Correlation of DPP4 enzyme with SARS-CoV-2 infection
Autor(a) principal: | |
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Data de Publicação: | 2021 |
Outros Autores: | , , , , , , , , , , , , , , , , , |
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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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 |
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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 instname:Universidade Federal de Itajubá (UNIFEI) instacron:UNIFEI |
instname_str |
Universidade Federal de Itajubá (UNIFEI) |
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UNIFEI |
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UNIFEI |
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Research, Society and Development |
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Research, Society and Development |
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Research, Society and Development - Universidade Federal de Itajubá (UNIFEI) |
repository.mail.fl_str_mv |
rsd.articles@gmail.com |
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1797052692162412544 |