Linked Life Data

19828202

Source:http://linkedlifedata.com/resource/pubmed/id/19828202

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2-3
pubmed:dateCreated
2009-11-30
pubmed:abstractText
Antibody-carbohydrate interactions play central roles in stimulating adverse immune reactions. The most familiar example of such a process is the reaction observed in ABO-incompatible blood transfusion and organ transplantation. The ABO blood groups are defined by the presence of specific carbohydrates expressed on the surface of red blood cells. Preformed antibodies in the incompatible recipient (i.e., different blood groups) recognize cells exhibiting host-incompatible ABO system antigens and proceed to initiate lysis of the incompatible cells. Pig-to-human xenotransplantation presents a similar immunological barrier. Antibodies present in humans recognize carbohydrate antigens on the surface of pig organs as foreign and proceed to initiate hyperacute xenograft rejection. The major carbohydrate xenoantigens all bear terminal Gal alpha(1,3)Gal epitopes (or alphaGal). In this study, we have developed and validated a site mapping technique to investigate protein-ligand recognition and applied it to antibody-carbohydrate systems. This site mapping technique involves the use of molecular docking to generate a series of antibody-carbohydrate complexes, followed by analysis of the hydrogen bonding and van der Waals interactions occurring in each complex. The technique was validated by application to a series of antibody-carbohydrate crystal structures. In each case, the majority of interactions made in the crystal structure complex were able to be reproduced. The technique was then applied to investigate xenoantigen recognition by a panel of monoclonal anti-alphaGal antibodies. The results indicate that there is a significant overlap of the antibody regions engaging the xenoantigens across the panel. Likewise, similar regions of the xenoantigens interact with the antibodies.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1872-9142
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
47
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
233-46
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:19828202-Amino Acid Sequence, pubmed-meshheading:19828202-Animals, pubmed-meshheading:19828202-Antibodies, Heterophile, pubmed-meshheading:19828202-Antibodies, Monoclonal, pubmed-meshheading:19828202-Binding Sites, Antibody, pubmed-meshheading:19828202-Carbohydrate Conformation, pubmed-meshheading:19828202-Carbohydrate Sequence, pubmed-meshheading:19828202-Carbohydrates, pubmed-meshheading:19828202-Complementarity Determining Regions, pubmed-meshheading:19828202-Computational Biology, pubmed-meshheading:19828202-Crystallography, X-Ray, pubmed-meshheading:19828202-Galactose, pubmed-meshheading:19828202-Humans, pubmed-meshheading:19828202-Hydrogen Bonding, pubmed-meshheading:19828202-Models, Molecular, pubmed-meshheading:19828202-Molecular Sequence Data, pubmed-meshheading:19828202-Reproducibility of Results, pubmed-meshheading:19828202-Sequence Alignment, pubmed-meshheading:19828202-Sus scrofa
pubmed:year
2009
pubmed:articleTitle
In silico analysis of antibody-carbohydrate interactions and its application to xenoreactive antibodies.
pubmed:affiliation
Medicinal Chemistry and Drug Action, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, VIC 3052, Australia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't