Robert Flower*

 

Address 44 Musk Avenue,
Australian Red Cross Blood Service
Kelvin Grove, QLD, Australia

 

Transfusion safety, encompassing both prevention of transfusion reactions and minimising risk of Haemolytic Disease of the Newborn, depends on reliable procedures to detect antibodies to a range of clinically important red blood cell antigens. Genetic exchanges between adjacent homologous genes have resulted in hybrid glycophorins of the MNS system with development of complex profiles of neoantigens. Some of these hybrids are found in East Asian populations, but are rare in Caucasians. Three approaches were developed to investigate peptide mimetics of these antigens. The first approach was capture of biotinylated peptide mimetics of several antigens found on hybrid glycophorins on streptavidin-coated ELISA plates. In sera that reacted with an intact hybrid glycophorin on red blood cells, in an antiglobulin test, antibodies reacting by peptide-ELISA with at least one of the MNS peptide epitopes were detected in 43% (64/150) of sera. The second approach was affinity chromatography on linear peptides representing these epitopes found on hybrid glycophorins. Purified antibodies of unique single specificities that agglutinated only red cells with the complementary antigen were recovered. The third approach was utilising a lipid with a linker and peptide mimetic (KODE technology1). For the antibodies that reacted with a specific epitope by peptide ELISA there was 75-100% concordance between peptide ELISA and serological testing with Kodecytes and for various antigens. In some cases antibodies to hybrid glycophorins react with identical peptides but react quite differently with RBC displaying different hybrids. The investigations reported do not resolve the structural complexity of the sequence when presented in the intact glycophorin molecule. In conclusion, several techniques were utilised to demonstrate that peptide mimetics successfully represent red cell antigens but the specific problems related to the different antigenic structure of identical peptide sequences in different molecules remain elusive.

 

Heathcote D., Carrol T., Wang JJ, Flower R, Rodionov I Tuzikov A Bovine N and Henry S Transfusion 2010 50, 635-641. Novel antibody screening cells, MUT+Mur kodecytes, created by attaching peptides onto red blood cells.

 

Biographic Details

Name Professor Robert Flower

Title: National Leader R&D

Australian Red Cross Blood Service, Australia

Phone: +61738389020Fax: +61738389428  E-mail: rflower@redcrossblood.org.au

Research interests: Professor Robert Flower’s research interests include emerging transfusion-transmitted infections and strategies for providing an evidence base for modeling transfusion associated risk, improvement in transfusion practice as well as research into the molecular basis of blood groups found in non-Caucasian ethnic groups in the Australian population

 

Venue

Room: 
Hawken N201