T4 Phage Tail Adhesin Gp12 Counteracts LPS-induced Inflammation In Vivo
Bacteriophages that infect Gram-negative bacteria often bind to the bacterial surface by interaction of specific proteins with lipopolysaccharide (LPS). Short tail fiber proteins (tail adhesin, gp12) mediate adsorption of T4-like bacteriophages to Escherichia coli, binding surface proteins or LPS. P...
| Main Authors: | , , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2016-07-01
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| Series: | Frontiers in Microbiology |
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| Online Access: | http://journal.frontiersin.org/Journal/10.3389/fmicb.2016.01112/full |
| _version_ | 1818547579897511936 |
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| author | Paulina Miernikiewicz Anna Klopot Ryszard Soluch Piotr Szkuta Weronika Keska Katarzyna Hodyra-Stefaniak Agnieszka Konopka Marcin Nowak Dorota Lecion Zuzanna Kazmierczak Joanna Majewska Marek Harhala Andrzej Gorski Krystyna Dabrowska |
| author_facet | Paulina Miernikiewicz Anna Klopot Ryszard Soluch Piotr Szkuta Weronika Keska Katarzyna Hodyra-Stefaniak Agnieszka Konopka Marcin Nowak Dorota Lecion Zuzanna Kazmierczak Joanna Majewska Marek Harhala Andrzej Gorski Krystyna Dabrowska |
| author_sort | Paulina Miernikiewicz |
| collection | DOAJ |
| description | Bacteriophages that infect Gram-negative bacteria often bind to the bacterial surface by interaction of specific proteins with lipopolysaccharide (LPS). Short tail fiber proteins (tail adhesin, gp12) mediate adsorption of T4-like bacteriophages to Escherichia coli, binding surface proteins or LPS. Produced as a recombined protein, gp12 retains its ability to bind LPS. Since LPS is able to exert a major impact on the immune response in animals and in humans, we have tested LPS-binding phage protein gp12 as a potential modulator of the LPS-induced immune response. We have produced tail adhesin gp12 in a bacterial expression system and confirmed its ability to form trimers and to bind lipopolysaccharide in vitro by dynamic light scattering. This product had no negative effect on mammalian cell proliferation in vitro. Further, no harmful effects of this protein were observed in mice. Thus, gp12 was used in combination with LPS in a murine model, and it decreased the inflammatory response to LPS in vivo, as assessed by serum levels of cytokines IL-1 alpha and IL-6 and by histopathological analysis of spleen, liver, kidney and lungs. Thus, in future studies gp12 may be considered as a potential tool for modulation and specifically for counteracting LPS-related physiological effects in vivo. |
| first_indexed | 2024-12-12T08:08:38Z |
| format | Article |
| id | doaj.art-d4d85033a7314f6498d0a301566c6c22 |
| institution | Directory Open Access Journal |
| issn | 1664-302X |
| language | English |
| last_indexed | 2024-12-12T08:08:38Z |
| publishDate | 2016-07-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Microbiology |
| spelling | doaj.art-d4d85033a7314f6498d0a301566c6c222022-12-22T00:31:52ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2016-07-01710.3389/fmicb.2016.01112211385T4 Phage Tail Adhesin Gp12 Counteracts LPS-induced Inflammation In VivoPaulina Miernikiewicz0Anna Klopot1Ryszard Soluch2Piotr Szkuta3Weronika Keska4Katarzyna Hodyra-Stefaniak5Agnieszka Konopka6Marcin Nowak7Dorota Lecion8Zuzanna Kazmierczak9Joanna Majewska10Marek Harhala11Andrzej Gorski12Krystyna Dabrowska13Ludwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of SciencesLudwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of SciencesLudwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of SciencesLudwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of SciencesLudwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of SciencesLudwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of SciencesLudwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of SciencesWroclaw University of Environmental and Life SciencesLudwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of SciencesLudwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of SciencesLudwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of SciencesLudwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of SciencesLudwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of SciencesLudwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of SciencesBacteriophages that infect Gram-negative bacteria often bind to the bacterial surface by interaction of specific proteins with lipopolysaccharide (LPS). Short tail fiber proteins (tail adhesin, gp12) mediate adsorption of T4-like bacteriophages to Escherichia coli, binding surface proteins or LPS. Produced as a recombined protein, gp12 retains its ability to bind LPS. Since LPS is able to exert a major impact on the immune response in animals and in humans, we have tested LPS-binding phage protein gp12 as a potential modulator of the LPS-induced immune response. We have produced tail adhesin gp12 in a bacterial expression system and confirmed its ability to form trimers and to bind lipopolysaccharide in vitro by dynamic light scattering. This product had no negative effect on mammalian cell proliferation in vitro. Further, no harmful effects of this protein were observed in mice. Thus, gp12 was used in combination with LPS in a murine model, and it decreased the inflammatory response to LPS in vivo, as assessed by serum levels of cytokines IL-1 alpha and IL-6 and by histopathological analysis of spleen, liver, kidney and lungs. Thus, in future studies gp12 may be considered as a potential tool for modulation and specifically for counteracting LPS-related physiological effects in vivo.http://journal.frontiersin.org/Journal/10.3389/fmicb.2016.01112/fullInflammationlipopolysaccharideLPST4 phagegp12short tail fibres |
| spellingShingle | Paulina Miernikiewicz Anna Klopot Ryszard Soluch Piotr Szkuta Weronika Keska Katarzyna Hodyra-Stefaniak Agnieszka Konopka Marcin Nowak Dorota Lecion Zuzanna Kazmierczak Joanna Majewska Marek Harhala Andrzej Gorski Krystyna Dabrowska T4 Phage Tail Adhesin Gp12 Counteracts LPS-induced Inflammation In Vivo Frontiers in Microbiology Inflammation lipopolysaccharide LPS T4 phage gp12 short tail fibres |
| title | T4 Phage Tail Adhesin Gp12 Counteracts LPS-induced Inflammation In Vivo |
| title_full | T4 Phage Tail Adhesin Gp12 Counteracts LPS-induced Inflammation In Vivo |
| title_fullStr | T4 Phage Tail Adhesin Gp12 Counteracts LPS-induced Inflammation In Vivo |
| title_full_unstemmed | T4 Phage Tail Adhesin Gp12 Counteracts LPS-induced Inflammation In Vivo |
| title_short | T4 Phage Tail Adhesin Gp12 Counteracts LPS-induced Inflammation In Vivo |
| title_sort | t4 phage tail adhesin gp12 counteracts lps induced inflammation in vivo |
| topic | Inflammation lipopolysaccharide LPS T4 phage gp12 short tail fibres |
| url | http://journal.frontiersin.org/Journal/10.3389/fmicb.2016.01112/full |
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