Proteome and phosphoproteome of Africanized and European honeybee venoms


Autoria(s): Resende, Virgínia Maria Ferreira; Vasilj, Andrej; Santos, Keity Souza; Palma, Mario Sergio; Shevchenko, Andrej
Contribuinte(s)

Universidade Estadual Paulista (UNESP)

Data(s)

27/05/2014

27/05/2014

01/09/2013

Resumo

Honey bee venom toxins trigger immunological, physiological, and neurological responses within victims. The high occurrence of bee attacks involving potentially fatal toxic and allergic reactions in humans and the prospect of developing novel pharmaceuticals make honey bee venom an attractive target for proteomic studies. Using label-free quantification, we compared the proteome and phosphoproteome of the venom of Africanized honeybees with that of two European subspecies, namely Apis mellifera ligustica and A. m. carnica. From the total of 51 proteins, 42 were common to all three subspecies. Remarkably, the toxins melittin and icarapin were phosphorylated. In all venoms, icarapin was phosphorylated at the 205Ser residue, which is located in close proximity to its known antigenic site. Melittin, the major toxin of honeybee venoms, was phosphorylated in all venoms at the 10Thr and 18Ser residues. 18Ser phosphorylated melittin-the major of its two phosphorylated forms-was less toxic compared to the native peptide. © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Formato

2638-2648

Identificador

http://dx.doi.org/10.1002/pmic.201300038

Proteomics, v. 13, n. 17, p. 2638-2648, 2013.

1615-9853

1615-9861

http://hdl.handle.net/11449/76373

10.1002/pmic.201300038

WOS:000327009000014

2-s2.0-84883308269

Idioma(s)

eng

Relação

Proteomics

Direitos

closedAccess

Palavras-Chave #Animal proteomics #Apis mellifera #Honeybee venom #LC-MS/MS #Melittin #Phosphorylation #amino acid #bee venom #icarapin #melittin #phosphoprotein #phosphoproteome #proteome #serine #unclassified drug #Africa #amino acid substitution #Europe #honeybee #insect #liquid chromatography #mass spectrometry #nonhuman #peptide analysis #priority journal #protein analysis #protein database #protein phosphorylation #proteomics #quantitative analysis #species comparison #toxin analysis
Tipo

info:eu-repo/semantics/article