Amino acids 15-28 in the ectodomain of SARS coronavirus 3a protein induces neutralizing antibodies.
Identifieur interne : 002200 ( PubMed/Corpus ); précédent : 002199; suivant : 002201Amino acids 15-28 in the ectodomain of SARS coronavirus 3a protein induces neutralizing antibodies.
Auteurs : Sara Akerström ; Yee-Joo Tan ; Ali MirazimiSource :
- FEBS letters [ 0014-5793 ] ; 2006.
English descriptors
- KwdEn :
- Amino Acids (immunology), Animals, Antibodies, Viral (immunology), Binding Sites, Antibody, COS Cells, Chlorocebus aethiops, Epitopes (chemistry), Epitopes (immunology), Humans, Neutralization Tests, Protein Structure, Tertiary, Rabbits, SARS Virus (immunology), Viral Proteins (chemistry), Viral Proteins (immunology).
- MESH :
- chemical , chemistry : Epitopes, Viral Proteins.
- chemical , immunology : Amino Acids, Antibodies, Viral, Epitopes, Viral Proteins.
- immunology : SARS Virus.
- Animals, Binding Sites, Antibody, COS Cells, Chlorocebus aethiops, Humans, Neutralization Tests, Protein Structure, Tertiary, Rabbits.
Abstract
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.
DOI: 10.1016/j.febslet.2006.06.002
PubMed: 16781713
Links to Exploration step
pubmed:16781713Le document en format XML
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<author><name sortKey="Akerstrom, Sara" sort="Akerstrom, Sara" uniqKey="Akerstrom S" first="Sara" last="Akerström">Sara Akerström</name>
<affiliation><nlm:affiliation>Center for Microbiological Preparedness, Swedish Institute for Infectious Disease Control, SE-171 82 Solna, Sweden.</nlm:affiliation>
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<author><name sortKey="Tan, Yee Joo" sort="Tan, Yee Joo" uniqKey="Tan Y" first="Yee-Joo" last="Tan">Yee-Joo Tan</name>
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<author><name sortKey="Mirazimi, Ali" sort="Mirazimi, Ali" uniqKey="Mirazimi A" first="Ali" last="Mirazimi">Ali Mirazimi</name>
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<author><name sortKey="Tan, Yee Joo" sort="Tan, Yee Joo" uniqKey="Tan Y" first="Yee-Joo" last="Tan">Yee-Joo Tan</name>
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<author><name sortKey="Mirazimi, Ali" sort="Mirazimi, Ali" uniqKey="Mirazimi A" first="Ali" last="Mirazimi">Ali Mirazimi</name>
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<term>Binding Sites, Antibody</term>
<term>COS Cells</term>
<term>Chlorocebus aethiops</term>
<term>Epitopes (chemistry)</term>
<term>Epitopes (immunology)</term>
<term>Humans</term>
<term>Neutralization Tests</term>
<term>Protein Structure, Tertiary</term>
<term>Rabbits</term>
<term>SARS Virus (immunology)</term>
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<term>Viral Proteins (immunology)</term>
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<term>Viral Proteins</term>
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<term>Epitopes</term>
<term>Viral Proteins</term>
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<front><div type="abstract" xml:lang="en">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.</div>
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<Abstract><AbstractText>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.</AbstractText>
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