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Engineering the PP7 Virus Capsid as a Peptide Display Platform.
Zhao L, Kopylov M, Potter CS, Carragher B, Finn MG. Zhao L, et al. ACS Nano. 2019 Apr 23;13(4):4443-4454. doi: 10.1021/acsnano.8b09683. Epub 2019 Mar 26. ACS Nano. 2019. PMID: 30912918 Free PMC article.
As self-assembling polyvalent nanoscale structures that can tolerate substantial genetic and chemical modification, virus-like particles are useful in a variety of fields. Here we describe the genetic modification and structural characterization of the Leviviridae PP7
As self-assembling polyvalent nanoscale structures that can tolerate substantial genetic and chemical modification, virus-like partic …
Immunogenic display of diverse peptides, including a broadly cross-type neutralizing human papillomavirus L2 epitope, on virus-like particles of the RNA bacteriophage PP7.
Caldeira Jdo C, Medford A, Kines RC, Lino CA, Schiller JT, Chackerian B, Peabody DS. Caldeira Jdo C, et al. Vaccine. 2010 Jun 17;28(27):4384-93. doi: 10.1016/j.vaccine.2010.04.049. Epub 2010 Apr 29. Vaccine. 2010. PMID: 20434554 Free PMC article.
Here we describe a highly versatile VLP platform for peptide display based on VLPs of the RNA bacteriophage PP7. We show that this platform can be used for the engineered display of specific peptide sequences as well as for …
Here we describe a highly versatile VLP platform for peptide display based on VLPs of the RNA bacteriophage PP7. …
Thermal stability of RNA phage virus-like particles displaying foreign peptides.
Caldeira JC, Peabody DS. Caldeira JC, et al. J Nanobiotechnology. 2011 May 24;9:22. doi: 10.1186/1477-3155-9-22. J Nanobiotechnology. 2011. PMID: 21609437 Free PMC article.
BACKGROUND: To be useful for genetic display of foreign peptides a viral coat protein must tolerate peptide insertions without major disruption of subunit folding and capsid assembly. ...RESULTS: Here we characterize the effects of peptide inser …
BACKGROUND: To be useful for genetic display of foreign peptides a viral coat protein must tolerate peptide insertions …