Isolation, biochemical characterization and anti-bacterial activity of BPIFA2 protein
Samo za registrovane korisnike
2014
Autori
Prokopovic, VladimirPopović, Milica M.
Anđelković, Uroš
Marsavelski, Aleksandra
Rašković, Brankica
Gavrović-Jankulović, Marija
Polović, Natalija
Članak u časopisu (Objavljena verzija)
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
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. (C) 2013 Elsevier Ltd. All rights reserved.
Ključne reči:
Parotid secretory protein / BPIFA2 / Saliva / Bactericidal activityIzvor:
Archives of Oral Biology, 2014, 59, 3, 302-309Izdavač:
- Pergamon-Elsevier Science Ltd, Oxford
Finansiranje / projekti:
- Alergeni, antitela, enzimi i mali fiziološki značajni molekuli: dizajn, struktura, funkcija i značaj (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
Kolekcije
Institucija/grupa
Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Prokopovic, Vladimir AU - Popović, Milica M. AU - Anđelković, Uroš AU - Marsavelski, Aleksandra AU - Rašković, Brankica AU - Gavrović-Jankulović, Marija AU - Polović, Natalija PY - 2014 UR - https://cherry.chem.bg.ac.rs/handle/123456789/1520 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. (C) 2013 Elsevier Ltd. All rights reserved. PB - Pergamon-Elsevier Science Ltd, Oxford 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 M. and Anđelković, Uroš and Marsavelski, Aleksandra and Rašković, 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. (C) 2013 Elsevier Ltd. All rights reserved.", publisher = "Pergamon-Elsevier Science Ltd, Oxford", 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. M., Anđelković, U., Marsavelski, A., Rašković, B., Gavrović-Jankulović, M.,& Polović, N.. (2014). Isolation, biochemical characterization and anti-bacterial activity of BPIFA2 protein. in Archives of Oral Biology Pergamon-Elsevier Science Ltd, Oxford., 59(3), 302-309. https://doi.org/10.1016/j.archoralbio.2013.12.005
Prokopovic V, Popović MM, Anđelković U, Marsavelski A, Rašković 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 M., Anđelković, Uroš, Marsavelski, Aleksandra, Rašković, 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 . .