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Cross-reactivity of antibody against SARS-coronavirus nucleocapsid protein with IL-11.

ABSTRACT: Infection of SARS-associated coronavirus (SARS-CoV) induced a strong anti-nucleocapsid (anti-N) antibody response. However, the pathophysiological significance of the anti-N antibodies in SARS pathogenesis is largely unknown. To profile the anti-N antibodies, a phage-displayed scFv library was prepared from mice immunized with heat-inactivated SARS-CoV-infected Vero E6 cell lysate. Specific anti-N scFvs were isolated by panning against a recombinant nucleocapsid protein and reactivity was confirmed with phage-ELISA. Sequence analysis indicated that two of the isolated anti-N scFv clones were identical and displayed a high homology with an scFv specific for interleukin 11 (IL-11), an anti-inflammatory cytokine derived from bone marrow stroma cells. In a neutralization assay, IL-11-induced STAT 3 phosphorylation in rat intestinal epithelial IEC-18 cells was completely suppressed by the anti-N scFv clone L9N01.

SUBMITTER: Cheng M 

PROVIDER: S-EPMC7092895 | biostudies-literature | 2005 Dec

REPOSITORIES: biostudies-literature

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Cross-reactivity of antibody against SARS-coronavirus nucleocapsid protein with IL-11.

Cheng Man M   Chan Ceci W L CW   Cheung Randy C F RC   Bikkavilli Rama Kamesh RK   Zhao Qi Q   Au Shannon W N SW   Chan Paul K S PK   Lee Susanna S T SS   Cheng Gregory G   Ho Walter K K WK   Cheung Wing-Tai WT  

Biochemical and biophysical research communications 20051025 3

Infection of SARS-associated coronavirus (SARS-CoV) induced a strong anti-nucleocapsid (anti-N) antibody response. However, the pathophysiological significance of the anti-N antibodies in SARS pathogenesis is largely unknown. To profile the anti-N antibodies, a phage-displayed scFv library was prepared from mice immunized with heat-inactivated SARS-CoV-infected Vero E6 cell lysate. Specific anti-N scFvs were isolated by panning against a recombinant nucleocapsid protein and reactivity was confir  ...[more]

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