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Peptidomic analysis of the venom of the solitary bee Xylocopa appendiculata circumvolans

Overview of attention for article published in Journal of Venomous Animals and Toxins including Tropical Diseases, August 2017
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Title
Peptidomic analysis of the venom of the solitary bee Xylocopa appendiculata circumvolans
Published in
Journal of Venomous Animals and Toxins including Tropical Diseases, August 2017
DOI 10.1186/s40409-017-0130-y
Pubmed ID
Authors

Kohei Kazuma, Kenji Ando, Ken-ichi Nihei, Xiaoyu Wang, Marisa Rangel, Marcia Regina Franzolin, Kanami Mori-Yasumoto, Setsuko Sekita, Makoto Kadowaki, Motoyoshi Satake, Katsuhiro Konno

Abstract

Among the hymenopteran insect venoms, those from social wasps and bees - such as honeybee, hornets and paper wasps - have been well documented. Their venoms are composed of a number of peptides and proteins and used for defending their nests and themselves from predators. In contrast, the venoms of solitary wasps and bees have not been the object of further research. In case of solitary bees, only major peptide components in a few venoms have been addressed. Therefore, the aim of the present study was to explore the peptide component profile of the venom from the solitary bee Xylocopa appendiculata circumvolans by peptidomic analysis with using LC-MS. A reverse-phase HPLC connected to ESI-OrbiTrap MS was used for LC-MS. On-line mass fingerprinting was made from TIC, and data-dependent tandem mass spectrometry gave MSMS spectra. A major peptide component was isolated by reverse-phase HPLC by conventional way, and its sequence was determined by Edman degradation, which was finally corroborated by solid phase synthesis. Using the synthetic specimen, biological activities (antimicrobial activity, mast cell devaluation, hemolysis, leishmanicidal activity) and pore formation in artificial lipid bilayer were evaluated. On-line mass fingerprinting revealed that the crude venom contained 124 components. MS/MS analysis gave 75 full sequences of the peptide components. Most of these are related to the major and novel peptide, xylopin. Its sequence, GFVALLKKLPLILKHLH-NH2, has characteristic features of linear cationic α-helical peptides; rich in hydrophobic and basic amino acids with no disulfide bond, and accordingly, it can be predicted to adopt an amphipathic α-helix secondary structure. In biological evaluation, xylopin exhibited broad-spectrum antimicrobial activity, and moderate mast cell degranulation and leishmanicidal activities, but showed virtually no hemolytic activity. Additionally, the peptide was able to incorporate pores in artificial lipid bilayers of azolectin, confirming the mechanism of the cytolytic activity by pore formation in biological membranes. LC-ESI-MS and MS/MS analysis of the crude venom extract from a solitary bee Xylocopa appendiculata circumvolans revealed that the component profile of this venom mostly consisted of small peptides. The major peptide components, xylopin and xylopinin, were purified and characterized in a conventional manner. Their chemical and biological characteristics, belonging to linear cationic α-helical peptides, are similar to the known solitary bee venom peptides, melectin and osmin. Pore formation in artificial lipid bilayers was demonstrated for the first time with a solitary bee peptide.

Twitter Demographics

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Mendeley readers

The data shown below were compiled from readership statistics for 26 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 26 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 5 19%
Professor 3 12%
Student > Doctoral Student 2 8%
Researcher 2 8%
Student > Bachelor 2 8%
Other 3 12%
Unknown 9 35%
Readers by discipline Count As %
Agricultural and Biological Sciences 4 15%
Medicine and Dentistry 3 12%
Biochemistry, Genetics and Molecular Biology 2 8%
Immunology and Microbiology 2 8%
Environmental Science 1 4%
Other 2 8%
Unknown 12 46%

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 01 September 2017.
All research outputs
#7,277,101
of 11,689,928 outputs
Outputs from Journal of Venomous Animals and Toxins including Tropical Diseases
#162
of 305 outputs
Outputs of similar age
#150,234
of 263,453 outputs
Outputs of similar age from Journal of Venomous Animals and Toxins including Tropical Diseases
#4
of 7 outputs
Altmetric has tracked 11,689,928 research outputs across all sources so far. This one is in the 23rd percentile – i.e., 23% of other outputs scored the same or lower than it.
So far Altmetric has tracked 305 research outputs from this source. They receive a mean Attention Score of 3.2. This one is in the 29th percentile – i.e., 29% of its peers scored the same or lower than it.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 263,453 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 33rd percentile – i.e., 33% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 7 others from the same source and published within six weeks on either side of this one. This one has scored higher than 3 of them.