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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
1994-5-4
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pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/L24465,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/L24466,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/L24467,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/L24468,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/L24469
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pubmed:abstractText |
We have purified and characterized the Amb p V allergen (A1 variant) from western ragweed (Ambrosia psilostachya) pollen. This allergen was found to be highly cross-reactive with the Amb a VA1 allergen from short ragweed (A. artemisiifolia) pollen in a competitive double-Ab radioimmunoassay (DARIA) and the two allergens showed concordant allergenic potency in histamine-release experiments. We cloned and sequenced several Amb p V genes from western ragweed pollen and flowers by direct PCR of genomic DNA. The amino acid sequences deduced from the nucleotide sequences indicated the presence of multiple forms of Amb p V that could be broadly classified into two groups: Amb p VA and Amb p VB variants. The sequences of the Amb p VA variants are highly homologous to Amb a V (about 90% identity) and very similar to the protein sequence that we obtained. The Amb p VB variants share approximately 65% amino acid homology with Amb a V and have five to seven cysteine residues as compared with the eight found in Amb a V and Amb t V. Two cysteine residues that form disulfide bonds in other Amb Vs (positions 19 and 43 in Amb a V) are replaced by serine and alanine in the Amb p VB1 and Amb p VB2 variants. We have generated model structures of Amb p VA1, VA2, VA3, and VB1 variants from the nuclear magnetic resonance-derived structure of Amb a VA1 by homology modeling. Comparison of antigenic epitopes predicted for the structures of Amb p V variants and Amb a VA1 explains the observed cross-reactivity of the two ragweed proteins and suggests the epitopes likely to be involved in Ab recognition.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0022-1767
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
|
pubmed:volume |
152
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2882-9
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:7511632-Allergens,
pubmed-meshheading:7511632-Amino Acid Sequence,
pubmed-meshheading:7511632-Antigens, Plant,
pubmed-meshheading:7511632-Base Sequence,
pubmed-meshheading:7511632-Basophils,
pubmed-meshheading:7511632-Cloning, Molecular,
pubmed-meshheading:7511632-Cross Reactions,
pubmed-meshheading:7511632-Histamine Release,
pubmed-meshheading:7511632-Humans,
pubmed-meshheading:7511632-Molecular Sequence Data,
pubmed-meshheading:7511632-Plant Proteins,
pubmed-meshheading:7511632-Pollen
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pubmed:year |
1994
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pubmed:articleTitle |
Immunologic and molecular characterization of Amb p V allergens from Ambrosia psilostachya (western Ragweed) pollen.
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pubmed:affiliation |
Johns Hopkins Asthma and Allergy Center, Johns Hopkins University School of Medicine, Baltimore, MD 21224.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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