Preparation and characterization of a novel monoclonal antibody specific to severe acute respiratory syndrome-coronavirus nucleocapsid protein.
Identifieur interne : 002107 ( PubMed/Curation ); précédent : 002106; suivant : 002108Preparation and characterization of a novel monoclonal antibody specific to severe acute respiratory syndrome-coronavirus nucleocapsid protein.
Auteurs : Gu-Choul Shin [Corée du Sud] ; Yoon-Seok Chung ; In-Soo Kim ; Hae-Wol Cho ; Chun KangSource :
- Virus research [ 0168-1702 ] ; 2006.
Descripteurs français
- KwdFr :
- Affinité des anticorps, Animaux, Anticorps antiviraux (immunologie), Anticorps antiviraux (isolement et purification), Anticorps monoclonaux (immunologie), Anticorps monoclonaux (isolement et purification), Antigènes viraux (immunologie), Cartographie épitopique, Humains, Immunotransfert, Lignée cellulaire, Protéines nucléocapside (immunologie), Réactions croisées, Souris, Test ELISA, Virus du SRAS (immunologie), Épitopes (immunologie).
- MESH :
- immunologie : Anticorps antiviraux, Anticorps monoclonaux, Antigènes viraux, Protéines nucléocapside, Virus du SRAS, Épitopes.
- isolement et purification : Anticorps antiviraux, Anticorps monoclonaux.
- Affinité des anticorps, Animaux, Cartographie épitopique, Humains, Immunotransfert, Lignée cellulaire, Réactions croisées, Souris, Test ELISA.
English descriptors
- KwdEn :
- Animals, Antibodies, Monoclonal (immunology), Antibodies, Monoclonal (isolation & purification), Antibodies, Viral (immunology), Antibodies, Viral (isolation & purification), Antibody Affinity, Antigens, Viral (immunology), Cell Line, Cross Reactions, Enzyme-Linked Immunosorbent Assay, Epitope Mapping, Epitopes (immunology), Humans, Immunoblotting, Mice, Nucleocapsid Proteins (immunology), SARS Virus (immunology).
- MESH :
- chemical , immunology : Antibodies, Monoclonal, Antibodies, Viral, Antigens, Viral, Epitopes, Nucleocapsid Proteins.
- chemical , isolation & purification : Antibodies, Monoclonal, Antibodies, Viral.
- immunology : SARS Virus.
- Animals, Antibody Affinity, Cell Line, Cross Reactions, Enzyme-Linked Immunosorbent Assay, Epitope Mapping, Humans, Immunoblotting, Mice.
Abstract
Severe acute respiratory syndrome-coronavirus nucleocapsid (SARS-CoV N) protein has been found to be important to the processes related to viral pathogenesis, such as virus replication, interference of the cell process and modulation of host immune response; detection of the antigen has been used for the early diagnosis of infection. We have used recombinant N protein expressed in insect cells to generate 17 mAbs directed against this protein. We selected five mAbs that could be used in various diagnostic assays, and all of these mAbs recognized linear epitopes. Three IgG(2b) mAbs were recognized within the N-terminus of N protein, whereas the epitope of two IgG(1) mAbs localized within the C-terminus. These mAbs were found to have significant reactivity with both non-phosphorylated and phosphorylated N proteins, which resulted in high reactivity with native N protein in virus-infected cells; however, they did not show cross-reactivity with human coronavirus. Therefore, these results suggested that these mAbs would be useful in the development of various diagnostic kits and in future studies of SARS-CoV pathology.
DOI: 10.1016/j.virusres.2006.07.004
PubMed: 16942813
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pubmed:16942813Le document en format XML
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<front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome-coronavirus nucleocapsid (SARS-CoV N) protein has been found to be important to the processes related to viral pathogenesis, such as virus replication, interference of the cell process and modulation of host immune response; detection of the antigen has been used for the early diagnosis of infection. We have used recombinant N protein expressed in insect cells to generate 17 mAbs directed against this protein. We selected five mAbs that could be used in various diagnostic assays, and all of these mAbs recognized linear epitopes. Three IgG(2b) mAbs were recognized within the N-terminus of N protein, whereas the epitope of two IgG(1) mAbs localized within the C-terminus. These mAbs were found to have significant reactivity with both non-phosphorylated and phosphorylated N proteins, which resulted in high reactivity with native N protein in virus-infected cells; however, they did not show cross-reactivity with human coronavirus. Therefore, these results suggested that these mAbs would be useful in the development of various diagnostic kits and in future studies of SARS-CoV pathology.</div>
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