rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
Pt 7
|
pubmed:dateCreated |
2003-7-11
|
pubmed:abstractText |
Pathogenic bacteria in the family Neisseriaceae express surface receptors to acquire iron from the mammalian iron-binding proteins. Transferrins and lactoferrins constitute a family of iron-binding proteins highly related in both sequence and structure, yet the bacterial receptors are able to distinguish between these proteins and uphold a strict binding specificity. In order to understand the molecular basis for this specificity, the interaction between human lactoferrin (hLf) and the lactoferrin-binding protein A (LbpA) from Moraxella catarrhalis was studied. A periplasmic expression system was designed for the heterologous expression of LbpA, which enabled the investigation of its binding activity in the absence of lactoferrin-binding protein B (LbpB). To facilitate delineation of the LbpA-binding regions of hLf, chimeric proteins composed of hLf and bovine transferrin were made. Binding studies performed with the chimeric proteins and recombinant LbpA identified two binding regions within the C-terminus of hLf. Furthermore, native LbpA from Moraxella and Neisseria spp. bound the identical spectrum of hybrid proteins as the recombinant receptor, demonstrating a conserved binding interaction with the C-lobe of hLf.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Outer Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/LBPA protein, Neisseria meningitidis,
http://linkedlifedata.com/resource/pubmed/chemical/Lactoferrin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transferrin,
http://linkedlifedata.com/resource/pubmed/chemical/lactoferrin binding proteins...
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jul
|
pubmed:issn |
1350-0872
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
149
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1729-37
|
pubmed:dateRevised |
2011-11-17
|
pubmed:meshHeading |
pubmed-meshheading:12855724-Amino Acid Sequence,
pubmed-meshheading:12855724-Animals,
pubmed-meshheading:12855724-Bacterial Outer Membrane Proteins,
pubmed-meshheading:12855724-Bacterial Proteins,
pubmed-meshheading:12855724-Binding Sites,
pubmed-meshheading:12855724-Carrier Proteins,
pubmed-meshheading:12855724-Cattle,
pubmed-meshheading:12855724-Humans,
pubmed-meshheading:12855724-Lactoferrin,
pubmed-meshheading:12855724-Molecular Sequence Data,
pubmed-meshheading:12855724-Moraxella (Branhamella) catarrhalis,
pubmed-meshheading:12855724-Protein Structure, Tertiary,
pubmed-meshheading:12855724-Receptors, Cell Surface,
pubmed-meshheading:12855724-Recombinant Fusion Proteins,
pubmed-meshheading:12855724-Recombinant Proteins,
pubmed-meshheading:12855724-Sequence Homology, Amino Acid,
pubmed-meshheading:12855724-Transferrin
|
pubmed:year |
2003
|
pubmed:articleTitle |
Bacterial lactoferrin-binding protein A binds to both domains of the human lactoferrin C-lobe.
|
pubmed:affiliation |
Department of Microbiology and Infectious Diseases, Faculty of Medicine, University of Calgary, Rm 274, Heritage Medical Research Building, 3330 Hospital Drive NW, Calgary, Alberta, Canada T2N 4N1.
|
pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
|