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Immunoproteomic analysis of Clostridium botulinum type B secretome for identification of immunogenic proteins against botulism

OBJECTIVES: To identify immunogenic proteins of C. botulinum type B secretome by immunoproteomic analysis. RESULTS: In the present study, an attempt was made to elucidate the vaccine candidates/diagnostic molecules against botulism using immuno proteomic approach. C. botulinum type B secretome was e...

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Autores principales: Sharma, Arti, Ponmariappan, S., Rani, Sarita, Alam, S. I., Shukla, S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7904509/
https://www.ncbi.nlm.nih.gov/pubmed/33629143
http://dx.doi.org/10.1007/s10529-021-03091-4
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author Sharma, Arti
Ponmariappan, S.
Rani, Sarita
Alam, S. I.
Shukla, S.
author_facet Sharma, Arti
Ponmariappan, S.
Rani, Sarita
Alam, S. I.
Shukla, S.
author_sort Sharma, Arti
collection PubMed
description OBJECTIVES: To identify immunogenic proteins of C. botulinum type B secretome by immunoproteomic analysis. RESULTS: In the present study, an attempt was made to elucidate the vaccine candidates/diagnostic molecules against botulism using immuno proteomic approach. C. botulinum type B secretome was elucidated when it was grown in TPGY as well as CMM media. Predominant 51 proteins were identified in both the media using 2-DE and mass spectrometry analysis. 2D gels (CMM & TPGY) were probed with respected proteins mice antiserum and obtained 17 and 10 immunogenic proteins in TPGY as well as CMM media respectively. Hypothetical protein CLOSPO_00563, ornithine carbamoyl transferase, FlaA, molecular chaperone GroEL and secreted protease proteins were found as the common immuno dominant proteins in both media. Polyclonal Antibodies raised against C. botulinum types A and E showed cross-reactivity with secretome C. botulinum type B at the lowest dilution (1:1000) but did not show cross reactivity with highest dilution (1:30,000) with C. botulinum type B secretome. Polyclonal antibodies against C. botulinum type F secretome did not show cross reactivity with C. botulinum type B secretome. CONCLUSIONS: Identified immunogenic proteins can be used as vaccine candidates and diagnostic markers for the infant and wound botulism but common immunogenic proteins may be the best vaccine candidate molecule for development of vaccine as well as diagnostic system against the infant and wound botulism. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s10529-021-03091-4.
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spelling pubmed-79045092021-02-25 Immunoproteomic analysis of Clostridium botulinum type B secretome for identification of immunogenic proteins against botulism Sharma, Arti Ponmariappan, S. Rani, Sarita Alam, S. I. Shukla, S. Biotechnol Lett Original Research Paper OBJECTIVES: To identify immunogenic proteins of C. botulinum type B secretome by immunoproteomic analysis. RESULTS: In the present study, an attempt was made to elucidate the vaccine candidates/diagnostic molecules against botulism using immuno proteomic approach. C. botulinum type B secretome was elucidated when it was grown in TPGY as well as CMM media. Predominant 51 proteins were identified in both the media using 2-DE and mass spectrometry analysis. 2D gels (CMM & TPGY) were probed with respected proteins mice antiserum and obtained 17 and 10 immunogenic proteins in TPGY as well as CMM media respectively. Hypothetical protein CLOSPO_00563, ornithine carbamoyl transferase, FlaA, molecular chaperone GroEL and secreted protease proteins were found as the common immuno dominant proteins in both media. Polyclonal Antibodies raised against C. botulinum types A and E showed cross-reactivity with secretome C. botulinum type B at the lowest dilution (1:1000) but did not show cross reactivity with highest dilution (1:30,000) with C. botulinum type B secretome. Polyclonal antibodies against C. botulinum type F secretome did not show cross reactivity with C. botulinum type B secretome. CONCLUSIONS: Identified immunogenic proteins can be used as vaccine candidates and diagnostic markers for the infant and wound botulism but common immunogenic proteins may be the best vaccine candidate molecule for development of vaccine as well as diagnostic system against the infant and wound botulism. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s10529-021-03091-4. Springer Netherlands 2021-02-25 2021 /pmc/articles/PMC7904509/ /pubmed/33629143 http://dx.doi.org/10.1007/s10529-021-03091-4 Text en © The Author(s), under exclusive licence to Springer Nature B.V. part of Springer Nature 2021 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic.
spellingShingle Original Research Paper
Sharma, Arti
Ponmariappan, S.
Rani, Sarita
Alam, S. I.
Shukla, S.
Immunoproteomic analysis of Clostridium botulinum type B secretome for identification of immunogenic proteins against botulism
title Immunoproteomic analysis of Clostridium botulinum type B secretome for identification of immunogenic proteins against botulism
title_full Immunoproteomic analysis of Clostridium botulinum type B secretome for identification of immunogenic proteins against botulism
title_fullStr Immunoproteomic analysis of Clostridium botulinum type B secretome for identification of immunogenic proteins against botulism
title_full_unstemmed Immunoproteomic analysis of Clostridium botulinum type B secretome for identification of immunogenic proteins against botulism
title_short Immunoproteomic analysis of Clostridium botulinum type B secretome for identification of immunogenic proteins against botulism
title_sort immunoproteomic analysis of clostridium botulinum type b secretome for identification of immunogenic proteins against botulism
topic Original Research Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7904509/
https://www.ncbi.nlm.nih.gov/pubmed/33629143
http://dx.doi.org/10.1007/s10529-021-03091-4
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