Título:	A structural in silico analysis of the immunogenicity of L-Asparaginase from Penicillium cerradense
Autor(es):	Andrade, Kellen Cruvinel Rodrigues Homem-de-Mello, Mauricio Motta, Julia Almeida Guimarães, Marina Borges Abreu, Joel Antônio Cordeiro de Souza, Paula Monteiro de Pessoa, Adalberto Pappas Júnior, Georgios Joannis Magalhães, Pérola de Oliveira
ORCID:	https://orcid.org/0000-0002-4541-9177 https://orcid.org/0000-0002-8767-407X https://orcid.org/0000-0002-5969-0806 https://orcid.org/0000-0002-5268-8690 https://orcid.org/0000-0002-1100-976X https://orcid.org/0000-0001-8011-6940
Afiliação do autor:	University of Brasília, School of Health Sciences, Department of Pharmacy, Laboratory of Natural Products University of Brasília, School of Health Sciences, Department of Pharmacy, inSiliTox University of Brasília, School of Health Sciences, Department of Pharmacy, inSiliTox University of Brasília, School of Health Sciences, Department of Pharmacy, Laboratory of Natural Products University of Brasília, School of Health Sciences, Department of Pharmacy, Laboratory of Natural Products University of Brasília, School of Health Sciences, Department of Pharmacy, Laboratory of Natural Products University of São Paulo, School of Pharmaceutical Sciences, Department of Biochemical and Pharmaceutical Technology University of Brasilia, Institute Biological Sciences, Department Cell Biology University of Brasília, School of Health Sciences, Department of Pharmacy, Laboratory of Natural Products
Assunto:	L-asparaginase Imunogenicidade Penicillium cerradense
Data de publicação:	2024
Editora:	MDPI
Referência:	ANDRADE, Kellen Cruvinel Rodrigues et al. A structural In silico analysis of the immunogenicity of L-Asparaginase from Penicillium cerradense. International Journal of Molecular Sciences, v. 25, n. 9, 2024. DOI: https://doi.org/10.3390/ijms25094788. Disponível em: https://www.mdpi.com/1422-0067/25/9/4788. Acesso em: 28 out. 2025.
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 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.
Unidade Acadêmica:	Faculdade de Ciências da Saúde (FS) Departamento de Farmácia (FS FAR) Instituto de Ciências Biológicas (IB) Departamento de Biologia Celular (IB CEL)
Programa de pós-graduação:	Programa de Pós-Graduação em Ciências Farmacêuticas
DOI:	https://doi.org/10.3390/ijms25094788
Aparece nas coleções:	Artigos publicados em periódicos e afins

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