PR00807

AMBALLERGEN

PRINTS entry
Member databasePRINTS
PRINTS typefamily
Short nameAMBALLERGEN

Description
Imported from IPR018082

Pectate lyase
4.2.2.2
is an enzyme involved in the maceration and soft rotting of plant tissue. Pectate lyase is responsible for the eliminative cleavage of pectate, yielding oligosaccharides with 4-deoxy-alpha-D-mann-4-enuronosyl groups at their non-reducing ends. The protein is maximally expressed late in pollen development. It has been suggested that the pollen expression of pectate lyase genes might relate to a requirement for pectin degradation during pollen tube growth
[1]
.

Some of the proteins in this family are allergens
[4]
. Allergies are hypersensitivity reactions of the immune system to specific substances called allergens (such as pollen, stings, drugs, or food) that, in most people, result in no symptoms. A nomenclature system has been established for antigens (allergens) that cause IgE-mediated atopic allergies in humans [WHO/IUIS Allergen Nomenclature Subcommittee King T.P., Hoffmann D., Loewenstein H., Marsh D.G., Platts-Mills T.A.E., Thomas W. Bull. World Health Organ. 72:797-806(1994)]. This nomenclature system is defined by a designation that is composed of the first three letters of the genus; a space; the first letter of the species name; a space and an arabic number. In the event that two species names have identical designations, they are discriminated from one another by adding one or more letters (as necessary) to each species designation.

The allergens in this family include allergens with the following designations: Amb a 1, Amb a 2, Amb a 3, Cha o 1, Cup a 1, Cry j 1, Jun a 1.

Two of the major allergens in the pollen of short ragweed (Ambrosia artemisiifolia) are Amb aI and Amb aII. The primary structure of Amb aII has been deduced and has been shown to share ~65% sequence identity with the Amb alpha I multigene family of allergens
[3]
. Members of the Amb aI/aII family include Nicotiana tabacum (Common tobacco) pectate lyase, which is similar to the deduced amino acid sequences of two pollen-specific pectate lyase genes identified in Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
[2]
; Cry jI, a major allergenic glycoprotein of Cryptomeria japonica (Japanese cedar) - the most common pollen allergen in Japan
[5]
; and P56 and P59, which share sequence similarity with pectate lyases of plant pathogenic bacteria
[1]
.

References
Imported from IPR018082

1.Molecular and genetic characterization of two pollen-expressed genes that have sequence similarity to pectate lyases of the plant pathogen Erwinia. Wing RA, Yamaguchi J, Larabell SK, Ursin VM, McCormick S. Plant Mol. Biol. 14, 17-28, (1990). View articlePMID: 1983191

2.Isolation and characterization of a tobacco gene with homology to pectate lyase which is specifically expressed during microsporogenesis. Rogers HJ, Harvey A, Lonsdale DM. Plant Mol. Biol. 20, 493-502, (1992). View articlePMID: 1421152

3.Complete sequence of the allergen Amb alpha II. Recombinant expression and reactivity with T cells from ragweed allergic patients. Rogers BL, Morgenstern JP, Griffith IJ, Yu XB, Counsell CM, Brauer AW, King TP, Garman RD, Kuo MC. J. Immunol. 147, 2547-52, (1991). View articlePMID: 1717566

4.Pectate lyase pollen allergens: sensitization profiles and cross-reactivity pattern. Pichler U, Hauser M, Wolf M, Bernardi ML, Gadermaier G, Weiss R, Ebner C, Yokoi H, Takai T, Didierlaurent A, Rafaiani C, Briza P, Mari A, Behrendt H, Wallner M, Ferreira F. PLoS ONE 10, e0120038, (2015). View articlePMID: 25978036

5.Antigenicity of the oligosaccharide moiety of the Japanese cedar (Cryptomeria japonica) pollen allergen, Cry jI. Hijikata A, Matsumoto I, Kojima K, Ogawa H. Int. Arch. Allergy Immunol. 105, 198-202, (1994). PMID: 7920021

Supplementary References

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