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Expression of feline angiotensin converting enzyme 2 and its interaction with SARS-CoV S1 protein

Feline angiotensin converting enzyme 2 (fACE2) gene was amplified from domestic cat lung with RT-PCR, cloned and sequenced. The complete coding region is 2418 bp in length and is the closest to human ACE2 among known ACE2 homologs of non-primate animals. The N terminal fragment 19– 367 aa was expres...

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Detalles Bibliográficos
Autores principales: Guo, Hongyan, Guo, Aizhen, Wang, Chong, Yan, Bangfen, Lu, Haisong, Chen, Huanchun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Ltd. 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7111849/
https://www.ncbi.nlm.nih.gov/pubmed/17658563
http://dx.doi.org/10.1016/j.rvsc.2007.05.011
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author Guo, Hongyan
Guo, Aizhen
Wang, Chong
Yan, Bangfen
Lu, Haisong
Chen, Huanchun
author_facet Guo, Hongyan
Guo, Aizhen
Wang, Chong
Yan, Bangfen
Lu, Haisong
Chen, Huanchun
author_sort Guo, Hongyan
collection PubMed
description Feline angiotensin converting enzyme 2 (fACE2) gene was amplified from domestic cat lung with RT-PCR, cloned and sequenced. The complete coding region is 2418 bp in length and is the closest to human ACE2 among known ACE2 homologs of non-primate animals. The N terminal fragment 19– 367 aa was expressed in Escherishia coli. Both Western blotting and ELISA demonstrated that fACE2 could react with SARS-CoV S1 protein as efficiently as ACE2 of Vero E6 cells did.
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spelling pubmed-71118492020-04-02 Expression of feline angiotensin converting enzyme 2 and its interaction with SARS-CoV S1 protein Guo, Hongyan Guo, Aizhen Wang, Chong Yan, Bangfen Lu, Haisong Chen, Huanchun Res Vet Sci Article Feline angiotensin converting enzyme 2 (fACE2) gene was amplified from domestic cat lung with RT-PCR, cloned and sequenced. The complete coding region is 2418 bp in length and is the closest to human ACE2 among known ACE2 homologs of non-primate animals. The N terminal fragment 19– 367 aa was expressed in Escherishia coli. Both Western blotting and ELISA demonstrated that fACE2 could react with SARS-CoV S1 protein as efficiently as ACE2 of Vero E6 cells did. Elsevier Ltd. 2008-06 2007-07-20 /pmc/articles/PMC7111849/ /pubmed/17658563 http://dx.doi.org/10.1016/j.rvsc.2007.05.011 Text en Copyright © 2007 Elsevier Ltd. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.
spellingShingle Article
Guo, Hongyan
Guo, Aizhen
Wang, Chong
Yan, Bangfen
Lu, Haisong
Chen, Huanchun
Expression of feline angiotensin converting enzyme 2 and its interaction with SARS-CoV S1 protein
title Expression of feline angiotensin converting enzyme 2 and its interaction with SARS-CoV S1 protein
title_full Expression of feline angiotensin converting enzyme 2 and its interaction with SARS-CoV S1 protein
title_fullStr Expression of feline angiotensin converting enzyme 2 and its interaction with SARS-CoV S1 protein
title_full_unstemmed Expression of feline angiotensin converting enzyme 2 and its interaction with SARS-CoV S1 protein
title_short Expression of feline angiotensin converting enzyme 2 and its interaction with SARS-CoV S1 protein
title_sort expression of feline angiotensin converting enzyme 2 and its interaction with sars-cov s1 protein
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7111849/
https://www.ncbi.nlm.nih.gov/pubmed/17658563
http://dx.doi.org/10.1016/j.rvsc.2007.05.011
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