Linked Life Data

17311414

Source:http://linkedlifedata.com/resource/pubmed/id/17311414

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2007-3-13
pubmed:abstractText
The 159 residue Bet v 1 is the major allergen from birch tree pollen. Its natural function is unknown although it is capable of binding several types of physiologically relevant ligands in a centrally placed cavity in the protein structure. Here we use circular dichroism and fluorescence spectroscopy to show that Bet v 1 binds to DOPC and DOPG phospholipid vesicles in a pH-dependent manner. Binding is facilitated by low pH, negatively charged phospholipids, and high vesicle curvature, indicating that electrostatic interactions and vesicle surface defects are important parameters for binding. Binding is accompanied by major structural rearrangements, involving an increase in alpha-helical structure and a decrease in beta-structure. A bilayer structure per se is not a prerequisite for these rearrangements, since they also occur in the presence of the micelle-forming lysophospholipids lysoMPC and lysoMPG. Two major bound states (A and B) with distinct secondary structure compositions were identified, which predominate in the pH ranges approximately 9.5-6.5 and approximately 5-2.5, respectively. Despite the high content of secondary structure, the A- and B-states are partially unfolded as they unfold noncooperatively in CD thermal scans, in contrast to the native state. In addition, the B-state (but not the A-state) shows intermediate proteolysis-resistance and is able to induce complete leakage of calcein from the vesicles, indicating that this state is partially inserted into and significantly perturbs the bilayer structure. We conclude that Bet v 1 is a membrane binding protein, highlighting a possible biological function of this protein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/1,2-oleoylphosphatidylcholine, http://linkedlifedata.com/resource/pubmed/chemical/Allergens, http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Plant, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Detergents, http://linkedlifedata.com/resource/pubmed/chemical/Glucosides, http://linkedlifedata.com/resource/pubmed/chemical/Liposomes, http://linkedlifedata.com/resource/pubmed/chemical/MALD1 protein, Malus domestica, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Micelles, http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylcholines, http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/STARD3 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Unilamellar Liposomes, http://linkedlifedata.com/resource/pubmed/chemical/dodecyl maltoside
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
46
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3356-65
pubmed:dateRevised
2011-6-21
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
The major allergen from birch tree pollen, Bet v 1, binds and permeabilizes membranes.
pubmed:affiliation
Centre for Insoluble Protein Structures (inSPIN) at Department of Life Sciences, Aalborg University, Sohngaardsholmsvej 49, DK-9000 Aalborg, Denmark.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't