Isolation, biochemical characterization and anti-bacterial activity of BPIFA2 protein
Authorized Users Only
2014
Authors
Prokopovic, VladimirPopović, Milica
Anđelković, Uroš
Marsavelski, Aleksandra
Raskovic, Brankica
Gavrović-Jankulović, Marija
Polović, Natalija
Article (Published version)
Metadata
Show full item recordAbstract
Objective: Human BPIFA2 (parotid secretory protein) is a ubiquitous soluble salivary protein, which belongs to the PLUNC family of proteins. Having sequence similarity to bactericidal/permeability-increasing protein and lipopolysaccharide-binding protein, PLUNC proteins are probably involved in local antibacterial response at mucosal sites, such as oral cavity. The aim of the study was to isolate and characterize human BPIFA2. Design: In this paper, we report one-step affinity chromatography method for BPIFA2 purification from whole human saliva. The isolated BPIFA2 was identified by trypsin mass fingerprinting and characterized by electrophoretic methods. Antibacterial activity of BPIFA2 against model microorganism Pseudomonas aeruginosa was shown in minimum inhibitory concentration and time kill study assays. Results: The protein showed microheterogeneity, both in molecular weight and pI value. BPIFA2 inhibited the growth of P. aeruginosa in microgram concentration range determined b...y minimum inhibitory concentration assay. In the time kill study, 32 mu g/mL BPIFA2 showed clear bactericidal activity and did not cause any aggregation of bacteria. Conclusion: Affinity chromatography is well suited for isolation of functional BPIFA2 with a potent bactericidal activity against P. aeruginosa.
Keywords:
Parotid secretory protein / BPIFA2 / Saliva / Bactericidal activitySource:
Archives of Oral Biology, 2014, 59, 3, 302-309Publisher:
- Oxford : Pergamon-Elsevier Science Ltd
Funding / projects:
- Allergens, antibodies, enzymes and small physiologically important molecules: design, structure, function and relevance (RS-MESTD-Basic Research (BR or ON)-172049)
DOI: 10.1016/j.archoralbio.2013.12.005
ISSN: 0003-9969
PubMed: 24581853
WoS: 000333489600010
Scopus: 2-s2.0-84891760970
Collections
Institution/Community
IHTMTY - JOUR AU - Prokopovic, Vladimir AU - Popović, Milica AU - Anđelković, Uroš AU - Marsavelski, Aleksandra AU - Raskovic, Brankica AU - Gavrović-Jankulović, Marija AU - Polović, Natalija PY - 2014 UR - https://cer.ihtm.bg.ac.rs/handle/123456789/1508 AB - Objective: Human BPIFA2 (parotid secretory protein) is a ubiquitous soluble salivary protein, which belongs to the PLUNC family of proteins. Having sequence similarity to bactericidal/permeability-increasing protein and lipopolysaccharide-binding protein, PLUNC proteins are probably involved in local antibacterial response at mucosal sites, such as oral cavity. The aim of the study was to isolate and characterize human BPIFA2. Design: In this paper, we report one-step affinity chromatography method for BPIFA2 purification from whole human saliva. The isolated BPIFA2 was identified by trypsin mass fingerprinting and characterized by electrophoretic methods. Antibacterial activity of BPIFA2 against model microorganism Pseudomonas aeruginosa was shown in minimum inhibitory concentration and time kill study assays. Results: The protein showed microheterogeneity, both in molecular weight and pI value. BPIFA2 inhibited the growth of P. aeruginosa in microgram concentration range determined by minimum inhibitory concentration assay. In the time kill study, 32 mu g/mL BPIFA2 showed clear bactericidal activity and did not cause any aggregation of bacteria. Conclusion: Affinity chromatography is well suited for isolation of functional BPIFA2 with a potent bactericidal activity against P. aeruginosa. PB - Oxford : Pergamon-Elsevier Science Ltd T2 - Archives of Oral Biology T1 - Isolation, biochemical characterization and anti-bacterial activity of BPIFA2 protein VL - 59 IS - 3 SP - 302 EP - 309 DO - 10.1016/j.archoralbio.2013.12.005 ER -
@article{ author = "Prokopovic, Vladimir and Popović, Milica and Anđelković, Uroš and Marsavelski, Aleksandra and Raskovic, Brankica and Gavrović-Jankulović, Marija and Polović, Natalija", year = "2014", abstract = "Objective: Human BPIFA2 (parotid secretory protein) is a ubiquitous soluble salivary protein, which belongs to the PLUNC family of proteins. Having sequence similarity to bactericidal/permeability-increasing protein and lipopolysaccharide-binding protein, PLUNC proteins are probably involved in local antibacterial response at mucosal sites, such as oral cavity. The aim of the study was to isolate and characterize human BPIFA2. Design: In this paper, we report one-step affinity chromatography method for BPIFA2 purification from whole human saliva. The isolated BPIFA2 was identified by trypsin mass fingerprinting and characterized by electrophoretic methods. Antibacterial activity of BPIFA2 against model microorganism Pseudomonas aeruginosa was shown in minimum inhibitory concentration and time kill study assays. Results: The protein showed microheterogeneity, both in molecular weight and pI value. BPIFA2 inhibited the growth of P. aeruginosa in microgram concentration range determined by minimum inhibitory concentration assay. In the time kill study, 32 mu g/mL BPIFA2 showed clear bactericidal activity and did not cause any aggregation of bacteria. Conclusion: Affinity chromatography is well suited for isolation of functional BPIFA2 with a potent bactericidal activity against P. aeruginosa.", publisher = "Oxford : Pergamon-Elsevier Science Ltd", journal = "Archives of Oral Biology", title = "Isolation, biochemical characterization and anti-bacterial activity of BPIFA2 protein", volume = "59", number = "3", pages = "302-309", doi = "10.1016/j.archoralbio.2013.12.005" }
Prokopovic, V., Popović, M., Anđelković, U., Marsavelski, A., Raskovic, B., Gavrović-Jankulović, M.,& Polović, N.. (2014). Isolation, biochemical characterization and anti-bacterial activity of BPIFA2 protein. in Archives of Oral Biology Oxford : Pergamon-Elsevier Science Ltd., 59(3), 302-309. https://doi.org/10.1016/j.archoralbio.2013.12.005
Prokopovic V, Popović M, Anđelković U, Marsavelski A, Raskovic B, Gavrović-Jankulović M, Polović N. Isolation, biochemical characterization and anti-bacterial activity of BPIFA2 protein. in Archives of Oral Biology. 2014;59(3):302-309. doi:10.1016/j.archoralbio.2013.12.005 .
Prokopovic, Vladimir, Popović, Milica, Anđelković, Uroš, Marsavelski, Aleksandra, Raskovic, Brankica, Gavrović-Jankulović, Marija, Polović, Natalija, "Isolation, biochemical characterization and anti-bacterial activity of BPIFA2 protein" in Archives of Oral Biology, 59, no. 3 (2014):302-309, https://doi.org/10.1016/j.archoralbio.2013.12.005 . .