Summary: Pathogenesis-related protein Bet v 1 family
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This is the Wikipedia entry entitled "Bet v I allergen". More...
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Bet v I allergen Edit Wikipedia article
|Bet v I allergen|
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 v 1, 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.
A nomenclature system has been established for antigens (allergens) that cause IgE-mediated atopic allergies in humans. 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:
- Aln g I from Alnus glutinosa (Alder);
- Api G I from Apium graveolens (Celery);
- Car b I from Carpinus betulus (European hornbeam);
- Cor a I from Corylus avellana (European hazel);
- Mal d I from Malus domestica (Apple).
NMR analysis has confirmed earlier predictions of the protein structure and site of the major T-cell epitope. 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. However, one very striking feature of the three-dimensional structure of Bet v 1 is the presence of a large hydrophobic cavity, which is open to the exterior and probably functions as a ligand binding site.
The motif is also found in:
- the wound-induced protein AoPR1 from Asparagus officinalis (Garden asparagus);
- the pathogenesis-related proteins from Phaseolus vulgaris (Kidney bean) and Petroselinum crispum (Parsley) (PR1-1 and PR1-3);
- the disease resistance response proteins, STH-2 and STH-21, from Solanum tuberosum (Potato) and pI49, pI176 and DRRG49-C from Pisum sativum (Garden pea);
- the P.sativum abscisic acid-responsive proteins ABR17 and ABR18;
- and the stress-induced protein SAM22 from Glycine max (Soybean).
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.
The biological function of Bet v 1 is still under investigations. Bet v 1 harbors a large hydrophobic pocket and is able to bind a large spectra of ligands in it like hormones and siderophores like flavenols. It belongs to the pathogenesis-related (PR) proteins, which are usually expressed upon infections and stressful conditions, implicating a role in host defense. In vitro, Bet v 1 has been shown to be immune-suppressive, when its pocket was filled by a ligand, but was able to mount a Th2-response important in allergy development, when the pocket remained empty.
- Gajhede, M.; Osmark, P.; Poulsen, F. M.; Ipsen, H.; Larsen, J. N.; Joost Van Neerven, R. J.; Schou, C.; LÃ¸wenstein, 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): 1040â€“1045. doi:10.1038/nsb1296-1040. PMID 8946858.
- [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)]
- 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): 19243â€“19250. doi:10.1074/jbc.271.32.19243. PMID 8702605.
- 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): 187â€“192. doi:10.1006/bbrc.1996.0867. PMID 8660368.
- Radauer, Christian; Lackner, Peter; Breiteneder, Heimo (2008-10-15). "The Bet v 1 fold: an ancient, versatile scaffold for binding of large, hydrophobic ligands". BMC Evolutionary Biology. 8 (1): 286. doi:10.1186/1471-2148-8-286. PMC 2577659. PMID 18922149.
- Mogensen, Jesper E.; Wimmer, Reinhard; Larsen, JÃ¸rgen N.; Spangfort, Michael D.; Otzen, Daniel E. (2002-04-12). "The major birch allergen, Bet v 1, shows affinity for a broad spectrum of physiological ligands". Journal of Biological Chemistry. 277 (26): 23684â€“92. doi:10.1074/jbc.M202065200. ISSN 0021-9258. PMID 11953433.
- Loon, L. C. van; Rep, M.; Pieterse, C. M. J. (2006-01-01). "Significance of Inducible Defense-related Proteins in Infected Plants". Annual Review of Phytopathology. 44 (1): 135â€“162. doi:10.1146/annurev.phyto.44.070505.143425. hdl:1874/27847. PMID 16602946.
- Roth-Walter, Franziska; Gomez-Casado, Cristina; Pacios, Luis F.; Mothes-Luksch, Nadine; Roth, Georg A.; Singer, Josef; Diaz-Perales, Araceli; Jensen-Jarolim, Erika (2014-06-20). "Bet v 1 from Birch Pollen Is a Lipocalin-like Protein Acting as Allergen Only When Devoid of Iron by Promoting Th2 Lymphocytes". Journal of Biological Chemistry. 289 (25): 17416â€“17421. doi:10.1074/jbc.M114.567875. ISSN 0021-9258. PMC 4067174. PMID 24798325.
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Pathogenesis-related protein Bet v 1 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 . 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  - 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 . - (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 . -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 . 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).
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
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
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
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
Internal database links
|Similarity to PfamA using HHSearch:||Polyketide_cyc2|
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 mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Biological process||defense response (GO:0006952)|
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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The Pfam:PF00407 entry is composed of sequences related to the major Birch (Betula verrucose) pollen antigen Bet v 1. This allergen is known to cause hayfever, dermatitis, asthma and occasionally anaphylactic shock. The other families in this clan share the same structure as Bet v 1, which is composed of antiparallel beta sheets and alpha helices. There is a cavity between the beta sheet and a long C terminal helix. The cavity appears to play roles in the binding of lipid molecules  which seems a common feature of the families in this clan.
The clan contains the following 21 members:AHSA1 Aromatic_hydrox Bet_v_1 COXG DAPG_hydrolase DUF1857 DUF2505 DUF3074 DUF3211 DUF3284 Fungal_KA1 IP_trans Lipoprotein_18 PaO Polyketide_cyc Polyketide_cyc2 PRELI Ring_hydroxyl_A START VanA_C VASt
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
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|Author:||Finn RD , Radauer C|
|Number in seed:||18|
|Number in full:||3709|
|Average length of the domain:||139.90 aa|
|Average identity of full alignment:||23 %|
|Average coverage of the sequence by the domain:||93.02 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||20|
|Download:||download the raw HMM for this family|
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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the More....
This chart is a modified "sunburst" visualisation of the species tree for this family. It shows each node in the tree as a separate arc, arranged radially with the superkingdoms at the centre and the species arrayed around the outermost ring.
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Unmapped species names
The tree is built by looking at each sequence in the full alignment for the family. We take the name of the species given by UniProt and try to map that to the full taxonomic tree from NCBI. In some cases, the name chosen by UniProt does not map to any node in the NCBI tree, perhaps because the chosen name is listed as a synonym or a misspelling in the NCBI taxonomy.
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Since we reduce the species tree to only the eight main taxonomic levels, sequences that are mapped to the sub-species level in the tree would not normally be shown. Rather than leave out these species, we map them instead to their parent species. So, for example, for sequences belonging to one of the Vibrio cholerae sub-species in the NCBI taxonomy, we show them instead as belonging to the species Vibrio cholerae.
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The tree shows the occurrence of this domain across different species. More...
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For all of the domain matches in a full alignment, we count the number that are found on all sequences in the alignment. This total is shown in the purple box.
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Finally, we group sequences from the same organism according to the NCBI code that is assigned by UniProt, allowing us to count the number of distinct sequences on which the domain is found. This value is shown in the pink boxes.
We use the NCBI species tree to group organisms according to their taxonomy and this forms the structure of the displayed tree. Note that in some cases the trees are too large (have too many nodes) to allow us to build an interactive tree, but in most cases you can still view the tree in a plain text, non-interactive representation. Those species which are represented in the seed alignment for this domain are highlighted.
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There are 2 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 200 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 sequence.
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