2026-10-13T22:30:24Z
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oai:figshare.com:article/34010799
2026-09-28T08:09:35Z
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Proteomic
Analysis Reveals Trace O‑Glycosylation Signatures
of Honeybee Venom Melittin
Hacı Mehmet Kayili (25120824)
Sena Aksoy (13647204)
Betul Karabudak (25120827)
Ekin Varol (25120830)
Lokman Varisli (11267712)
Kemal Sami Korkmaz (11267730)
Banu Yücel (25120833)
Bekir Salih (5985044)
Ayse Nalbantsoy (2808874)
Biochemistry
Genetics
Molecular Biology
Environmental Sciences not elsewhere classified
Chemical Sciences not elsewhere classified
Ecology
targeted analysis demonstrated
sampled colony pools
quantitative analyses revealed
performed using label
multivariate bioinformatic analyses
analyzed using lc
6 – 2
proteomic profiling showed
performed proteomic characterization
pooled colony samples
assess genetic variability
major venom component
total melittin intensity
distinguishable melittin isoforms
apis mellifera </
proteomic scale
proteome samples
genetic variations
venom glands
secapin peptides
free quantification
eight distinct
crude venom
coordinated changes
coding sequences
bioactive secretion
bee venom
abundance proteins
>- glycosylation
4 %)
Bee venom is a complex, bioactive secretion with the
composition
and molecular diversity varying across honeybee subspecies and ecotypes,
which influence both the function of the venom and the potential for
apitherapy. In this study, we performed proteomic characterization
of <i>Apis mellifera</i> bee venom from eight distinct,
pooled colony samples. Proteome samples from crude venom were analyzed
using LC-MS/MS, and multivariate bioinformatic analyses were performed
using label-free quantification. In parallel, melittin-coding sequences
were amplified from the venom glands and sequenced to assess genetic
variability. Proteomic profiling showed that melittin was the major
venom component at all locations, whereas observed differences among
the colony pools arose mainly from coordinated changes in moderately
and low-abundance proteins, such as PLA2, apamin, secapin peptides,
and hyaluronidase. Targeted analysis demonstrated the presence of
trace but reproducible <i>O</i>-glycosylation in melittin.
Quantitative analyses revealed that <i>O</i>-glycosylated
melittin accounted for a small but variable portion (∼0.6–2.4%)
of the total melittin intensity, and that single HexNAc modifications
predominated across regions. Targeted melittin cDNA sequencing analysis
of the melittin gene revealed position-specific amino acid polymorphisms
within and among the sampled colony pools; however, these genetic
variations were not reflected as distinguishable melittin isoforms
on a proteomic scale.
2026-09-28T00:00:00Z
Dataset
Dataset
10.1021/acs.jproteome.6c00015.s002
https://figshare.com/articles/dataset/Proteomic_Analysis_Reveals_Trace_O_Glycosylation_Signatures_of_Honeybee_Venom_Melittin/34010799
CC BY-NC 4.0