In 2018 George Smith from the University of Missouri was awarded the Nobel Prize in chemistry for the phage display of peptides and antibodies. As he mentioned in his Nobel Prize lecture, it was not the discovery but the observation and understanding of phage biology that led to the development of a new powerful methodology called phage library. In the method, the bacteriophage genome is utilized to inbuild a gene of interest that is later expressed on the surface of the virus. Large numbers of genes can be inserted into the genome of bacteriophages to form a phage library, where each bacteriophage presents a different peptide or protein on its surface. That, in turn, gives us a tool to isolate and characterize peptides and antibodies specific to any target of interest.
Today several biotechnological companies offer construction of a custom antibody phage library of certain species as well as screening services to isolate ligands of any target. At the same time improved technology of the development of phage antibody library from different species yields new discoveries and clues to unsolved disease in human. Cloning and manipulating metazoan adaptive IgG immune genes has resulted in the development of complex antibodies for diagnostic and therapeutic applications. Due to adaptive evolutionary differences in the structure of the IgG fold in some species, each of them has its own scaffold for use in synthetic biology. Apart from the interchangeable use of mouse and human IgG scaffolds for producing partially or entirely humanized recombinant monoclonal antibodies, sharks and camelids have provided distinctive variants on the mammalian IgG fold.
This Research Topic aims to demonstrate the overall results of use of the robust methodology of antibody and peptide phage display, from the time of its acknowledgment in 2018 until today. Particularly it presents the specific outcomes of this technology such as novel potential immunotherapeutics, distinctive structural features of antibodies in different species, characterization of peptide-peptide interactions.
Malgorzata Lisowska received her PhD in microbiology and immunology from the National University of Singapore. She works as a postdoctoral fellow and team leader at the International Centre for Cancer Vaccine Science, at University of Gdańsk, where in collaboration with the University of Edinburgh, she was involved in the development a canine antibody phage library and isolation of canine antibodies specific to canine proteins e.g. EGFR, PD1, CD20.
Keywords:
phage library, antibody library, peptide library, antibody discovery, phage-peptide
Important Note:
All contributions to this Research Topic must be within the scope of the section and journal to which they are submitted, as defined in their mission statements. Frontiers reserves the right to guide an out-of-scope manuscript to a more suitable section or journal at any stage of peer review.
In 2018 George Smith from the University of Missouri was awarded the Nobel Prize in chemistry for the phage display of peptides and antibodies. As he mentioned in his Nobel Prize lecture, it was not the discovery but the observation and understanding of phage biology that led to the development of a new powerful methodology called phage library. In the method, the bacteriophage genome is utilized to inbuild a gene of interest that is later expressed on the surface of the virus. Large numbers of genes can be inserted into the genome of bacteriophages to form a phage library, where each bacteriophage presents a different peptide or protein on its surface. That, in turn, gives us a tool to isolate and characterize peptides and antibodies specific to any target of interest.
Today several biotechnological companies offer construction of a custom antibody phage library of certain species as well as screening services to isolate ligands of any target. At the same time improved technology of the development of phage antibody library from different species yields new discoveries and clues to unsolved disease in human. Cloning and manipulating metazoan adaptive IgG immune genes has resulted in the development of complex antibodies for diagnostic and therapeutic applications. Due to adaptive evolutionary differences in the structure of the IgG fold in some species, each of them has its own scaffold for use in synthetic biology. Apart from the interchangeable use of mouse and human IgG scaffolds for producing partially or entirely humanized recombinant monoclonal antibodies, sharks and camelids have provided distinctive variants on the mammalian IgG fold.
This Research Topic aims to demonstrate the overall results of use of the robust methodology of antibody and peptide phage display, from the time of its acknowledgment in 2018 until today. Particularly it presents the specific outcomes of this technology such as novel potential immunotherapeutics, distinctive structural features of antibodies in different species, characterization of peptide-peptide interactions.
Malgorzata Lisowska received her PhD in microbiology and immunology from the National University of Singapore. She works as a postdoctoral fellow and team leader at the International Centre for Cancer Vaccine Science, at University of Gdańsk, where in collaboration with the University of Edinburgh, she was involved in the development a canine antibody phage library and isolation of canine antibodies specific to canine proteins e.g. EGFR, PD1, CD20.
Keywords:
phage library, antibody library, peptide library, antibody discovery, phage-peptide
Important Note:
All contributions to this Research Topic must be within the scope of the section and journal to which they are submitted, as defined in their mission statements. Frontiers reserves the right to guide an out-of-scope manuscript to a more suitable section or journal at any stage of peer review.