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62  structures 180  species 1  interaction 1250  sequences 8  architectures

Family: Bet_v_1 (PF00407)

Summary: Pathogenesis-related protein Bet v I family

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This is the Wikipedia entry entitled "Bet v I allergen". More...

Bet v I allergen Edit Wikipedia article

Bet v I allergen
1bv1.png
Birch Pollen Allergen Bet V 1 PDB 1bv1[1]
Identifiers
Symbol Bet_v_I
Pfam PF00407
InterPro IPR000916
PROSITE PDOC00437

Bet v I allergen is a family of protein allergens. 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.

Trees within the order Fagales possess particularly potent allergens, e.g. the prototypical Bet v1, the major white birch (Betula verrucosa) pollen antigen. Bet v 1 is the main cause of type I allergies observed in early spring. Type I, or immunoglobulin E-mediated (IgE-mediated) allergies affect 1 in 5 people in Europe and North America. Commonly observed symptoms are hay fever, dermatitis, asthma and, in severe cases, anaphylactic shock. First contact with these allergens results in sensitisation; subsequent contact produces a cross-linking reaction of IgE on mast cells and concomitant release of histamine. The inevitable symptoms of an allergic reaction ensue.

Categorization[edit]

A nomenclature system has been established for antigens (allergens) that cause IgE-mediated atopic allergies in humans.[2] 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: Bet v 1, Dau c 1, and Pru a 1. Other proteins belonging to this family include the major pollen allergens:

Structure[edit]

NMR analysis[3] has confirmed earlier predictions of the protein structure and site of the major T-cell epitope.[4] The Bet v 1 protein comprises 6 anti-parallel beta-strands and 3 alpha-helices. Four of the strands dominate the global fold, and 2 of the helices form a C-terminal amphipathic helical motif. This motif is believed to be the T-cell epitope.

The motif is also found in:

Additionally, the core domain of Bet v 1 founds or is part of a superfamily of domains called SRPBCC (START/RHOalphaC/PITP/Bet v1/CoxG/CalC) that include the StAR-related lipid-transfer (START) domain.

References[edit]

  1. ^ Gajhede, M.; Osmark, P.; Poulsen, F. M.; Ipsen, H.; Larsen, J. N.; Joost Van Neerven, R. J.; Schou, C.; Løwenstein, H.; Spangfort, M. D. (1996). "X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy". Nature structural biology 3 (12): 1040–1045. doi:10.1038/nsb1296-1040. PMID 8946858.  edit
  2. ^ [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)]
  3. ^ Rosch P, Kraft D, Faber C, Lindemann A, Sticht H, Ejchart A, Kungl A, Susani M, Frank RW, Breitenbach M (1996). "Secondary structure and tertiary fold of the birch pollen allergen Bet v 1 in solution". J. Biol. Chem. 271 (32): 19243–19250. doi:10.1074/jbc.271.32.19243. PMID 8702605. 
  4. ^ Kungl AJ, Kraft D, Lindemann A, Susani M, Breitenbach M, Scheiner O, Auer M, Machius M, Visser AJ (1996). "Evidence for an alpha helical T cell epitope in the C-terminus of the main birch pollen allergen Bet V 1". Biochem. Biophys. Res. Commun. 223 (1): 187–192. doi:10.1006/bbrc.1996.0867. PMID 8660368. 

This article incorporates text from the public domain Pfam and InterPro IPR000916

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Pathogenesis-related protein Bet v I family Provide feedback

This family is named after Bet v 1, the major birch pollen allergen. This protein belongs to family 10 of plant pathogenesis-related proteins (PR-10), cytoplasmic proteins of 15-17 kd that are wide-spread among dicotyledonous plants [1]. In recent years, a number of diverse plant proteins with low sequence similarity to Bet v 1 was identified. A classification by sequence similarity yielded several subfamilies related to PR-10 [2] - Pathogenesis-related proteins PR-10: These proteins were identified as major tree pollen allergens in birch and related species (hazel, alder), as plant food allergens expressed in high levels in fruits, vegetables and seeds (apple, celery, hazelnut), and as pathogenesis-related proteins whose expression is induced by pathogen infection, wounding, or abiotic stress. Hyp-1 (Q8H1L1), an enzyme involved in the synthesis of the bioactive naphthodianthrone hypericin in St. John's wort (Hypericum perforatum) also belongs to this family. Most of these proteins were found in dicotyledonous plants. In addition, related sequences were identified in monocots and conifers. - Cytokinin-specific binding proteins: These legume proteins bind cytokinin plant hormones [3]. - (S)-Norcoclaurine synthases are enzymes catalysing the condensation of dopamine and 4-hydroxyphenylacetaldehyde to (S)-norcoclaurine, the first committed step in the biosynthesis of benzylisoquinoline alkaloids such as morphine [4]. -Major latex proteins and ripening-related proteins are proteins of unknown biological function that were first discovered in the latex of opium poppy (Papaver somniferum) and later found to be upregulated during ripening of fruits such as strawberry and cucumber [5]. The occurrence of Bet v 1-related proteins is confined to seed plants with the exception of a cytokinin-binding protein from the moss Physcomitrella patens (Q9AXI3).

Literature references

  1. Wen J, Vanek-Krebitz M, Hoffmann-Sommergruber K, Scheiner O, Breiteneder H; , Mol Phylogenet Evol. 1997;8:317-333.: The potential of Betv1 homologues, a nuclear multigene family, as phylogenetic markers in flowering plants. PUBMED:9417891 EPMC:9417891

  2. Radauer C, Lackner P, Breiteneder H; , BMC Evol Biol. 2008;8:286.: The Bet v 1 fold: an ancient, versatile scaffold for binding of large, hydrophobic ligands. PUBMED:18922149 EPMC:18922149

  3. Fujimoto Y, Nagata R, Fukasawa H, Yano K, Azuma M, Iida A, Sugimoto S, Shudo K, Hashimoto Y; , Eur J Biochem. 1998;258:794-802.: Purification and cDNA cloning of cytokinin-specific binding protein from mung bean (Vigna radiata). PUBMED:9874249 EPMC:9874249

  4. Samanani N, Liscombe DK, Facchini PJ; , Plant J. 2004;40:302-313.: Molecular cloning and characterization of norcoclaurine synthase, an enzyme catalyzing the first committed step in benzylisoquinoline alkaloid biosynthesis. PUBMED:15447655 EPMC:15447655

  5. Samanani N, Liscombe DK, Facchini PJ; , Plant J. 2004;40:302-313.: Molecular cloning and characterization of norcoclaurine synthase, an enzyme catalyzing the first committed step in benzylisoquinoline alkaloid biosynthesis. PUBMED:15447655 EPMC:15447655


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000916

This domain is named after Bet v 1, the major birch pollen allergen. Bet v 1 belongs to family 10 of plant pathogenesis-related proteins (PR-10), cytoplasmic proteins of 15-17 kd that are wide-spread among dicotyledonous plants [PUBMED:9417891]. In recent years, a number of diverse plant proteins with low sequence similarity to Bet v 1 was identified. A classification by sequence similarity yielded several subfamilies related to PR-10 [PUBMED:18922149]:

  • Pathogenesis-related proteins PR-10: These proteins were identified as major tree pollen allergens in birch and related species (hazel, alder), as plant food allergens expressed in high levels in fruits, vegetables and seeds (apple, celery, hazelnut), and as pathogenesis-related proteins whose expression is induced by pathogen infection, wounding, or abiotic stress. Hyp-1 (SWISSPROT), an enzyme involved in the synthesis of the bioactive naphthodianthrone hypericin in St. John's wort (Hypericum perforatum) also belongs to this family. Most of these proteins were found in dicotyledonous plants. In addition, related sequences were identified in monocots and conifers.
  • Cytokinin-specific binding proteins: These legume proteins bind cytokinin plant hormones [PUBMED:9874249].
  • (S)-Norcoclaurine synthases are enzymes catalysing the condensation of dopamine and 4-hydroxyphenylacetaldehyde to (S)-norcoclaurine, the first committed step in the biosynthesis of benzylisoquinoline alkaloids such as morphine [PUBMED:15447655].
  • Major latex proteins and ripening-related proteins are proteins of unknown biological function that were first discovered in the latex of opium poppy (Papaver somniferum) and later found to be upregulated during ripening of fruits such as strawberry and cucumber [PUBMED:15447655].
The occurrence of Bet v 1-related proteins is confined to seed plants with the exception of a cytokinin-binding protein from the moss Physcomitrella patens (SWISSPROT).

Gene Ontology

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Domain organisation

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Alignments

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(34)
Full
(1250)
Representative proteomes NCBI
(1394)
Meta
(4)
RP15
(47)
RP35
(183)
RP55
(242)
RP75
(290)
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  Seed
(34)
Full
(1250)
Representative proteomes NCBI
(1394)
Meta
(4)
RP15
(47)
RP35
(183)
RP55
(242)
RP75
(290)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

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Curation and family details

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Curation View help on the curation process

Seed source: Prosite
Previous IDs: Bet_v_I;
Type: Domain
Author: Finn RD, Radauer C
Number in seed: 34
Number in full: 1250
Average length of the domain: 142.70 aa
Average identity of full alignment: 32 %
Average coverage of the sequence by the domain: 95.24 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.8 20.8
Trusted cut-off 20.8 20.9
Noise cut-off 20.6 20.6
Model length: 151
Family (HMM) version: 14
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Species distribution

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Interactions

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Bet_v_1

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Bet_v_1 domain has been found. There are 62 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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