The research, funded by the Biotechnology and Biological Sciences Research Council (BBSRC), is an important tool in the search for new therapies to combat bacteria, such as streptococcus, that cause serious human infections.
Traditional methods of producing antibodies for research are slow and laborious and pose a significant bottleneck to proteomics research as they can take months of effort. This research offers a potential solution that could produce antibodies in just weeks, according to the BBSRC.
Antibodies are vital tools for the study of proteins because they can bind specifically to a protein of interest and enable researchers to identify, count and track the protein in vitro and in vivo, providing valuable insights into protein targets for vaccine development, the raw materials for bioprocessing or use as biomarkers.
The researchers, from Imperial College London at Hammersmith Hospital, discovered that a large proportion of antibodies created in response to synthetic peptide immunisation bind to the end of a peptide known as the C-terminus. The unique way that it is presented means that the antibodies will only bind to proteins that contain a precise sequence in their C-terminus.
Dr Rob Edwards, the research leader at Imperial College London, said: "The fact that the antibodies only bind to proteins with the specific sequence in their C-terminus means they are incredibly specific. We started looking at antibodies raised against simple peptide chains comprising just 5 amino acid residues and found that every one these bound only to the target protein."
"New research in proteomics has already identified thousands of proteins that may be important," he continued, "but we need to be able to study them at a higher rate than we can currently."
The new method is a simple way of creating libraries of specifically binding antibodies to aid in such studies. The team has already used it to produce antibodies against a group of bacterial proteins in just a few weeks, something that would have taken several years with traditional methods.
Dr Edwards is proving the effectiveness of the new technique through an existing collaboration with Dr Shiranee Sriskandan at Imperial College London to characterise novel proteins produced by Streptococcus pyogenes.
By creating specific antibodies to S pyogenes virulence factors the scientists hope to take the first steps towards developing drugs and vaccines against the organism, which can cause scarlet fever and rheumatic fever. While docile strains cause relatively harmless infections such as strep throat, the more virulent strains can trigger toxic shock syndrome, and attack muscle (the notorious 'flesh-eating bug' organism).