Linked Life Data

7513555

Source:http://linkedlifedata.com/resource/pubmed/id/7513555

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
1994-6-8
pubmed:abstractText
The binding site of monoclonal antibody Se155-4, which has been the object of successful crystallographic and antibody-engineering studies, is shown by solid-phase immunoassays to be complementary to a branched trisaccharide, alpha-D-Galp(1-->2) [alpha-D-Abep(1-->3)]-alpha-D-Manp(1, rather than to the tetrasaccharide repeating unit alpha-D-Galp(1-->2) [alpha-D-Abep(1-->3)]-alpha-D-Manp(1-->4) alpha-L-Rhap(1- of the bacterial antigen. Specificity for the 3,6-dideoxy-D-xylo-hexose (3,6-dideoxy-D-galactose) epitope present in Salmonella paratyphi B O-antigens was ensured by screening hybridoma experiments with glycoconjugates derived from synthetic oligosaccharides. Detailed epitope mapping of the molecular recognition by modified and monodeoxy oligosaccharide derivatives showed that complementary surfaces and three antibody-saccharide hydrogen bonds are essential for full binding activity. Both hydroxyl groups of the 3,6-dideoxy-D-galactose residue were obligatory for binding and consistent with the directional nature of their involvement in carbohydrate-protein hydrogen bonds; related tetrasaccharides built from the isomeric 3,6-dideoxyhexoses, 3,6-dideoxy-D-glucose, paratose, and 3,6-dideoxy-D-mannose, tyvelose were not bound by the antibody. Titration microcalorimetry measurements were consistent with the hydrogen-bonding map inferred from the crystal structure and suggest that the displacement of water molecules from the binding site accounts for the favorable entropy that accompanies binding of the native trisaccharide determinant. The protein sequences determined for the antibody VL and VH domains reveal somatic mutation of the VL germ line gene, implying that this antibody-binding site results from a mature antibody response.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
33
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5172-82
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:7513555-Amino Acid Sequence, pubmed-meshheading:7513555-Animals, pubmed-meshheading:7513555-Antibodies, Monoclonal, pubmed-meshheading:7513555-Binding Sites, Antibody, pubmed-meshheading:7513555-Calorimetry, pubmed-meshheading:7513555-Carbohydrate Conformation, pubmed-meshheading:7513555-Carbohydrate Sequence, pubmed-meshheading:7513555-Epitopes, pubmed-meshheading:7513555-Immunoglobulin Heavy Chains, pubmed-meshheading:7513555-Immunoglobulin Light Chains, pubmed-meshheading:7513555-Immunoglobulin Variable Region, pubmed-meshheading:7513555-Kinetics, pubmed-meshheading:7513555-Lipopolysaccharides, pubmed-meshheading:7513555-Mice, pubmed-meshheading:7513555-Mice, Inbred BALB C, pubmed-meshheading:7513555-Molecular Sequence Data, pubmed-meshheading:7513555-Salmonella, pubmed-meshheading:7513555-Salmonella paratyphi A, pubmed-meshheading:7513555-Salmonella typhi, pubmed-meshheading:7513555-Sequence Homology, Amino Acid, pubmed-meshheading:7513555-Trisaccharides
pubmed:year
1994
pubmed:articleTitle
Molecular recognition of a Salmonella trisaccharide epitope by monoclonal antibody Se155-4.
pubmed:affiliation
Institute for Biological Sciences, National Research Council of Canada, Ottawa, Ontario.
pubmed:publicationType
Journal Article, Comparative Study