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Amino acids 15–28 in the ectodomain of SARS coronavirus 3a protein induces neutralizing antibodies

A synthetic peptide corresponding to amino acids (aa) 15–28 of the severe acute respiratory syndrome coronavirus (SARS‐CoV) 3a protein was used to raise polyclonal antibodies in rabbits. This anti‐3a N‐terminal antibody could detect 3a protein in infected cells, as did an anti‐3a C‐terminal antibody...

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Detalles Bibliográficos
Autores principales: Åkerström, Sara, Tan, Yee-Joo, Mirazimi, Ali
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2006
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7094653/
https://www.ncbi.nlm.nih.gov/pubmed/16781713
http://dx.doi.org/10.1016/j.febslet.2006.06.002
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author Åkerström, Sara
Tan, Yee-Joo
Mirazimi, Ali
author_facet Åkerström, Sara
Tan, Yee-Joo
Mirazimi, Ali
author_sort Åkerström, Sara
collection PubMed
description A synthetic peptide corresponding to amino acids (aa) 15–28 of the severe acute respiratory syndrome coronavirus (SARS‐CoV) 3a protein was used to raise polyclonal antibodies in rabbits. This anti‐3a N‐terminal antibody could detect 3a protein in infected cells, as did an anti‐3a C‐terminal antibody previously described. The latter targeted the C‐terminal cytoplasmic domain of 3a (aa 134–274). The anti‐3a N‐terminal antibody could detect intracellular 3a as well as 3a expressed on the cell surface. Interestingly, only the anti‐3a N‐terminal antibody can inhibit SARS‐CoV propagation in Vero E6 culture although the binding affinity of the anti‐3a N‐terminal antibody was lower than the anti‐3a C‐terminal antibody.
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spelling pubmed-70946532020-03-25 Amino acids 15–28 in the ectodomain of SARS coronavirus 3a protein induces neutralizing antibodies Åkerström, Sara Tan, Yee-Joo Mirazimi, Ali FEBS Lett Short Communications A synthetic peptide corresponding to amino acids (aa) 15–28 of the severe acute respiratory syndrome coronavirus (SARS‐CoV) 3a protein was used to raise polyclonal antibodies in rabbits. This anti‐3a N‐terminal antibody could detect 3a protein in infected cells, as did an anti‐3a C‐terminal antibody previously described. The latter targeted the C‐terminal cytoplasmic domain of 3a (aa 134–274). The anti‐3a N‐terminal antibody could detect intracellular 3a as well as 3a expressed on the cell surface. Interestingly, only the anti‐3a N‐terminal antibody can inhibit SARS‐CoV propagation in Vero E6 culture although the binding affinity of the anti‐3a N‐terminal antibody was lower than the anti‐3a C‐terminal antibody. John Wiley and Sons Inc. 2006-07-10 2006-06-12 /pmc/articles/PMC7094653/ /pubmed/16781713 http://dx.doi.org/10.1016/j.febslet.2006.06.002 Text en FEBS Letters 580 (2006) 1873-3468 © 2015 Federation of European Biochemical Societies This article is being made freely available through PubMed Central as part of the COVID-19 public health emergency response. It can be used for unrestricted research re-use and analysis in any form or by any means with acknowledgement of the original source, for the duration of the public health emergency.
spellingShingle Short Communications
Åkerström, Sara
Tan, Yee-Joo
Mirazimi, Ali
Amino acids 15–28 in the ectodomain of SARS coronavirus 3a protein induces neutralizing antibodies
title Amino acids 15–28 in the ectodomain of SARS coronavirus 3a protein induces neutralizing antibodies
title_full Amino acids 15–28 in the ectodomain of SARS coronavirus 3a protein induces neutralizing antibodies
title_fullStr Amino acids 15–28 in the ectodomain of SARS coronavirus 3a protein induces neutralizing antibodies
title_full_unstemmed Amino acids 15–28 in the ectodomain of SARS coronavirus 3a protein induces neutralizing antibodies
title_short Amino acids 15–28 in the ectodomain of SARS coronavirus 3a protein induces neutralizing antibodies
title_sort amino acids 15–28 in the ectodomain of sars coronavirus 3a protein induces neutralizing antibodies
topic Short Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7094653/
https://www.ncbi.nlm.nih.gov/pubmed/16781713
http://dx.doi.org/10.1016/j.febslet.2006.06.002
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