In-solution behavior and protective potential of asparagine synthetase A from
l-Asparagine synthetase (AS) acts in asparagine formation and can be classified into two families: AS-A or AS-B. AS-A is mainly found in prokaryotes and can synthetize asparagine from ammonia. Distinct from other eukaryotes, Trypanosoma cruzi produces an AS-A. AS-A from Trypanosoma cruzi (Tc-AS-A) d...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Souza Morini, Flávia [verfasserIn] de Castro, Emanuella [verfasserIn] de Morais, Stephanie Bath [verfasserIn] Lancheros Contreras, Cesar [verfasserIn] Pereira Weiler, Ana Valéria [verfasserIn] Murakami, Mario Tyago [verfasserIn] Pinge-Filho, Phileno [verfasserIn] Yamada-Ogatta, Sueli Fumie [verfasserIn] de Arruda Campos Brasil de Souza, Tatiana [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2019 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Molecular and biochemical parasitology - Amsterdam : Elsevier, 1980, 230, Seite 1-7 |
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| Übergeordnetes Werk: |
volume:230 ; pages:1-7 |
| DOI / URN: |
10.1016/j.molbiopara.2019.03.002 |
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| Katalog-ID: |
ELV002250136 |
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| 520 | |a l-Asparagine synthetase (AS) acts in asparagine formation and can be classified into two families: AS-A or AS-B. AS-A is mainly found in prokaryotes and can synthetize asparagine from ammonia. Distinct from other eukaryotes, Trypanosoma cruzi produces an AS-A. AS-A from Trypanosoma cruzi (Tc-AS-A) differs from prokaryotic AS-A due to its ability to catalyze asparagine synthesis using both glutamine and ammonia as nitrogen sources. Regarding these peculiarities, this work uses several biophysical techniques to provide data concerning the Tc-AS-A in-solution behavior. Tc-AS-A was produced as a recombinant and purified by three chromatography steps. Circular dichroism, dynamic light scattering, and analytical size exclusion chromatography showed that Tc-AS-A has the same fold and quaternary arrangement of prokaryotic AS-A. Despite the tendency of protein to aggregate, stable dimers were obtained when solubilization occurred at pH ≤ 7.0. We also demonstrate the protective efficacy against T. cruzi infection in mice immunized with Tc-AS-A. Our results indicate that immunization with Tc-AS-A might confer partial protection to infective forms of T. cruzi in this particular model. | ||
| 650 | 4 | |a Asparagine synthetase A | |
| 650 | 4 | |a In-solution behavior | |
| 650 | 4 | |a Immunoprotection | |
| 700 | 1 | |a de Castro, Emanuella |e verfasserin |4 aut | |
| 700 | 1 | |a de Morais, Stephanie Bath |e verfasserin |0 (orcid)0000-0002-5729-8202 |4 aut | |
| 700 | 1 | |a Lancheros Contreras, Cesar |e verfasserin |4 aut | |
| 700 | 1 | |a Pereira Weiler, Ana Valéria |e verfasserin |4 aut | |
| 700 | 1 | |a Murakami, Mario Tyago |e verfasserin |4 aut | |
| 700 | 1 | |a Pinge-Filho, Phileno |e verfasserin |0 (orcid)0000-0002-1500-3998 |4 aut | |
| 700 | 1 | |a Yamada-Ogatta, Sueli Fumie |e verfasserin |0 (orcid)0000-0003-1183-146X |4 aut | |
| 700 | 1 | |a de Arruda Campos Brasil de Souza, Tatiana |e verfasserin |0 (orcid)0000-0002-1850-6080 |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Molecular and biochemical parasitology |d Amsterdam : Elsevier, 1980 |g 230, Seite 1-7 |w (DE-627)302466061 |w (DE-600)1491098-6 |w (DE-576)079719295 |x 1872-9428 |7 nnns |
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| 912 | |a GBV_ILN_2059 | ||
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| 912 | |a GBV_ILN_4242 | ||
| 912 | |a GBV_ILN_4251 | ||
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10.1016/j.molbiopara.2019.03.002 doi (DE-627)ELV002250136 (ELSEVIER)S0166-6851(18)30107-5 DE-627 ger DE-627 rda eng 590 540 610 DE-600 44.44 bkl Souza Morini, Flávia verfasserin aut In-solution behavior and protective potential of asparagine synthetase A from 2019 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier l-Asparagine synthetase (AS) acts in asparagine formation and can be classified into two families: AS-A or AS-B. AS-A is mainly found in prokaryotes and can synthetize asparagine from ammonia. Distinct from other eukaryotes, Trypanosoma cruzi produces an AS-A. AS-A from Trypanosoma cruzi (Tc-AS-A) differs from prokaryotic AS-A due to its ability to catalyze asparagine synthesis using both glutamine and ammonia as nitrogen sources. Regarding these peculiarities, this work uses several biophysical techniques to provide data concerning the Tc-AS-A in-solution behavior. Tc-AS-A was produced as a recombinant and purified by three chromatography steps. Circular dichroism, dynamic light scattering, and analytical size exclusion chromatography showed that Tc-AS-A has the same fold and quaternary arrangement of prokaryotic AS-A. Despite the tendency of protein to aggregate, stable dimers were obtained when solubilization occurred at pH ≤ 7.0. We also demonstrate the protective efficacy against T. cruzi infection in mice immunized with Tc-AS-A. Our results indicate that immunization with Tc-AS-A might confer partial protection to infective forms of T. cruzi in this particular model. Asparagine synthetase A In-solution behavior Immunoprotection de Castro, Emanuella verfasserin aut de Morais, Stephanie Bath verfasserin (orcid)0000-0002-5729-8202 aut Lancheros Contreras, Cesar verfasserin aut Pereira Weiler, Ana Valéria verfasserin aut Murakami, Mario Tyago verfasserin aut Pinge-Filho, Phileno verfasserin (orcid)0000-0002-1500-3998 aut Yamada-Ogatta, Sueli Fumie verfasserin (orcid)0000-0003-1183-146X aut de Arruda Campos Brasil de Souza, Tatiana verfasserin (orcid)0000-0002-1850-6080 aut Enthalten in Molecular and biochemical parasitology Amsterdam : Elsevier, 1980 230, Seite 1-7 (DE-627)302466061 (DE-600)1491098-6 (DE-576)079719295 1872-9428 nnns volume:230 pages:1-7 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 44.44 Parasitologie Medizin AR 230 1-7 |
| spelling |
10.1016/j.molbiopara.2019.03.002 doi (DE-627)ELV002250136 (ELSEVIER)S0166-6851(18)30107-5 DE-627 ger DE-627 rda eng 590 540 610 DE-600 44.44 bkl Souza Morini, Flávia verfasserin aut In-solution behavior and protective potential of asparagine synthetase A from 2019 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier l-Asparagine synthetase (AS) acts in asparagine formation and can be classified into two families: AS-A or AS-B. AS-A is mainly found in prokaryotes and can synthetize asparagine from ammonia. Distinct from other eukaryotes, Trypanosoma cruzi produces an AS-A. AS-A from Trypanosoma cruzi (Tc-AS-A) differs from prokaryotic AS-A due to its ability to catalyze asparagine synthesis using both glutamine and ammonia as nitrogen sources. Regarding these peculiarities, this work uses several biophysical techniques to provide data concerning the Tc-AS-A in-solution behavior. Tc-AS-A was produced as a recombinant and purified by three chromatography steps. Circular dichroism, dynamic light scattering, and analytical size exclusion chromatography showed that Tc-AS-A has the same fold and quaternary arrangement of prokaryotic AS-A. Despite the tendency of protein to aggregate, stable dimers were obtained when solubilization occurred at pH ≤ 7.0. We also demonstrate the protective efficacy against T. cruzi infection in mice immunized with Tc-AS-A. Our results indicate that immunization with Tc-AS-A might confer partial protection to infective forms of T. cruzi in this particular model. Asparagine synthetase A In-solution behavior Immunoprotection de Castro, Emanuella verfasserin aut de Morais, Stephanie Bath verfasserin (orcid)0000-0002-5729-8202 aut Lancheros Contreras, Cesar verfasserin aut Pereira Weiler, Ana Valéria verfasserin aut Murakami, Mario Tyago verfasserin aut Pinge-Filho, Phileno verfasserin (orcid)0000-0002-1500-3998 aut Yamada-Ogatta, Sueli Fumie verfasserin (orcid)0000-0003-1183-146X aut de Arruda Campos Brasil de Souza, Tatiana verfasserin (orcid)0000-0002-1850-6080 aut Enthalten in Molecular and biochemical parasitology Amsterdam : Elsevier, 1980 230, Seite 1-7 (DE-627)302466061 (DE-600)1491098-6 (DE-576)079719295 1872-9428 nnns volume:230 pages:1-7 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 44.44 Parasitologie Medizin AR 230 1-7 |
| allfields_unstemmed |
10.1016/j.molbiopara.2019.03.002 doi (DE-627)ELV002250136 (ELSEVIER)S0166-6851(18)30107-5 DE-627 ger DE-627 rda eng 590 540 610 DE-600 44.44 bkl Souza Morini, Flávia verfasserin aut In-solution behavior and protective potential of asparagine synthetase A from 2019 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier l-Asparagine synthetase (AS) acts in asparagine formation and can be classified into two families: AS-A or AS-B. AS-A is mainly found in prokaryotes and can synthetize asparagine from ammonia. Distinct from other eukaryotes, Trypanosoma cruzi produces an AS-A. AS-A from Trypanosoma cruzi (Tc-AS-A) differs from prokaryotic AS-A due to its ability to catalyze asparagine synthesis using both glutamine and ammonia as nitrogen sources. Regarding these peculiarities, this work uses several biophysical techniques to provide data concerning the Tc-AS-A in-solution behavior. Tc-AS-A was produced as a recombinant and purified by three chromatography steps. Circular dichroism, dynamic light scattering, and analytical size exclusion chromatography showed that Tc-AS-A has the same fold and quaternary arrangement of prokaryotic AS-A. Despite the tendency of protein to aggregate, stable dimers were obtained when solubilization occurred at pH ≤ 7.0. We also demonstrate the protective efficacy against T. cruzi infection in mice immunized with Tc-AS-A. Our results indicate that immunization with Tc-AS-A might confer partial protection to infective forms of T. cruzi in this particular model. Asparagine synthetase A In-solution behavior Immunoprotection de Castro, Emanuella verfasserin aut de Morais, Stephanie Bath verfasserin (orcid)0000-0002-5729-8202 aut Lancheros Contreras, Cesar verfasserin aut Pereira Weiler, Ana Valéria verfasserin aut Murakami, Mario Tyago verfasserin aut Pinge-Filho, Phileno verfasserin (orcid)0000-0002-1500-3998 aut Yamada-Ogatta, Sueli Fumie verfasserin (orcid)0000-0003-1183-146X aut de Arruda Campos Brasil de Souza, Tatiana verfasserin (orcid)0000-0002-1850-6080 aut Enthalten in Molecular and biochemical parasitology Amsterdam : Elsevier, 1980 230, Seite 1-7 (DE-627)302466061 (DE-600)1491098-6 (DE-576)079719295 1872-9428 nnns volume:230 pages:1-7 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 44.44 Parasitologie Medizin AR 230 1-7 |
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10.1016/j.molbiopara.2019.03.002 doi (DE-627)ELV002250136 (ELSEVIER)S0166-6851(18)30107-5 DE-627 ger DE-627 rda eng 590 540 610 DE-600 44.44 bkl Souza Morini, Flávia verfasserin aut In-solution behavior and protective potential of asparagine synthetase A from 2019 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier l-Asparagine synthetase (AS) acts in asparagine formation and can be classified into two families: AS-A or AS-B. AS-A is mainly found in prokaryotes and can synthetize asparagine from ammonia. Distinct from other eukaryotes, Trypanosoma cruzi produces an AS-A. AS-A from Trypanosoma cruzi (Tc-AS-A) differs from prokaryotic AS-A due to its ability to catalyze asparagine synthesis using both glutamine and ammonia as nitrogen sources. Regarding these peculiarities, this work uses several biophysical techniques to provide data concerning the Tc-AS-A in-solution behavior. Tc-AS-A was produced as a recombinant and purified by three chromatography steps. Circular dichroism, dynamic light scattering, and analytical size exclusion chromatography showed that Tc-AS-A has the same fold and quaternary arrangement of prokaryotic AS-A. Despite the tendency of protein to aggregate, stable dimers were obtained when solubilization occurred at pH ≤ 7.0. We also demonstrate the protective efficacy against T. cruzi infection in mice immunized with Tc-AS-A. Our results indicate that immunization with Tc-AS-A might confer partial protection to infective forms of T. cruzi in this particular model. Asparagine synthetase A In-solution behavior Immunoprotection de Castro, Emanuella verfasserin aut de Morais, Stephanie Bath verfasserin (orcid)0000-0002-5729-8202 aut Lancheros Contreras, Cesar verfasserin aut Pereira Weiler, Ana Valéria verfasserin aut Murakami, Mario Tyago verfasserin aut Pinge-Filho, Phileno verfasserin (orcid)0000-0002-1500-3998 aut Yamada-Ogatta, Sueli Fumie verfasserin (orcid)0000-0003-1183-146X aut de Arruda Campos Brasil de Souza, Tatiana verfasserin (orcid)0000-0002-1850-6080 aut Enthalten in Molecular and biochemical parasitology Amsterdam : Elsevier, 1980 230, Seite 1-7 (DE-627)302466061 (DE-600)1491098-6 (DE-576)079719295 1872-9428 nnns volume:230 pages:1-7 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 44.44 Parasitologie Medizin AR 230 1-7 |
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10.1016/j.molbiopara.2019.03.002 doi (DE-627)ELV002250136 (ELSEVIER)S0166-6851(18)30107-5 DE-627 ger DE-627 rda eng 590 540 610 DE-600 44.44 bkl Souza Morini, Flávia verfasserin aut In-solution behavior and protective potential of asparagine synthetase A from 2019 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier l-Asparagine synthetase (AS) acts in asparagine formation and can be classified into two families: AS-A or AS-B. AS-A is mainly found in prokaryotes and can synthetize asparagine from ammonia. Distinct from other eukaryotes, Trypanosoma cruzi produces an AS-A. AS-A from Trypanosoma cruzi (Tc-AS-A) differs from prokaryotic AS-A due to its ability to catalyze asparagine synthesis using both glutamine and ammonia as nitrogen sources. Regarding these peculiarities, this work uses several biophysical techniques to provide data concerning the Tc-AS-A in-solution behavior. Tc-AS-A was produced as a recombinant and purified by three chromatography steps. Circular dichroism, dynamic light scattering, and analytical size exclusion chromatography showed that Tc-AS-A has the same fold and quaternary arrangement of prokaryotic AS-A. Despite the tendency of protein to aggregate, stable dimers were obtained when solubilization occurred at pH ≤ 7.0. We also demonstrate the protective efficacy against T. cruzi infection in mice immunized with Tc-AS-A. Our results indicate that immunization with Tc-AS-A might confer partial protection to infective forms of T. cruzi in this particular model. Asparagine synthetase A In-solution behavior Immunoprotection de Castro, Emanuella verfasserin aut de Morais, Stephanie Bath verfasserin (orcid)0000-0002-5729-8202 aut Lancheros Contreras, Cesar verfasserin aut Pereira Weiler, Ana Valéria verfasserin aut Murakami, Mario Tyago verfasserin aut Pinge-Filho, Phileno verfasserin (orcid)0000-0002-1500-3998 aut Yamada-Ogatta, Sueli Fumie verfasserin (orcid)0000-0003-1183-146X aut de Arruda Campos Brasil de Souza, Tatiana verfasserin (orcid)0000-0002-1850-6080 aut Enthalten in Molecular and biochemical parasitology Amsterdam : Elsevier, 1980 230, Seite 1-7 (DE-627)302466061 (DE-600)1491098-6 (DE-576)079719295 1872-9428 nnns volume:230 pages:1-7 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 44.44 Parasitologie Medizin AR 230 1-7 |
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Enthalten in Molecular and biochemical parasitology 230, Seite 1-7 volume:230 pages:1-7 |
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Souza Morini, Flávia @@aut@@ de Castro, Emanuella @@aut@@ de Morais, Stephanie Bath @@aut@@ Lancheros Contreras, Cesar @@aut@@ Pereira Weiler, Ana Valéria @@aut@@ Murakami, Mario Tyago @@aut@@ Pinge-Filho, Phileno @@aut@@ Yamada-Ogatta, Sueli Fumie @@aut@@ de Arruda Campos Brasil de Souza, Tatiana @@aut@@ |
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in-solution behavior and protective potential of asparagine synthetase a from |
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In-solution behavior and protective potential of asparagine synthetase A from |
| abstract |
l-Asparagine synthetase (AS) acts in asparagine formation and can be classified into two families: AS-A or AS-B. AS-A is mainly found in prokaryotes and can synthetize asparagine from ammonia. Distinct from other eukaryotes, Trypanosoma cruzi produces an AS-A. AS-A from Trypanosoma cruzi (Tc-AS-A) differs from prokaryotic AS-A due to its ability to catalyze asparagine synthesis using both glutamine and ammonia as nitrogen sources. Regarding these peculiarities, this work uses several biophysical techniques to provide data concerning the Tc-AS-A in-solution behavior. Tc-AS-A was produced as a recombinant and purified by three chromatography steps. Circular dichroism, dynamic light scattering, and analytical size exclusion chromatography showed that Tc-AS-A has the same fold and quaternary arrangement of prokaryotic AS-A. Despite the tendency of protein to aggregate, stable dimers were obtained when solubilization occurred at pH ≤ 7.0. We also demonstrate the protective efficacy against T. cruzi infection in mice immunized with Tc-AS-A. Our results indicate that immunization with Tc-AS-A might confer partial protection to infective forms of T. cruzi in this particular model. |
| abstractGer |
l-Asparagine synthetase (AS) acts in asparagine formation and can be classified into two families: AS-A or AS-B. AS-A is mainly found in prokaryotes and can synthetize asparagine from ammonia. Distinct from other eukaryotes, Trypanosoma cruzi produces an AS-A. AS-A from Trypanosoma cruzi (Tc-AS-A) differs from prokaryotic AS-A due to its ability to catalyze asparagine synthesis using both glutamine and ammonia as nitrogen sources. Regarding these peculiarities, this work uses several biophysical techniques to provide data concerning the Tc-AS-A in-solution behavior. Tc-AS-A was produced as a recombinant and purified by three chromatography steps. Circular dichroism, dynamic light scattering, and analytical size exclusion chromatography showed that Tc-AS-A has the same fold and quaternary arrangement of prokaryotic AS-A. Despite the tendency of protein to aggregate, stable dimers were obtained when solubilization occurred at pH ≤ 7.0. We also demonstrate the protective efficacy against T. cruzi infection in mice immunized with Tc-AS-A. Our results indicate that immunization with Tc-AS-A might confer partial protection to infective forms of T. cruzi in this particular model. |
| abstract_unstemmed |
l-Asparagine synthetase (AS) acts in asparagine formation and can be classified into two families: AS-A or AS-B. AS-A is mainly found in prokaryotes and can synthetize asparagine from ammonia. Distinct from other eukaryotes, Trypanosoma cruzi produces an AS-A. AS-A from Trypanosoma cruzi (Tc-AS-A) differs from prokaryotic AS-A due to its ability to catalyze asparagine synthesis using both glutamine and ammonia as nitrogen sources. Regarding these peculiarities, this work uses several biophysical techniques to provide data concerning the Tc-AS-A in-solution behavior. Tc-AS-A was produced as a recombinant and purified by three chromatography steps. Circular dichroism, dynamic light scattering, and analytical size exclusion chromatography showed that Tc-AS-A has the same fold and quaternary arrangement of prokaryotic AS-A. Despite the tendency of protein to aggregate, stable dimers were obtained when solubilization occurred at pH ≤ 7.0. We also demonstrate the protective efficacy against T. cruzi infection in mice immunized with Tc-AS-A. Our results indicate that immunization with Tc-AS-A might confer partial protection to infective forms of T. cruzi in this particular model. |
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| score |
7.398569 |