Api m 6: A new bee venom allergen

Kettner, Alexander; Hughes, Graham J.; Frutiger, Séverine; Astori, Mireille; Roggero, Mario A.; Spertini, François; Corradin, Giampietro

doi:10.1067/mai.2001.113867

Cited by 61 publications

(46 citation statements)

References 36 publications

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“…A very low intensity peak (S/N 1.7) at m/z 6919.3 also revealed the presence of isoform 8 -71 ( Figure S5, Supplemental Material). It is important to bear in mind that Api m 6 is not reported to be subjected to any modification upon venom inoculation and interaction with the tissue [20]; this is confirmed by the observation that most of the above species were present in the crude venom extract (Scheme 1).…”

Section: Maldi Msi Analysis Of Envenomed Tissuesmentioning

confidence: 69%

“…The isoforms, Api m 6.02 and 6.04 exhibit an extra two amino acids at the carboxy-terminus (leucine and proline, not necessarily in this order) so that their molecular weights are 7389.9 (5-73), and 7798.3 Da (1-73). respectively [20]. Reasons for the presence of these isoforms have been described by Perein and collaborators.…”

mentioning

confidence: 83%

“…This property would be responsible for skeletal muscle, heart, and blood vessel contraction as well as nerve depolarization, with the latter macroscopically translating into the intense pain caused by the sting. Api m 6 was isolated and fully characterized for the first time in 2001 by Kettner and coworkers [20], who found it to bind to IgE antibodies in greater than 40% to 42% of bee venom hypersensitive patients, thus making it a minor allergen [20,21]. Api m 6 accounts for 1% to 2% of the crude venom, with four isoforms in equimolar amounts and with the same allergenicity [20].…”

mentioning

confidence: 99%

“…Api m 6 was isolated and fully characterized for the first time in 2001 by Kettner and coworkers [20], who found it to bind to IgE antibodies in greater than 40% to 42% of bee venom hypersensitive patients, thus making it a minor allergen [20,21]. Api m 6 accounts for 1% to 2% of the crude venom, with four isoforms in equimolar amounts and with the same allergenicity [20]. The four isoforms, named Api m 6.01 to Api m 6.04, share a common central amino acid sequence of 67 residues and differ only in their amino and carboxyterminus by up to 6 amino acids.…”

mentioning

confidence: 99%

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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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Section: Maldi Msi Analysis Of Envenomed Tissuesmentioning

confidence: 69%

mentioning

confidence: 83%

mentioning

confidence: 99%

mentioning

confidence: 99%

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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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“…Some 420 protein allergens and 190 isoforms had been classified, as of December 2002. This may represent only a small fraction of the total as individual allergens may have many isoforms (10,11). Furthermore, while this certified list contains many characterized allergens, it is not exhaustive as unlisted allergens can be found in the literature.…”

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confidence: 99%

Allergen databases

Brusic

Millot

Petrovsky

et al. 2003

Allergy

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Allergies represent a significant medical and industrial problem. Molecular and clinical data on allergens are growing exponentially and in this article we have reviewed nine specialized allergen databases and identified data sources related to protein allergens contained in general purpose molecular databases. An analysis of allergens contained in public databases indicates a high level of redundancy of entries and a relatively low coverage of allergens by individual databases. From this analysis we identify current database needs for allergy research and, in particular, highlight the need for a centralized reference allergen database.

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Biomedical Research with Honey Bees

Elekonich

Sourcebook of Models for Biomedical Research

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Api m 6: A new bee venom allergen

Cited by 61 publications

References 36 publications

Detection of honeybee venom in envenomed tissues by direct MALDI MSI

Detection of honeybee venom in envenomed tissues by direct MALDI MSI

Allergen databases

Biomedical Research with Honey Bees

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