TY - JOUR
T1 - Characterization of the honeybee venom proteins C1q-like protein and PVF1 and their allergenic potential
AU - Russkamp, Dennis
AU - Van Vaerenbergh, Matthias
AU - Etzold, Stefanie
AU - Eberlein, Bernadette
AU - Darsow, Ulf
AU - Schiener, Maximilian
AU - De Smet, Lina
AU - Absmaier, Magdalena
AU - Biedermann, Tilo
AU - Spillner, Edzard
AU - Ollert, Markus
AU - Jakob, Thilo
AU - Schmidt-Weber, Carsten B.
AU - de Graaf, Dirk C.
AU - Blank, Simon
N1 - Publisher Copyright:
© 2018 Elsevier Ltd
PY - 2018/8
Y1 - 2018/8
N2 - Honeybee (Apis mellifera) venom (HBV) represents an ideal model to study the role of particular venom components in allergic reactions in sensitized individuals as well as in the eusociality of Hymenoptera species. The aim of this study was to further characterize the HBV components C1q-like protein (C1q) and PDGF/VEGF-like factor 1 (PVF1). C1q and PVF1 were produced as recombinant proteins in insect cells. Their allergenic properties were examined by determining the level of specific IgE antibodies in the sera of HBV-allergic patients (n = 26) as well as by their capacity to activate patients' basophils (n = 11). Moreover, the transcript heterogeneity of PVF1 was analyzed. It could be demonstrated that at least three PVF1 variants are present in the venom gland, which all result from alternative splicing of one transcript. Additionally, recombinant C1q and PVF1 from Spodoptera frugiperda insect cells exhibited specific IgE reactivity with approximately 38.5% of sera of HBV-allergic patients. Interestingly, both proteins were unable to activate basophils of the patients, questioning their role in the context of clinically relevant sensitization. Recombinant C1q and PVF1 can build the basis for a deeper understanding of the molecular mechanisms of Hymenoptera venoms. Moreover, the conflicting results between IgE sensitization and lack of basophil activation, might in the future contribute to the identification of factors that determine the allergenic potential of proteins.
AB - Honeybee (Apis mellifera) venom (HBV) represents an ideal model to study the role of particular venom components in allergic reactions in sensitized individuals as well as in the eusociality of Hymenoptera species. The aim of this study was to further characterize the HBV components C1q-like protein (C1q) and PDGF/VEGF-like factor 1 (PVF1). C1q and PVF1 were produced as recombinant proteins in insect cells. Their allergenic properties were examined by determining the level of specific IgE antibodies in the sera of HBV-allergic patients (n = 26) as well as by their capacity to activate patients' basophils (n = 11). Moreover, the transcript heterogeneity of PVF1 was analyzed. It could be demonstrated that at least three PVF1 variants are present in the venom gland, which all result from alternative splicing of one transcript. Additionally, recombinant C1q and PVF1 from Spodoptera frugiperda insect cells exhibited specific IgE reactivity with approximately 38.5% of sera of HBV-allergic patients. Interestingly, both proteins were unable to activate basophils of the patients, questioning their role in the context of clinically relevant sensitization. Recombinant C1q and PVF1 can build the basis for a deeper understanding of the molecular mechanisms of Hymenoptera venoms. Moreover, the conflicting results between IgE sensitization and lack of basophil activation, might in the future contribute to the identification of factors that determine the allergenic potential of proteins.
KW - C1q-like protein
KW - Honeybee venom
KW - Hymenoptera venom allergy
KW - PDGF/VEGF-like factors 1
KW - PVF1
KW - Venom allergen
UR - http://www.scopus.com/inward/record.url?scp=85048507815&partnerID=8YFLogxK
U2 - 10.1016/j.toxicon.2018.05.017
DO - 10.1016/j.toxicon.2018.05.017
M3 - Article
C2 - 29842867
AN - SCOPUS:85048507815
SN - 0041-0101
VL - 150
SP - 198
EP - 206
JO - Toxicon
JF - Toxicon
ER -