BMC Genomics, 2013 Nov 7;14(1):766
BACKGROUND:
Honeybee venom is a complicated defensive toxin that has a
wide range of pharmacologically active compounds. Some of these compounds are
useful for human therapeutics. There are two major forms of honeybee venom used
in pharmacological applications: manually (or reservoir disrupting) extracted
glandular venom (GV), and venom extracted through the use of electrical
stimulation (ESV). A proteome comparison of these two venom forms and an
understanding of the phosphorylation status of ESV, are still very limited.
Here, the proteomes of GV and ESV were compared using both gel-based and
gel-free proteomics approaches and the phosphoproteome of ESV was determined
through the use of TiO2 enrichment.
RESULTS:
Of the 43 proteins identified in GV, < 40% were venom
toxins, and > 60% of the proteins were non-toxic proteins resulting from
contamination by gland tissue damage during extraction and bee death. Of the 17
proteins identified in ESV, 14 proteins (>80%) were venom toxic proteins and
most of them were found in higher abundance than in GV. Moreover, two novel
proteins (dehydrogenase/reductase SDR family member 11-like and histone
H2B.3-like) and three novel phosphorylation sites (icarapin (S43),
phospholipase A-2 (T145), and apamin (T23)) were identified.
CONCLUSIONS:
Our data demonstrate that venom extracted manually is
different from venom extracted using ESV, and these differences may be
important in their use as pharmacological agents. ESV may be more efficient
than GV as a potential pharmacological source because of its higher venom
protein content, production efficiency, and without the need to kill honeybee.
The three newly identified phosphorylated venom proteins in ESV may elicit a
different immune response through the specific recognition of antigenic
determinants. The two novel venom proteins extend our proteome coverage of
honeybee venom.
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