A Structural In Silico Analysis of the Immunogenicity of L-Asparaginase from Penicillium cerradense
L-asparaginase is an essential drug used to treat acute lymphoid leukemia (ALL), a cancer of high prevalence in children. Several adverse reactions associated with L-asparaginase have been observed, mainly caused by immunogenicity and allergenicity. Some strategies have been adopted, such as searchi...
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| Published in: | International journal of molecular sciences Vol. 25; no. 9; p. 4788 |
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| Main Authors: | , , , , , , , , |
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| Abstract | L-asparaginase is an essential drug used to treat acute lymphoid leukemia (ALL), a cancer of high prevalence in children. Several adverse reactions associated with L-asparaginase have been observed, mainly caused by immunogenicity and allergenicity. Some strategies have been adopted, such as searching for new microorganisms that produce the enzyme and applying protein engineering. Therefore, this work aimed to elucidate the molecular structure and predict the immunogenic profile of L-asparaginase from
, recently revealed as a new fungus of the genus
and producer of the enzyme, as a motivation to search for alternatives to bacterial L-asparaginase. In the evolutionary relationship, L-asparaginase from
closely matches
species. Using in silico tools, we characterized the enzyme as a protein fragment of 378 amino acids (39 kDa), including a signal peptide containing 17 amino acids, and the isoelectric point at 5.13. The oligomeric state was predicted to be a homotetramer. Also, this L-asparaginase presented a similar immunogenicity response (T- and B-cell epitopes) compared to
and
enzymes. These results suggest a potentially useful L-asparaginase, with insights that can drive strategies to improve enzyme production. |
|---|---|
| AbstractList | L-asparaginase is an essential drug used to treat acute lymphoid leukemia (ALL), a cancer of high prevalence in children. Several adverse reactions associated with L-asparaginase have been observed, mainly caused by immunogenicity and allergenicity. Some strategies have been adopted, such as searching for new microorganisms that produce the enzyme and applying protein engineering. Therefore, this work aimed to elucidate the molecular structure and predict the immunogenic profile of L-asparaginase from Penicillium cerradense, recently revealed as a new fungus of the genus Penicillium and producer of the enzyme, as a motivation to search for alternatives to bacterial L-asparaginase. In the evolutionary relationship, L-asparaginase from P. cerradense closely matches Aspergillus species. Using in silico tools, we characterized the enzyme as a protein fragment of 378 amino acids (39 kDa), including a signal peptide containing 17 amino acids, and the isoelectric point at 5.13. The oligomeric state was predicted to be a homotetramer. Also, this L-asparaginase presented a similar immunogenicity response (T- and B-cell epitopes) compared to Escherichia coli and Dickeya chrysanthemi enzymes. These results suggest a potentially useful L-asparaginase, with insights that can drive strategies to improve enzyme production. L-asparaginase is an essential drug used to treat acute lymphoid leukemia (ALL), a cancer of high prevalence in children. Several adverse reactions associated with L-asparaginase have been observed, mainly caused by immunogenicity and allergenicity. Some strategies have been adopted, such as searching for new microorganisms that produce the enzyme and applying protein engineering. Therefore, this work aimed to elucidate the molecular structure and predict the immunogenic profile of L-asparaginase from , recently revealed as a new fungus of the genus and producer of the enzyme, as a motivation to search for alternatives to bacterial L-asparaginase. In the evolutionary relationship, L-asparaginase from closely matches species. Using in silico tools, we characterized the enzyme as a protein fragment of 378 amino acids (39 kDa), including a signal peptide containing 17 amino acids, and the isoelectric point at 5.13. The oligomeric state was predicted to be a homotetramer. Also, this L-asparaginase presented a similar immunogenicity response (T- and B-cell epitopes) compared to and enzymes. These results suggest a potentially useful L-asparaginase, with insights that can drive strategies to improve enzyme production. L-asparaginase is an essential drug used to treat acute lymphoid leukemia (ALL), a cancer of high prevalence in children. Several adverse reactions associated with L-asparaginase have been observed, mainly caused by immunogenicity and allergenicity. Some strategies have been adopted, such as searching for new microorganisms that produce the enzyme and applying protein engineering. Therefore, this work aimed to elucidate the molecular structure and predict the immunogenic profile of L-asparaginase from Penicillium cerradense, recently revealed as a new fungus of the genus Penicillium and producer of the enzyme, as a motivation to search for alternatives to bacterial L-asparaginase. In the evolutionary relationship, L-asparaginase from P. cerradense closely matches Aspergillus species. Using in silico tools, we characterized the enzyme as a protein fragment of 378 amino acids (39 kDa), including a signal peptide containing 17 amino acids, and the isoelectric point at 5.13. The oligomeric state was predicted to be a homotetramer. Also, this L-asparaginase presented a similar immunogenicity response (T- and B-cell epitopes) compared to Escherichia coli and Dickeya chrysanthemi enzymes. These results suggest a potentially useful L-asparaginase, with insights that can drive strategies to improve enzyme production.L-asparaginase is an essential drug used to treat acute lymphoid leukemia (ALL), a cancer of high prevalence in children. Several adverse reactions associated with L-asparaginase have been observed, mainly caused by immunogenicity and allergenicity. Some strategies have been adopted, such as searching for new microorganisms that produce the enzyme and applying protein engineering. Therefore, this work aimed to elucidate the molecular structure and predict the immunogenic profile of L-asparaginase from Penicillium cerradense, recently revealed as a new fungus of the genus Penicillium and producer of the enzyme, as a motivation to search for alternatives to bacterial L-asparaginase. In the evolutionary relationship, L-asparaginase from P. cerradense closely matches Aspergillus species. Using in silico tools, we characterized the enzyme as a protein fragment of 378 amino acids (39 kDa), including a signal peptide containing 17 amino acids, and the isoelectric point at 5.13. The oligomeric state was predicted to be a homotetramer. Also, this L-asparaginase presented a similar immunogenicity response (T- and B-cell epitopes) compared to Escherichia coli and Dickeya chrysanthemi enzymes. These results suggest a potentially useful L-asparaginase, with insights that can drive strategies to improve enzyme production. |
| Author | Homem-de-Mello, Mauricio Borges, Marina Guimarães Pappas, Jr, Georgios J Pessoa, Adalberto de Oliveira Magalhães, Pérola de Souza, Paula Monteiro Motta, Julia Almeida Andrade, Kellen Cruvinel Rodrigues de Abreu, Joel Antônio Cordeiro |
| Author_xml | – sequence: 1 givenname: Kellen Cruvinel Rodrigues surname: Andrade fullname: Andrade, Kellen Cruvinel Rodrigues organization: Laboratory of Natural Products, Department of Pharmacy, Faculty of Health Sciences, University of Brasilia, Brasilia 70910-900, Brazil – sequence: 2 givenname: Mauricio orcidid: 0000-0002-4541-9177 surname: Homem-de-Mello fullname: Homem-de-Mello, Mauricio organization: inSiliTox, Department of Pharmacy, Faculty of Health Sciences, University of Brasilia, Brasilia 70910-900, Brazil – sequence: 3 givenname: Julia Almeida surname: Motta fullname: Motta, Julia Almeida organization: inSiliTox, Department of Pharmacy, Faculty of Health Sciences, University of Brasilia, Brasilia 70910-900, Brazil – sequence: 4 givenname: Marina Guimarães orcidid: 0000-0002-8767-407X surname: Borges fullname: Borges, Marina Guimarães organization: Laboratory of Natural Products, Department of Pharmacy, Faculty of Health Sciences, University of Brasilia, Brasilia 70910-900, Brazil – sequence: 5 givenname: Joel Antônio Cordeiro orcidid: 0000-0002-5969-0806 surname: de Abreu fullname: de Abreu, Joel Antônio Cordeiro organization: Laboratory of Natural Products, Department of Pharmacy, Faculty of Health Sciences, University of Brasilia, Brasilia 70910-900, Brazil – sequence: 6 givenname: Paula Monteiro surname: de Souza fullname: de Souza, Paula Monteiro organization: Laboratory of Natural Products, Department of Pharmacy, Faculty of Health Sciences, University of Brasilia, Brasilia 70910-900, Brazil – sequence: 7 givenname: Adalberto orcidid: 0000-0002-5268-8690 surname: Pessoa fullname: Pessoa, Adalberto organization: Department of Biochemical and Pharmaceutical Technology, School of Pharmaceutical Sciences, University of São Paulo, São Paulo 05508-000, Brazil – sequence: 8 givenname: Georgios J orcidid: 0000-0002-1100-976X surname: Pappas, Jr fullname: Pappas, Jr, Georgios J organization: Department Cell Biology, Institute Biological Sciences, University of Brasilia, Brasilia 70910-900, Brazil – sequence: 9 givenname: Pérola orcidid: 0000-0001-8011-6940 surname: de Oliveira Magalhães fullname: de Oliveira Magalhães, Pérola organization: Laboratory of Natural Products, Department of Pharmacy, Faculty of Health Sciences, University of Brasilia, Brasilia 70910-900, Brazil |
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| Title | A Structural In Silico Analysis of the Immunogenicity of L-Asparaginase from Penicillium cerradense |
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