TY  - JOUR
AU  - Lukić, Jovanka
AU  - Chen, Vivien
AU  - Strahinić, Ivana
AU  - Begović, Jelena
AU  - Lev-Tov, Hadar
AU  - Davis, Stephen C.
AU  - Tomić-Canić, Marjana
AU  - Pastar, Irena
PY  - 2017
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1042
AB  - Probiotics are beneficial microorganisms, known to exert numerous positive effects on human health, primarily in the battle against pathogens. Probiotics have been associated with improved healing of intestinal ulcers, and healing of infected cutaneous wounds. This article reviews the latest findings on probiotics related to their pro-healing properties on gut epithelium and skin. Proven mechanisms by which probiotic bacteria exert their beneficial effects include direct killing of pathogens, competitive displacement of pathogenic bacteria, reinforcement of epithelial barrier, induction of fibroblasts, and epithelial cells' migration and function. Beneficial immunomodulatory effects of probiotics relate to modulation and activation of intraepithelial lymphocytes, natural killer cells, and macrophages through induced production of cytokines. Systemic effects of beneficial bacteria and link between gut microbiota, immune system, and cutaneous health through gut-brain-skin axes are discussed as well. In light of growing antibiotic resistance of pathogens, antibiotic use is becoming less effective in treating cutaneous and systemic infections. This review points to a new perspective and therapeutic potential of beneficial probiotic species as a safe alternative approach for treatment of patients affected by wound healing disorders and cutaneous infections.
PB  - Wiley, Hoboken
T2  - Wound Repair and Regeneration
T1  - Probiotics or pro-healers: the role of beneficial bacteria in tissue repair
EP  - 922
IS  - 6
SP  - 912
VL  - 25
DO  - 10.1111/wrr.12607
ER  - 

@article{
author = "Lukić, Jovanka and Chen, Vivien and Strahinić, Ivana and Begović, Jelena and Lev-Tov, Hadar and Davis, Stephen C. and Tomić-Canić, Marjana and Pastar, Irena",
year = "2017",
abstract = "Probiotics are beneficial microorganisms, known to exert numerous positive effects on human health, primarily in the battle against pathogens. Probiotics have been associated with improved healing of intestinal ulcers, and healing of infected cutaneous wounds. This article reviews the latest findings on probiotics related to their pro-healing properties on gut epithelium and skin. Proven mechanisms by which probiotic bacteria exert their beneficial effects include direct killing of pathogens, competitive displacement of pathogenic bacteria, reinforcement of epithelial barrier, induction of fibroblasts, and epithelial cells' migration and function. Beneficial immunomodulatory effects of probiotics relate to modulation and activation of intraepithelial lymphocytes, natural killer cells, and macrophages through induced production of cytokines. Systemic effects of beneficial bacteria and link between gut microbiota, immune system, and cutaneous health through gut-brain-skin axes are discussed as well. In light of growing antibiotic resistance of pathogens, antibiotic use is becoming less effective in treating cutaneous and systemic infections. This review points to a new perspective and therapeutic potential of beneficial probiotic species as a safe alternative approach for treatment of patients affected by wound healing disorders and cutaneous infections.",
publisher = "Wiley, Hoboken",
journal = "Wound Repair and Regeneration",
title = "Probiotics or pro-healers: the role of beneficial bacteria in tissue repair",
pages = "922-912",
number = "6",
volume = "25",
doi = "10.1111/wrr.12607"
}

Lukić, J., Chen, V., Strahinić, I., Begović, J., Lev-Tov, H., Davis, S. C., Tomić-Canić, M.,& Pastar, I.. (2017). Probiotics or pro-healers: the role of beneficial bacteria in tissue repair. in Wound Repair and Regeneration
Wiley, Hoboken., 25(6), 912-922.
https://doi.org/10.1111/wrr.12607

Lukić J, Chen V, Strahinić I, Begović J, Lev-Tov H, Davis SC, Tomić-Canić M, Pastar I. Probiotics or pro-healers: the role of beneficial bacteria in tissue repair. in Wound Repair and Regeneration. 2017;25(6):912-922.
doi:10.1111/wrr.12607 .

Lukić, Jovanka, Chen, Vivien, Strahinić, Ivana, Begović, Jelena, Lev-Tov, Hadar, Davis, Stephen C., Tomić-Canić, Marjana, Pastar, Irena, "Probiotics or pro-healers: the role of beneficial bacteria in tissue repair" in Wound Repair and Regeneration, 25, no. 6 (2017):912-922,
https://doi.org/10.1111/wrr.12607 . .

TY  - JOUR
AU  - Pastar, I.
AU  - Begović, Jelena
AU  - Lozo, Jelena
AU  - Topisirović, Ljubiša
AU  - Golić, Nataša
PY  - 2007
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/281
AB  - The prtP-prtM intergenic region of Lactobacillus paracasei subsp. paracasei BGHN14 was cloned and sequenced. The nucleotide sequence of the prtP-prtM intergenic region in BGHN14, containing divergently orientated P-prtP and P-prtM promoters, was shorter by 35 bp in comparison with that in lactococci. The nucleotide sequence involved in casitone-dependent transcriptional regulation of the lactococcal prt genes was not found in the BGHN14. The activity of P-prtM in L. lactis NZ9000 was very low and insignificantly changed in the presence of casitone, whereas P-prtP was completely inactive. When L. casei ATCC393(T) was used as host, both P-prtP and P-prtM were active and strongly regulated by casitone. The results strongly indicate that the mechanisms of the casitone-dependent regulation of the prt genes in BGHN14 and lactococci are different.
PB  - Springer, Dordrecht
T2  - Folia Microbiologica
T1  - Casitone-dependent transcriptional regulation of the prtP and prtM genes in the natural isolate Lactobacillus paracasei subsp paracasei
EP  - 584
IS  - 6
SP  - 577
VL  - 52
DO  - 10.1007/BF02932186
ER  - 

@article{
author = "Pastar, I. and Begović, Jelena and Lozo, Jelena and Topisirović, Ljubiša and Golić, Nataša",
year = "2007",
abstract = "The prtP-prtM intergenic region of Lactobacillus paracasei subsp. paracasei BGHN14 was cloned and sequenced. The nucleotide sequence of the prtP-prtM intergenic region in BGHN14, containing divergently orientated P-prtP and P-prtM promoters, was shorter by 35 bp in comparison with that in lactococci. The nucleotide sequence involved in casitone-dependent transcriptional regulation of the lactococcal prt genes was not found in the BGHN14. The activity of P-prtM in L. lactis NZ9000 was very low and insignificantly changed in the presence of casitone, whereas P-prtP was completely inactive. When L. casei ATCC393(T) was used as host, both P-prtP and P-prtM were active and strongly regulated by casitone. The results strongly indicate that the mechanisms of the casitone-dependent regulation of the prt genes in BGHN14 and lactococci are different.",
publisher = "Springer, Dordrecht",
journal = "Folia Microbiologica",
title = "Casitone-dependent transcriptional regulation of the prtP and prtM genes in the natural isolate Lactobacillus paracasei subsp paracasei",
pages = "584-577",
number = "6",
volume = "52",
doi = "10.1007/BF02932186"
}

Pastar, I., Begović, J., Lozo, J., Topisirović, L.,& Golić, N.. (2007). Casitone-dependent transcriptional regulation of the prtP and prtM genes in the natural isolate Lactobacillus paracasei subsp paracasei. in Folia Microbiologica
Springer, Dordrecht., 52(6), 577-584.
https://doi.org/10.1007/BF02932186

Pastar I, Begović J, Lozo J, Topisirović L, Golić N. Casitone-dependent transcriptional regulation of the prtP and prtM genes in the natural isolate Lactobacillus paracasei subsp paracasei. in Folia Microbiologica. 2007;52(6):577-584.
doi:10.1007/BF02932186 .

Pastar, I., Begović, Jelena, Lozo, Jelena, Topisirović, Ljubiša, Golić, Nataša, "Casitone-dependent transcriptional regulation of the prtP and prtM genes in the natural isolate Lactobacillus paracasei subsp paracasei" in Folia Microbiologica, 52, no. 6 (2007):577-584,
https://doi.org/10.1007/BF02932186 . .

TY  - JOUR
AU  - Pastar, I.
AU  - Fira, Đorđe
AU  - Strahinić, Ivana
AU  - Krstić, Katarina
AU  - Begović, Jelena
AU  - Topisirović, Ljubiša
AU  - Jovanović, Goran
PY  - 2006
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/249
AB  - The region of the prtR gene coding for the active site of PrtR proteinase was detected in natural isolates of lactobacilli, previously determined as Lactobacillus rhamnosus. This region was present in all L. rhamnosus strains with proteolytic activity. The PCR primers used were constructed on the basis of the sequence of the catalytic domain of the prtR proteinase gene. These primers generated in colony-PCR procedure specific 611-bp product with DNA from natural isolates of L. rhamnosus. No PCR amplifications using these primers were obtained for closely related bacteria of genus Lactobacillus, regardless of their proteolytic activity. In addition, these primers could be used singly or in multiplex PCR together with the Lactobacillus genus-specific primers. Compared with the other proteinases within the genus Lactobacillus (PrtP, PrtB and PrtH) which retained the activity in cell-free proteinase extracts, PrtR proteinase showed proteolytic activity only under in vivo conditions (whole cells of the producing strains).
PB  - Springer, Dordrecht
T2  - Folia Microbiologica
T1  - Analysis of the presence of prtR proteinase gene in natural isolates of Lactobacillus rhamnosus
EP  - 540
IS  - 6
SP  - 535
VL  - 51
DO  - 10.1007/BF02931617
ER  - 

@article{
author = "Pastar, I. and Fira, Đorđe and Strahinić, Ivana and Krstić, Katarina and Begović, Jelena and Topisirović, Ljubiša and Jovanović, Goran",
year = "2006",
abstract = "The region of the prtR gene coding for the active site of PrtR proteinase was detected in natural isolates of lactobacilli, previously determined as Lactobacillus rhamnosus. This region was present in all L. rhamnosus strains with proteolytic activity. The PCR primers used were constructed on the basis of the sequence of the catalytic domain of the prtR proteinase gene. These primers generated in colony-PCR procedure specific 611-bp product with DNA from natural isolates of L. rhamnosus. No PCR amplifications using these primers were obtained for closely related bacteria of genus Lactobacillus, regardless of their proteolytic activity. In addition, these primers could be used singly or in multiplex PCR together with the Lactobacillus genus-specific primers. Compared with the other proteinases within the genus Lactobacillus (PrtP, PrtB and PrtH) which retained the activity in cell-free proteinase extracts, PrtR proteinase showed proteolytic activity only under in vivo conditions (whole cells of the producing strains).",
publisher = "Springer, Dordrecht",
journal = "Folia Microbiologica",
title = "Analysis of the presence of prtR proteinase gene in natural isolates of Lactobacillus rhamnosus",
pages = "540-535",
number = "6",
volume = "51",
doi = "10.1007/BF02931617"
}

Pastar, I., Fira, Đ., Strahinić, I., Krstić, K., Begović, J., Topisirović, L.,& Jovanović, G.. (2006). Analysis of the presence of prtR proteinase gene in natural isolates of Lactobacillus rhamnosus. in Folia Microbiologica
Springer, Dordrecht., 51(6), 535-540.
https://doi.org/10.1007/BF02931617

Pastar I, Fira Đ, Strahinić I, Krstić K, Begović J, Topisirović L, Jovanović G. Analysis of the presence of prtR proteinase gene in natural isolates of Lactobacillus rhamnosus. in Folia Microbiologica. 2006;51(6):535-540.
doi:10.1007/BF02931617 .

Pastar, I., Fira, Đorđe, Strahinić, Ivana, Krstić, Katarina, Begović, Jelena, Topisirović, Ljubiša, Jovanović, Goran, "Analysis of the presence of prtR proteinase gene in natural isolates of Lactobacillus rhamnosus" in Folia Microbiologica, 51, no. 6 (2006):535-540,
https://doi.org/10.1007/BF02931617 . .

TY  - JOUR
AU  - Pastar, I
AU  - Tonić, I
AU  - Golić, Nataša
AU  - Kojić, Milan
AU  - van Kranenburg, R
AU  - Kleerebezem, M
AU  - Topisirović, Ljubiša
AU  - Jovanović, Goran
PY  - 2003
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/172
AB  - A novel proteinase, PrtR, produced by the human vaginal isolate Lactobacillus rhamnosus strain BGT10 was identified and genetically characterized. The prtR gene and flanking regions were cloned and sequenced. The deduced amino acid sequence of PrtR shares characteristics that are common for other cell envelope proteinases (CEPs) characterized to date, but in contrast to the other cell surface subtilisin-like serine proteinases, it has a smaller and somewhat different B domain and lacks the helix domain, and the anchor domain has a rare sorting signal sequence. Furthermore, PrtR lacks the insert domain, which otherwise is situated inside the catalytic serine protease domain of all CEPs, and has a different cell wall spacer (W) domain similar to that of the cell surface antigen I and II polypeptides expressed by oral and vaginal streptococci. Moreover, the PrtR W domain exhibits significant sequence homology to the consensus sequence that has been shown to be the hallmark of human intestinal mucin protein. According to its alpha(S1)- and beta-casein cleavage efficacy, PrtR is an efficient proteinase at pH 6.5 and is distributed throughout all L. rhamnosus strains tested. Proteinase extracts of the BGT10 strain obtained with Ca2+-free buffer at pH 6.5 were proteolytically active. The prtR promoter-like sequence was determined, and the minimal promoter region was defined by use of prtR-gusA operon fusions. The prtR expression is Casitone dependent, emphasizing that nitrogen depletion elevates its transcription. This is in correlation with the catalytic activity of the PrtR proteinase.
PB  - Amer Soc Microbiology, Washington
T2  - Applied and Environmental Microbiology
T1  - Identification and genetic characterization of a novel proteinase, PrtR, from the human isolate Lactobacillus rhamnosus BGT10
EP  - 5811
IS  - 10
SP  - 5802
VL  - 69
DO  - 10.1128/AEM.69.10.5802-5811.2003
ER  - 

@article{
author = "Pastar, I and Tonić, I and Golić, Nataša and Kojić, Milan and van Kranenburg, R and Kleerebezem, M and Topisirović, Ljubiša and Jovanović, Goran",
year = "2003",
abstract = "A novel proteinase, PrtR, produced by the human vaginal isolate Lactobacillus rhamnosus strain BGT10 was identified and genetically characterized. The prtR gene and flanking regions were cloned and sequenced. The deduced amino acid sequence of PrtR shares characteristics that are common for other cell envelope proteinases (CEPs) characterized to date, but in contrast to the other cell surface subtilisin-like serine proteinases, it has a smaller and somewhat different B domain and lacks the helix domain, and the anchor domain has a rare sorting signal sequence. Furthermore, PrtR lacks the insert domain, which otherwise is situated inside the catalytic serine protease domain of all CEPs, and has a different cell wall spacer (W) domain similar to that of the cell surface antigen I and II polypeptides expressed by oral and vaginal streptococci. Moreover, the PrtR W domain exhibits significant sequence homology to the consensus sequence that has been shown to be the hallmark of human intestinal mucin protein. According to its alpha(S1)- and beta-casein cleavage efficacy, PrtR is an efficient proteinase at pH 6.5 and is distributed throughout all L. rhamnosus strains tested. Proteinase extracts of the BGT10 strain obtained with Ca2+-free buffer at pH 6.5 were proteolytically active. The prtR promoter-like sequence was determined, and the minimal promoter region was defined by use of prtR-gusA operon fusions. The prtR expression is Casitone dependent, emphasizing that nitrogen depletion elevates its transcription. This is in correlation with the catalytic activity of the PrtR proteinase.",
publisher = "Amer Soc Microbiology, Washington",
journal = "Applied and Environmental Microbiology",
title = "Identification and genetic characterization of a novel proteinase, PrtR, from the human isolate Lactobacillus rhamnosus BGT10",
pages = "5811-5802",
number = "10",
volume = "69",
doi = "10.1128/AEM.69.10.5802-5811.2003"
}

Pastar, I., Tonić, I., Golić, N., Kojić, M., van Kranenburg, R., Kleerebezem, M., Topisirović, L.,& Jovanović, G.. (2003). Identification and genetic characterization of a novel proteinase, PrtR, from the human isolate Lactobacillus rhamnosus BGT10. in Applied and Environmental Microbiology
Amer Soc Microbiology, Washington., 69(10), 5802-5811.
https://doi.org/10.1128/AEM.69.10.5802-5811.2003

Pastar I, Tonić I, Golić N, Kojić M, van Kranenburg R, Kleerebezem M, Topisirović L, Jovanović G. Identification and genetic characterization of a novel proteinase, PrtR, from the human isolate Lactobacillus rhamnosus BGT10. in Applied and Environmental Microbiology. 2003;69(10):5802-5811.
doi:10.1128/AEM.69.10.5802-5811.2003 .

Pastar, I, Tonić, I, Golić, Nataša, Kojić, Milan, van Kranenburg, R, Kleerebezem, M, Topisirović, Ljubiša, Jovanović, Goran, "Identification and genetic characterization of a novel proteinase, PrtR, from the human isolate Lactobacillus rhamnosus BGT10" in Applied and Environmental Microbiology, 69, no. 10 (2003):5802-5811,
https://doi.org/10.1128/AEM.69.10.5802-5811.2003 . .