Immunoreactive proteins of Bifidobacterium longum ssp. longum CCM 7952 and Bifidobacterium longum ssp. longum CCDM 372 identified by gnotobiotic mono-colonized mice sera, immune rabbit sera and nonimmune human sera.
The Bifidobacteria show great diversity in the cell surface architecture which may influence the physicochemical properties of the bacterial cell and strain specific properties. The immunomodulatory role of bifidobacteria has been extensively studied, however studies on the immunoreactivity of their...
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| Format: | Article |
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Frontiers Media S.A.
2016-09-01
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| Series: | Frontiers in Microbiology |
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| Online Access: | http://journal.frontiersin.org/Journal/10.3389/fmicb.2016.01537/full |
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| author | Sabina Górska Ewa Dylus Angelika Rudawska Ewa Brzozowska Dagmar Srutkova Martin Schwarzer Agnieszka Razim Hana Kozakova Andrzej Gamian |
| author_facet | Sabina Górska Ewa Dylus Angelika Rudawska Ewa Brzozowska Dagmar Srutkova Martin Schwarzer Agnieszka Razim Hana Kozakova Andrzej Gamian |
| author_sort | Sabina Górska |
| collection | DOAJ |
| description | The Bifidobacteria show great diversity in the cell surface architecture which may influence the physicochemical properties of the bacterial cell and strain specific properties. The immunomodulatory role of bifidobacteria has been extensively studied, however studies on the immunoreactivity of their protein molecules are very limited. Here, we compared six different methods of protein isolation and purification and we report identification of immunogenic and immunoreactive protein of two human Bifidobacterium longum ssp. longum strains. We evaluated potential immunoreactive properties of proteins employing polyclonal sera obtained from germ free mouse, rabbit and human. The protein yield was isolation method-dependent and the reactivity of proteins detected by SDS-PAGE and Western blotting was heterogeneous and varied between different serum samples. The proteins with the highest immunoreactivity were isolated, purified and have them sequenced. Among the immunoreactive proteins we identified enolase, aspartokinase, pyruvate kinase, DnaK (B. longum ssp. longum CCM 7952) and sugar ABC transporter ATP-binding protein, phosphoglycerate kinase, peptidoglycan synthethase penicillin-binding protein 3, transaldolase, ribosomal proteins and glyceraldehyde 3-phosphate dehydrogenase (B. longum ssp. longum CCDM 372). |
| first_indexed | 2024-12-19T05:21:48Z |
| format | Article |
| id | doaj.art-3e2e2b6a603446f38927b66e8f90d92e |
| institution | Directory Open Access Journal |
| issn | 1664-302X |
| language | English |
| last_indexed | 2024-12-19T05:21:48Z |
| publishDate | 2016-09-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Microbiology |
| spelling | doaj.art-3e2e2b6a603446f38927b66e8f90d92e2022-12-21T20:34:28ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2016-09-01710.3389/fmicb.2016.01537206844Immunoreactive proteins of Bifidobacterium longum ssp. longum CCM 7952 and Bifidobacterium longum ssp. longum CCDM 372 identified by gnotobiotic mono-colonized mice sera, immune rabbit sera and nonimmune human sera.Sabina Górska0Ewa Dylus1Angelika Rudawska2Ewa Brzozowska3Dagmar Srutkova4Martin Schwarzer5Agnieszka Razim6Hana Kozakova7Andrzej Gamian8Institute of Immunology and Experimantal Therapy, Polish Academy of SciencesInstitute of Immunology and Experimantal Therapy, Polish Academy of SciencesInstitute of Immunology and Experimantal Therapy, Polish Academy of SciencesInstitute of Immunology and Experimantal Therapy, Polish Academy of SciencesLaboratory of Gnotobiology, Institute of Microbiology, Academy of Sciences of the Czech Republic v. v. i.Laboratory of Gnotobiology, Institute of Microbiology, Academy of Sciences of the Czech Republic v. v. i.Institute of Immunology and Experimantal Therapy, Polish Academy of SciencesLaboratory of Gnotobiology, Institute of Microbiology, Academy of Sciences of the Czech Republic v. v. i.Institute of Immunology and Experimantal Therapy, Polish Academy of SciencesThe Bifidobacteria show great diversity in the cell surface architecture which may influence the physicochemical properties of the bacterial cell and strain specific properties. The immunomodulatory role of bifidobacteria has been extensively studied, however studies on the immunoreactivity of their protein molecules are very limited. Here, we compared six different methods of protein isolation and purification and we report identification of immunogenic and immunoreactive protein of two human Bifidobacterium longum ssp. longum strains. We evaluated potential immunoreactive properties of proteins employing polyclonal sera obtained from germ free mouse, rabbit and human. The protein yield was isolation method-dependent and the reactivity of proteins detected by SDS-PAGE and Western blotting was heterogeneous and varied between different serum samples. The proteins with the highest immunoreactivity were isolated, purified and have them sequenced. Among the immunoreactive proteins we identified enolase, aspartokinase, pyruvate kinase, DnaK (B. longum ssp. longum CCM 7952) and sugar ABC transporter ATP-binding protein, phosphoglycerate kinase, peptidoglycan synthethase penicillin-binding protein 3, transaldolase, ribosomal proteins and glyceraldehyde 3-phosphate dehydrogenase (B. longum ssp. longum CCDM 372).http://journal.frontiersin.org/Journal/10.3389/fmicb.2016.01537/fullBifidobacteriumProbioticsMoonlighting ProteinsImmunoreactivitySurface proteins |
| spellingShingle | Sabina Górska Ewa Dylus Angelika Rudawska Ewa Brzozowska Dagmar Srutkova Martin Schwarzer Agnieszka Razim Hana Kozakova Andrzej Gamian Immunoreactive proteins of Bifidobacterium longum ssp. longum CCM 7952 and Bifidobacterium longum ssp. longum CCDM 372 identified by gnotobiotic mono-colonized mice sera, immune rabbit sera and nonimmune human sera. Frontiers in Microbiology Bifidobacterium Probiotics Moonlighting Proteins Immunoreactivity Surface proteins |
| title | Immunoreactive proteins of Bifidobacterium longum ssp. longum CCM 7952 and Bifidobacterium longum ssp. longum CCDM 372 identified by gnotobiotic mono-colonized mice sera, immune rabbit sera and nonimmune human sera. |
| title_full | Immunoreactive proteins of Bifidobacterium longum ssp. longum CCM 7952 and Bifidobacterium longum ssp. longum CCDM 372 identified by gnotobiotic mono-colonized mice sera, immune rabbit sera and nonimmune human sera. |
| title_fullStr | Immunoreactive proteins of Bifidobacterium longum ssp. longum CCM 7952 and Bifidobacterium longum ssp. longum CCDM 372 identified by gnotobiotic mono-colonized mice sera, immune rabbit sera and nonimmune human sera. |
| title_full_unstemmed | Immunoreactive proteins of Bifidobacterium longum ssp. longum CCM 7952 and Bifidobacterium longum ssp. longum CCDM 372 identified by gnotobiotic mono-colonized mice sera, immune rabbit sera and nonimmune human sera. |
| title_short | Immunoreactive proteins of Bifidobacterium longum ssp. longum CCM 7952 and Bifidobacterium longum ssp. longum CCDM 372 identified by gnotobiotic mono-colonized mice sera, immune rabbit sera and nonimmune human sera. |
| title_sort | immunoreactive proteins of bifidobacterium longum ssp longum ccm 7952 and bifidobacterium longum ssp longum ccdm 372 identified by gnotobiotic mono colonized mice sera immune rabbit sera and nonimmune human sera |
| topic | Bifidobacterium Probiotics Moonlighting Proteins Immunoreactivity Surface proteins |
| url | http://journal.frontiersin.org/Journal/10.3389/fmicb.2016.01537/full |
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