Marc Torrent, Ph.D., Medical Research Council, Laboratory of Molecular Biology, has been honored as a recipient of a 2013 ICAAC Young Investigator Award. Torrent is being recognized for his outstanding research, which includes developing the first algorithm to predict antimicrobial regions in proteins. Luis Rivas, Centro de Investigaciones Biolgicas(CSIC), said, "we are now applying this algorithm to interrogate full genomes in order to define new antimicrobial peptide leads with very appealing results."
Torrent obtained his Ph.D. from the Biochemistry and Molecular Biology Department at the Universitat Autnoma de Barcelona. During this time, he was interested in understanding the mechanism of action of antimicrobial proteins, particularly human ribonucleases. He was fascinated by the ability of a particular protein (RNase 3) to agglutinate gram-negative bacteria. His investigations revealed that RNase 3 was able to aggregate on the external layers of these pathogens in an amyloid-like manner. Failure to aggregate would cause the loss of agglutination. This was the first report of amyloid-like aggregates pursuing a defense function. During his time as a Ph.D. student at the Universitat Autnoma de Barcelona, Torrent worked under Ester Boix's supervision. She said Torrent, "has an outstanding capacity to work independently and develop new methodologies, contributing to our project with brilliant ideas."
After he completed his Ph.D., he worked as a postdoctoral researcher at the Universitat Pompeu Fabra where he expanded upon his interest in antimicrobial peptides by studying them from a chemical perspective. He directed his efforts to see whether antimicrobial proteins could be dissected in smaller peptides in order to be used as anti-infective drugs. He continued using ribonucleases as protein models and discovered that their antimicrobial properties were retained at specific domains that could be further dissected without losing activity. Later, he showed that these results could be generalized to include other proteins and developed computational tools to identify antimicrobial domains. These studies revealed, once more, that aggregation properties could modulate the activity of antimicrobial peptides. Hence, he directed his efforts to understand whether antimicrobial peptides could be related to amyloid-prone proteins. Surprisingly, his results suggested that antimicrobial peptides might have arisen during evolution after cationization of amyloid-prone sequences.
Presently, Torrent is a Marie Curie fellow at the Medical Research Council, Laboratory of Molecular Biology in Cambridge, England, where he is investigating the regulatory roles of tRNAs. These studies can help to understand, among other questions, how viruses manipulate tRNA populations to favor translation of their own proteins.
|Contact: Garth Hogan|
American Society for Microbiology