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Biophysical Characterization of the Type III Secretion Tip Proteins and the Tip Proteins Attached to Bacterium-Like Particles
- Source :
- Journal of Pharmaceutical Sciences. 104:424-432
- Publication Year :
- 2015
- Publisher :
- Elsevier BV, 2015.
-
Abstract
- Bacterium-like particles (BLPs), derived from Lactococcus lactis , offer a self-adjuvanting delivery vehicle for subunit protein vaccines. Proteins can be specifically loaded onto the BLPs via a peptidoglycan anchoring (PA) domain. In this study, the tip proteins IpaD, SipD, and LcrV belonging to type III secretion systems of Shigella flexneri, Salmonella enterica, and Yersinia enterocolitica , respectively, were fused to the PA and loaded onto the BLPs. Herein, we biophysically characterized these nine samples and condensed the spectroscopic results into three-index empirical phase diagrams (EPDs). The EPDs show distinctions between the IpaD/SipD and LcrV subfamilies of tip proteins, based on their physical stability, even upon addition of the PA. Upon attachment to the BLPs, the BLPs become defining moiety in the spectroscopic measurements, leaving the tip proteins to have a subtle yet modulating effect on the structural integrity of the tip proteins-BLPs binding. In summary, this work provides a comprehensive view of physical stability of the tip proteins and tip protein-BLPs and serves as a baseline for screening of excipients to increase the stability of the tip protein-BLPs for future vaccine formulation. © 2014 Wiley Periodicals, Inc. and the American Pharmacists Association J Pharm Sci 104:424-432, 2015
- Subjects :
- Circular dichroism
Protein subunit
Pharmaceutical Science
Article
Biophysical Phenomena
03 medical and health sciences
chemistry.chemical_compound
Shigella flexneri
Bacterial Proteins
LcrV
Secretion
Particle Size
Yersinia enterocolitica
Bacterial Secretion Systems
030304 developmental biology
0303 health sciences
biology
030306 microbiology
Chemistry
Lactococcus lactis
biology.organism_classification
Biochemistry
Vaccines, Subunit
Biophysics
Peptidoglycan
Subjects
Details
- ISSN :
- 00223549
- Volume :
- 104
- Database :
- OpenAIRE
- Journal :
- Journal of Pharmaceutical Sciences
- Accession number :
- edsair.doi.dedup.....193eb9cf3707d848b14ba567ca7bc65d