Correlation of DPP4 enzyme with SARS-CoV-2 infection

Detalhes bibliográficos
Autor(a) principal: Mota, Lennara Pereira
Data de Publicação: 2021
Outros Autores: Sousa, Maria Vitalina Alves de, Silva, Maria Jandeline do Nascimento, Eckhardt , Amanda, Vasconcelos, Domennique Miranda, Almeida, Lyrlanda Maria Cavalcante de, Freitas, Juliana Maria de, Cardoso, Alexandra Rodrigues, Oliveira, Annyelli Victória Moura, Oliveira, João Pedro Tavares de, Freitas, Francilene Vieira da Silva, Penha, Ana Alinne Gomes da, Borges, Eldson Rodrigues, Santos, Joice Mara Ferreira dos, Lima, Beatriz Caroline Leão, Feitosa, Andressa Dâmaras Freitas, Figueiredo, Iaggo Henrique de Sousa, Gomes , Emanuelle da Costa, Teixeira, Geovana Marques
Tipo de documento: Artigo
Idioma: por
Título da fonte: Research, Society and Development
Texto Completo: https://rsdjournal.org/index.php/rsd/article/view/21361
Resumo: COVID-19 has become a high-risk issue of global concern. The glycoprotein (S) peak in the virion envelope is proteolytically cleaved into the S1 and S2 subunits, and receptor recognition is mediated by receptor binding domain (RBD) and membrane fusion. This is a literature review of a qualitative nature based on scientific production from studies published between 2019 and 2021 that addressed the main objective of this study to correlate DPP4 in SARS-CoV-2 infection. Coronavirus tropism mainly depends on the ability of the glycoprotein (S) entry peak to bind to cell surface receptors. It is currently reported that SARS-CoV-2 can use angiotensin-2 converting enzyme (ACE2), the same receptor as SARS-CoV, to infect humans. However, recent evidence suggests that SARS-CoV-2 binds to DPP4/CD26 after entering airway cells. It appears that the interaction between the peak glycoprotein SARS-CoV-2 and human DPP4/CD26 (also known as dipeptidyl peptidase-4 (DPP4) is a key factor in sequestration and virulence. In the absence of results from well-designed randomized clinical trials, the efficacy or safety data of DPP4 inhibitors in the treatment of COVID-19 must be interpreted with caution and no clear conclusions can be drawn.The results of these studies may help reveal the impact of using drugs that inhibit DPP4 and whether they can be effective in the treatment of COVID-19 infection.
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spelling Correlation of DPP4 enzyme with SARS-CoV-2 infectionCorrelación de la enzima DPP4 con la infección por SARS-CoV-2Correlação da enzima DPP4 com a infecção por SARS-CoV-2EnzimaDipeptidil peptidase 4COVID-19Glicose.EnzimaDipeptidil peptidasa 4COVID-19Glucosa.EnzymeDipeptidyl peptidase 4COVID-19Glucose.COVID-19 has become a high-risk issue of global concern. The glycoprotein (S) peak in the virion envelope is proteolytically cleaved into the S1 and S2 subunits, and receptor recognition is mediated by receptor binding domain (RBD) and membrane fusion. This is a literature review of a qualitative nature based on scientific production from studies published between 2019 and 2021 that addressed the main objective of this study to correlate DPP4 in SARS-CoV-2 infection. Coronavirus tropism mainly depends on the ability of the glycoprotein (S) entry peak to bind to cell surface receptors. It is currently reported that SARS-CoV-2 can use angiotensin-2 converting enzyme (ACE2), the same receptor as SARS-CoV, to infect humans. However, recent evidence suggests that SARS-CoV-2 binds to DPP4/CD26 after entering airway cells. It appears that the interaction between the peak glycoprotein SARS-CoV-2 and human DPP4/CD26 (also known as dipeptidyl peptidase-4 (DPP4) is a key factor in sequestration and virulence. In the absence of results from well-designed randomized clinical trials, the efficacy or safety data of DPP4 inhibitors in the treatment of COVID-19 must be interpreted with caution and no clear conclusions can be drawn.The results of these studies may help reveal the impact of using drugs that inhibit DPP4 and whether they can be effective in the treatment of COVID-19 infection.COVID-19 se ha convertido en un problema de alto riesgo de preocupación mundial. El pico de glicoproteína (S) en la envoltura del virión se escinde proteolíticamente en las subunidades S1 y S2, y el reconocimiento del receptor está mediado por el dominio de unión al receptor (RBD) y la fusión de la membrana. Se trata de una revisión de la literatura de carácter cualitativo basada en la producción científica de estudios publicados entre 2019 y 2021 que abordaron el objetivo principal de este estudio de correlacionar DPP4 en la infección por SARS-CoV-2. El tropismo por coronavirus depende principalmente de la capacidad del pico de entrada de la glicoproteína (S) para unirse a los receptores de la superficie celular. Actualmente se informa que el SARS-CoV-2 puede usar la enzima convertidora de angiotensina-2 (ACE2), el mismo receptor que el SARS-CoV, para infectar a los seres humanos. Sin embargo, evidencia reciente sugiere que el SARS-CoV-2 se une a DPP4 / CD26 después de ingresar a las células de las vías respiratorias. Parece que la interacción entre el pico de glucoproteína SARS-CoV-2 y la DPP4 / CD26 humana (también conocida como dipeptidil peptidasa-4 (DPP4) es un factor clave en el secuestro y la virulencia. En ausencia de resultados de estudios clínicos aleatorizados bien diseñados ensayos, los datos de eficacia o seguridad de los inhibidores de la DPP4 en el tratamiento de COVID-19 deben interpretarse con precaución y no se pueden sacar conclusiones claras. Los resultados de estos estudios pueden ayudar a revelar el impacto del uso de fármacos que inhiben la DPP4 y si pueden ser eficaz en el tratamiento de la infección por COVID-19.A COVID-19 se tornou uma questão de alto risco de preocupação global. O pico da glicoproteína (S) no envelope do vírion é clivado proteoliticamente nas subunidades S1 e S2, e o reconhecimento do receptor é mediado pelo domínio de ligação ao receptor (RBD) e fusão da membrana. Trata-se de uma revisão bibliográfica de caráter qualitativo que se baseia na produção científica a partir de estudos já publicados entre os anos de 2019 a 2021 que abordavam o objetivo principal deste estudo correlacionar a DPP4 na infecção por SARS-CoV-2. O tropismo dos coronavírus depende principalmente da capacidade do pico de entrada da glicoproteína (S) para se ligar aos receptores da superfície celular. Atualmente, é relatado que o SARS-CoV-2 pode usar a enzima de conversão da angiotensina-2 (ACE2), o mesmo receptor do SARS-CoV, para infectar humanos. No entanto, evidências recentes sugerem que o SARS-CoV-2 se liga ao DPP4 / CD26 após entrar nas células das vias aéreas. Parece que a interação entre a glicoproteína de pico SARS-CoV-2 e DPP4 / CD26 humana (também conhecida como dipeptidil peptidase-4 (DPP4) é um fator chave no sequestro e virulência. Na ausência de resultados de ensaios clínicos randomizados bem desenhados, os dados de eficácia ou segurança dos inibidores DPP4 no tratamento de COVID-19 devem ser interpretados com cautela e nenhuma conclusão clara pode ser feita. Os resultados desses estudos podem ajudar a revelar o impacto do uso de medicamentos que inibem a DPP4 e se eles podem ser eficazes no tratamento da infecção por COVID-19.Research, Society and Development2021-10-17info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://rsdjournal.org/index.php/rsd/article/view/2136110.33448/rsd-v10i13.21361Research, Society and Development; Vol. 10 No. 13; e415101321361Research, Society and Development; Vol. 10 Núm. 13; e415101321361Research, Society and Development; v. 10 n. 13; e4151013213612525-3409reponame:Research, Society and Developmentinstname:Universidade Federal de Itajubá (UNIFEI)instacron:UNIFEIporhttps://rsdjournal.org/index.php/rsd/article/view/21361/19048Copyright (c) 2021 Lennara Pereira Mota; Maria Vitalina Alves de Sousa; Maria Jandeline do Nascimento Silva; Amanda Eckhardt ; Domennique Miranda Vasconcelos; Lyrlanda Maria Cavalcante de Almeida; Juliana Maria de Freitas; Alexandra Rodrigues Cardoso; Annyelli Victória Moura Oliveira; João Pedro Tavares de Oliveira; Francilene Vieira da Silva Freitas; Ana Alinne Gomes da Penha; Eldson Rodrigues Borges; Joice Mara Ferreira dos Santos; Beatriz Caroline Leão Lima; Andressa Dâmaras Freitas Feitosa; Iaggo Henrique de Sousa Figueiredo; Emanuelle da Costa Gomes ; Geovana Marques Teixeirahttps://creativecommons.org/licenses/by/4.0info:eu-repo/semantics/openAccessMota, Lennara PereiraSousa, Maria Vitalina Alves de Silva, Maria Jandeline do Nascimento Eckhardt , Amanda Vasconcelos, Domennique Miranda Almeida, Lyrlanda Maria Cavalcante de Freitas, Juliana Maria de Cardoso, Alexandra Rodrigues Oliveira, Annyelli Victória Moura Oliveira, João Pedro Tavares de Freitas, Francilene Vieira da Silva Penha, Ana Alinne Gomes da Borges, Eldson Rodrigues Santos, Joice Mara Ferreira dos Lima, Beatriz Caroline Leão Feitosa, Andressa Dâmaras Freitas Figueiredo, Iaggo Henrique de Sousa Gomes , Emanuelle da Costa Teixeira, Geovana Marques 2021-11-21T18:26:28Zoai:ojs.pkp.sfu.ca:article/21361Revistahttps://rsdjournal.org/index.php/rsd/indexPUBhttps://rsdjournal.org/index.php/rsd/oairsd.articles@gmail.com2525-34092525-3409opendoar:2024-01-17T09:40:47.647Research, Society and Development - Universidade Federal de Itajubá (UNIFEI)false
dc.title.none.fl_str_mv Correlation of DPP4 enzyme with SARS-CoV-2 infection
Correlación de la enzima DPP4 con la infección por SARS-CoV-2
Correlação da enzima DPP4 com a infecção por SARS-CoV-2
title Correlation of DPP4 enzyme with SARS-CoV-2 infection
spellingShingle Correlation of DPP4 enzyme with SARS-CoV-2 infection
Mota, Lennara Pereira
Enzima
Dipeptidil peptidase 4
COVID-19
Glicose.
Enzima
Dipeptidil peptidasa 4
COVID-19
Glucosa.
Enzyme
Dipeptidyl peptidase 4
COVID-19
Glucose.
title_short Correlation of DPP4 enzyme with SARS-CoV-2 infection
title_full Correlation of DPP4 enzyme with SARS-CoV-2 infection
title_fullStr Correlation of DPP4 enzyme with SARS-CoV-2 infection
title_full_unstemmed Correlation of DPP4 enzyme with SARS-CoV-2 infection
title_sort Correlation of DPP4 enzyme with SARS-CoV-2 infection
author Mota, Lennara Pereira
author_facet Mota, Lennara Pereira
Sousa, Maria Vitalina Alves de
Silva, Maria Jandeline do Nascimento
Eckhardt , Amanda
Vasconcelos, Domennique Miranda
Almeida, Lyrlanda Maria Cavalcante de
Freitas, Juliana Maria de
Cardoso, Alexandra Rodrigues
Oliveira, Annyelli Victória Moura
Oliveira, João Pedro Tavares de
Freitas, Francilene Vieira da Silva
Penha, Ana Alinne Gomes da
Borges, Eldson Rodrigues
Santos, Joice Mara Ferreira dos
Lima, Beatriz Caroline Leão
Feitosa, Andressa Dâmaras Freitas
Figueiredo, Iaggo Henrique de Sousa
Gomes , Emanuelle da Costa
Teixeira, Geovana Marques
author_role author
author2 Sousa, Maria Vitalina Alves de
Silva, Maria Jandeline do Nascimento
Eckhardt , Amanda
Vasconcelos, Domennique Miranda
Almeida, Lyrlanda Maria Cavalcante de
Freitas, Juliana Maria de
Cardoso, Alexandra Rodrigues
Oliveira, Annyelli Victória Moura
Oliveira, João Pedro Tavares de
Freitas, Francilene Vieira da Silva
Penha, Ana Alinne Gomes da
Borges, Eldson Rodrigues
Santos, Joice Mara Ferreira dos
Lima, Beatriz Caroline Leão
Feitosa, Andressa Dâmaras Freitas
Figueiredo, Iaggo Henrique de Sousa
Gomes , Emanuelle da Costa
Teixeira, Geovana Marques
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
dc.contributor.author.fl_str_mv Mota, Lennara Pereira
Sousa, Maria Vitalina Alves de
Silva, Maria Jandeline do Nascimento
Eckhardt , Amanda
Vasconcelos, Domennique Miranda
Almeida, Lyrlanda Maria Cavalcante de
Freitas, Juliana Maria de
Cardoso, Alexandra Rodrigues
Oliveira, Annyelli Victória Moura
Oliveira, João Pedro Tavares de
Freitas, Francilene Vieira da Silva
Penha, Ana Alinne Gomes da
Borges, Eldson Rodrigues
Santos, Joice Mara Ferreira dos
Lima, Beatriz Caroline Leão
Feitosa, Andressa Dâmaras Freitas
Figueiredo, Iaggo Henrique de Sousa
Gomes , Emanuelle da Costa
Teixeira, Geovana Marques
dc.subject.por.fl_str_mv Enzima
Dipeptidil peptidase 4
COVID-19
Glicose.
Enzima
Dipeptidil peptidasa 4
COVID-19
Glucosa.
Enzyme
Dipeptidyl peptidase 4
COVID-19
Glucose.
topic Enzima
Dipeptidil peptidase 4
COVID-19
Glicose.
Enzima
Dipeptidil peptidasa 4
COVID-19
Glucosa.
Enzyme
Dipeptidyl peptidase 4
COVID-19
Glucose.
description COVID-19 has become a high-risk issue of global concern. The glycoprotein (S) peak in the virion envelope is proteolytically cleaved into the S1 and S2 subunits, and receptor recognition is mediated by receptor binding domain (RBD) and membrane fusion. This is a literature review of a qualitative nature based on scientific production from studies published between 2019 and 2021 that addressed the main objective of this study to correlate DPP4 in SARS-CoV-2 infection. Coronavirus tropism mainly depends on the ability of the glycoprotein (S) entry peak to bind to cell surface receptors. It is currently reported that SARS-CoV-2 can use angiotensin-2 converting enzyme (ACE2), the same receptor as SARS-CoV, to infect humans. However, recent evidence suggests that SARS-CoV-2 binds to DPP4/CD26 after entering airway cells. It appears that the interaction between the peak glycoprotein SARS-CoV-2 and human DPP4/CD26 (also known as dipeptidyl peptidase-4 (DPP4) is a key factor in sequestration and virulence. In the absence of results from well-designed randomized clinical trials, the efficacy or safety data of DPP4 inhibitors in the treatment of COVID-19 must be interpreted with caution and no clear conclusions can be drawn.The results of these studies may help reveal the impact of using drugs that inhibit DPP4 and whether they can be effective in the treatment of COVID-19 infection.
publishDate 2021
dc.date.none.fl_str_mv 2021-10-17
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv https://rsdjournal.org/index.php/rsd/article/view/21361
10.33448/rsd-v10i13.21361
url https://rsdjournal.org/index.php/rsd/article/view/21361
identifier_str_mv 10.33448/rsd-v10i13.21361
dc.language.iso.fl_str_mv por
language por
dc.relation.none.fl_str_mv https://rsdjournal.org/index.php/rsd/article/view/21361/19048
dc.rights.driver.fl_str_mv https://creativecommons.org/licenses/by/4.0
info:eu-repo/semantics/openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/4.0
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Research, Society and Development
publisher.none.fl_str_mv Research, Society and Development
dc.source.none.fl_str_mv Research, Society and Development; Vol. 10 No. 13; e415101321361
Research, Society and Development; Vol. 10 Núm. 13; e415101321361
Research, Society and Development; v. 10 n. 13; e415101321361
2525-3409
reponame:Research, Society and Development
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instname_str Universidade Federal de Itajubá (UNIFEI)
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institution UNIFEI
reponame_str Research, Society and Development
collection Research, Society and Development
repository.name.fl_str_mv Research, Society and Development - Universidade Federal de Itajubá (UNIFEI)
repository.mail.fl_str_mv rsd.articles@gmail.com
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