptions and choice of insect host plant. Bemisia tabaci is a notorious insect pest which can damage more than 600 plant species. In order to explore functions of OBPs in B. tabaci, here we investigated binding characteristics and function of odorant-binding protein 3 in B. tabaci (BtabOBP3). The results indicated that BtabOBP3 shows highly similar sequence with OBPs of other insects, including the typical signature motif of six cysteines. The recombinant BtabOBP3 protein was obtained, and the evaluation of binding affinities to tested volatiles of host plant was conducted, then the results indicated that β-ionone had significantly higher binding to BtabOBP3 among other tested plant volatiles. Furthermore, silencing of BtabOBP3 significantly altered choice behavior of B. tabaci to β-ionone. In conclusion, it has been demonstrated that BtabOBP3 exerts function as one carrier of β-ionone and the results could be contributed to reveal the mechanisms of choosing host plant in B. tabaci.

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