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Protein Science, Vol 1, Issue 9 1154-1161, Copyright © 1992 by Cold Spring Harbor Laboratory Press

ARTICLE

Three-dimensional structure of the Fab fragment of a neutralizing antibody to human rhinovirus serotype 2

J. TORMO, E. STADLER, T. SKERN, H. AUER, O. KANZLER, C. BETZEL, D. BLAAS and I. FITA
Department d'Enginyeria Quimica, Escola Tecnica Superior d'Enginyers Industrials, E-08028 Barcelona, Spain

The crystal structure of the antigen-binding fragment of a monoclonal antibody (8F5) that neutralizes human rhinovirus serotype 2 has been determined by X-ray diffraction studies. Antibody 8F5, obtained by immunization with native HRV2 virions, cross-reacts with peptides of the viral capsid protein VP2, which contribute to the neutralizing immunogenic site B in this serotype. The structure was solved by the molecular replacement method and has been refined to an R-factor of 18.9% at 2.8 A resolution. The elbow angle, relating the variable and constant modules of the molecule is 127{deg}, representing the smallest elbow angle observed so far in an Fab fragment. Furthermore, the charged residues of the epitope can be well accommodated in the antigen-binding site. This is the first crystal structure reported for an antibody directed against an icosahedral virus.
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