Structure and Biology of Stinging Insect Venom Allergens

King, Te Piao; Spangfort, Michael D.

doi:10.1159/000024440

Cited by 208 publications

(145 citation statements)

References 42 publications

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“…The CAP family is related to venom allergens in social wasps and ants (Hoffman, 1993;King and Spangfort, 2000) and to antifungal proteins in plants (Stintzi et al, 1993;Szyperski et al, 1998). Members of this protein family are found in the SG of many bloodsucking insects and ticks (Francischetti et al, 2002;Li et al, 2001;Valenzuela et al, 2002b).…”

Section: Ag5 Familymentioning

confidence: 99%

An insight into the sialotranscriptome of the non-blood feeding Toxorhynchites amboinensis mosquito

Calvo

Pham

Ribeiro

2008

Insect Biochemistry and Molecular Biology

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All adult mosquitoes take sugar meals, and most adult females also take blood meals to develop eggs. Salivary glands (SG) of males are thus much smaller and do not contain many of the antihemostatic and antiinflammatory compounds found in females. In the past 5 years, transcriptome analyses have identified nearly 70 different genes expressed in adult female SG. For most of these, no function can be assigned in either blood or sugar feeding. Exceptionally, Toxorhynchites mosquitoes are unusual in that they never feed on blood, and the SG of adults are identical in both sexes. Transcriptome analysis of the adult SG of this mosquito was performed to increase knowledge of the evolution of blood feeding-and to identify polypeptide families associated with sugar feeding-in mosquitoes.

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Section: Ag5 Familymentioning

confidence: 99%

An insight into the sialotranscriptome of the non-blood feeding Toxorhynchites amboinensis mosquito

Calvo

Pham

Ribeiro

2008

Insect Biochemistry and Molecular Biology

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“…Api m 1 is the most common allergen detected by specific IgE (sIgE) determination, regardless of the method used [4][5][6]. Api m 2 is a cross-reactivity marker [7], while Api m 4 is a 2.84-kDa peptide that is found in abundance in venom [8] but has been associated with low allergenicity [4]. The combined use of these 3 components, which make up the bulk of the dry weight of venom, was found to increase diagnostic performance by 15% compared with the use of rApi m 1 alone [9].…”

Section: Introductionmentioning

confidence: 99%

IgE-Api m 4 Is Useful for Identifying a Particular Phenotype of Bee Venom Allergy

Ruiz¹,

Serrano²,

Moreno‐Aguilar³

2016

J Investig Allergol Clin Immunol

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Background and Objective: Different clinical behaviors have been identified in patients allergic to bee venom. Compound-resolved diagnosis could be an appropriate tool for investigating these differences. The aims of this study were to analyze whether specific IgE to Api m 4 (sIgE-Api m 4) can identify a particular kind of bee venom allergy and to describe response to bee venom immunotherapy (bVIT). Methods: Prospective study of 31 patients allergic to bee venom who were assigned to phenotype group A (sIgE-Api m 4 <0.98 kU/L), treated with native aqueous (NA) extract, or phenotype group B (sIgE-Api m 4 ≥0.98 kU/L), treated with purified aqueous (PA) extract. Sex, age, cardiovascular risk, severity of preceding sting reaction, exposure to beekeeping, and immunological data (intradermal test, sIgE/ sIgG4-Apis-nApi m 1, and sIgE-rApi m 2-Api m 4 were analyzed. Systemic reactions (SRs) during bVIT build-up were analyzed. Immunological and sting challenge outcomes were evaluated in each group after 1 and 2 years of bVIT. Results: Phenotype B patients had more severe reactions (P=.049) and higher skin sensitivity (P=.011), baseline sIgE-Apis (P=.0004), sIgE-nApi m 1 (P=.0004), and sIgG4-Apis (P=.027) than phenotype A patients. Furthermore, 41% of patients in group B experienced SRs during the build-up phase with NA; the sting challenge success rate in this group was 82%. There were no significant reductions in serial intradermal test results, but an intense reduction in sIgE-nApi m 1 (P=.013) and sIgE-Api m 4 (P=.004) was observed after the first year of bVIT. Conclusion: Use of IgE-Api m 4 as the only discrimination criterion demonstrated differences in bee venom allergy. Further investigation with larger populations is necessary.

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“…It was first reported by Shkenderov et al in 1973 [22] as an allergenic protein of ϳ39 kDa. It was then detected by other laboratories [23][24][25][26], and shown to contain a typical tryptic protease domain with a serine protease catalytic triad. Despite not being reported in the official allergen list, the newly discovered HBV Icarapin (MW 19.6 kDa) [9] is a glycoprotein worth mentioning along with the other allergens, as it has been cloned, expressed and found to bind IgE [10].…”

mentioning

confidence: 99%

“…So far, researchers studying HBV have concentrated their efforts on elucidating the properties of the aller-genic proteins and peptides [26,28,29], on their isolation and characterization [21], on VIT [30], and on the study of tissue damage from a physiological point of view [31]. The study, isolation and characterization of allergenic proteins and peptides are being performed using much more sophisticated analytical techniques including: gene cloning, mass spectrometry, X-ray and genomic techniques [21].…”

mentioning

confidence: 99%

Detection of honeybee venom in envenomed tissues by direct MALDI MSI

Francese

Lambardi

Mastrobuoni

et al. 2009

J. Am. Soc. Mass Spectrom.

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A new analytical approach using matrix-assisted laser desorption/ionization mass spectrometry imaging (MALDI MSI) for the study of honeybee venom is shown. In vitro and in vivo models simulating the bee sting have been developed using live honeybees and, as the envenomation sites, pig ears and rat legs; MALDI MSI has been used to map, over time, the diffusion and distribution of three venom allergens (Api m 1, Api m 4, and Api m 6) and two venom toxins (apamine and mast cell degranulating peptide). In conjunction with other classical biochemical techniques and high resolution mass spectrometry (HRMS), structural data have been obtained that contribute to current understanding of honeybee venom composition. Initial data have also been obtained demonstrating the feasibility of mapping the organism's response to the sting. The opportunity to monitor venom diffusion and the organism's response at the same time might open new pathways for in vivo preclinical studies in designing and testing new venom immunotherapy (VIT). (J Am Soc Mass Spectrom 2009, 20, 112-123)

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Structure and Biology of Stinging Insect Venom Allergens

Cited by 208 publications

References 42 publications

An insight into the sialotranscriptome of the non-blood feeding Toxorhynchites amboinensis mosquito

An insight into the sialotranscriptome of the non-blood feeding Toxorhynchites amboinensis mosquito

IgE-Api m 4 Is Useful for Identifying a Particular Phenotype of Bee Venom Allergy

Detection of honeybee venom in envenomed tissues by direct MALDI MSI

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