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

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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Molecular and Functional Characterization of Three Odorant-Binding Protein from Periplaneta americana

PLoS ONE ◽

10.1371/journal.pone.0170072 ◽

2017 ◽

Vol 12 (1) ◽

pp. e0170072 ◽

Cited By ~ 10

Author(s):

Zhao-Qun Li ◽

Peng He ◽

Ya-Nan Zhang ◽

Shuang-Lin Dong

Keyword(s):

Periplaneta Americana ◽

Binding Protein ◽

Functional Characterization ◽

Odorant Binding Protein ◽

Odorant Binding

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Molecular and Functional Characterization of an Odorant Binding Protein of the Asian Elephant,Elephas maximus: Implications for the Role of Lipocalins in Mammalian Olfaction†

Biochemistry ◽

10.1021/bi0256734 ◽

2002 ◽

Vol 41 (39) ◽

pp. 11786-11794 ◽

Cited By ~ 33

Author(s):

Josef Lazar ◽

David R. Greenwood ◽

L. E. L. Rasmussen ◽

Glenn D. Prestwich

Keyword(s):

Binding Protein ◽

Functional Characterization ◽

Odorant Binding Protein ◽

Asian Elephant ◽

Elephas Maximus ◽

Odorant Binding

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Key Amino Residues Determining Binding Activities of the Odorant Binding Protein AlucOBP22 to Two Host Plant Terpenoids of Apolygus lucorum

Journal of Agricultural and Food Chemistry ◽

10.1021/acs.jafc.8b05975 ◽

2019 ◽

Vol 67 (21) ◽

pp. 5949-5956 ◽

Cited By ~ 7

Author(s):

Hangwei Liu ◽

Hongxia Duan ◽

Qi Wang ◽

Yong Xiao ◽

Qian Wang ◽

...

Keyword(s):

Host Plant ◽

Binding Protein ◽

Odorant Binding Protein ◽

Apolygus Lucorum ◽

Odorant Binding

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Localization and Functional Characterization of Pulmonary Bovine Odorant-Binding Protein

Veterinary Pathology ◽

10.1177/0300985810381907 ◽

2010 ◽

Vol 48 (6) ◽

pp. 1054-1060 ◽

Cited By ~ 3

Author(s):

G. B. Mitchell ◽

M. E. Clark ◽

R. Lu ◽

J. L. Caswell

Keyword(s):

Inflammatory Mediators ◽

Binding Protein ◽

Pulmonary Inflammation ◽

Functional Characterization ◽

Odorant Binding Protein ◽

Surface Epithelium ◽

Functional Studies ◽

Flight Mass Spectrometry ◽

Odorant Binding

Bovine odorant-binding protein (OBP) may function in olfaction and defense against oxidative injury, but its role in inflammation and defense against bacterial infection has not been investigated. Expression of OBP was discovered in the bovine lung and found to undergo changes in abundance during glucocorticoid administration and stress. OBP was localized to nasal, tracheal, and bronchial mucosal glands with immunohistochemistry, with faint expression in airway surface epithelium and none in bronchioles or alveoli. Two isoforms of OBP were identified, appearing to be differentially regulated during lipopolysaccharide-induced pulmonary inflammation, but differences between these isoforms were not revealed by matrix-assisted laser desorption/ionization–time of flight mass spectrometry. Functional studies showed no effect of OBP on in vitro growth of Escherichia coli or Mannheimia haemolytica under iron-replete or iron-depleted conditions, nor did OBP opsonize bacteria for an enhanced neutrophil oxidative burst. However, OBP did reduce the ability of supernatants from lipopolysaccharide-stimulated macrophages to induce neutrophil chemotaxis. These findings indicate that OBP may inhibit neutrophil recruitment by inflammatory mediators, and they suggest an ability to bind macrophage-derived inflammatory mediators within the airways.

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