A Neutralizing Epitope on Human Rhinovirus Type 2 Includes Amino Acid Residues between 153 and 164 of Virus Capsid Protein VP2

Skern, Tim; Neubauer, Christoph; Frasel, Lela; Gründler, Peter; Sommergruber, Wolfgang; Zorn, Manfred; Kuechler, Ernst; Blaas, Dieter

doi:10.1099/0022-1317-68-2-315

Cited by 63 publications

(42 citation statements)

References 20 publications

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“…The preparation of murine monoclonal antibody 8F5 (IgG2a, K ) , and the production, purification, and crystallization of its Fab fragment have been published (Skern et al, 1987;Tormo et al, 1990).…”

Section: Preparation and Crystallization Of The Fab Fragmentmentioning

confidence: 99%

“…One such antibody (8F5), raised against native virions, was found to bind not only to the viral particle in its native conformation, but also to the viral protein VP2 on Western blots. This property was used to define the region of the binding site by bacterial expression of various deletion mutants of VP2; the binding site lies between residues 153 and 164 (Skern et al, 1987). This polypeptide segment is located in the region of site B and is analogous to the Nim-I1 antigenic site on HRV14, which appears as a "puff" on the viral particle surface between strands PE and PF of the eight-stranded &barrel (Kinemage 4; Rossmann et al, 1985).…”

mentioning

confidence: 99%

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

Tormo¹,

Stadler²,

Skern³

et al. 1992

Protein Science

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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 Å resolution. The elbow angle, relating the variable and constant modules of the molecule is 127°, 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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Section: Preparation and Crystallization Of The Fab Fragmentmentioning

confidence: 99%

mentioning

confidence: 99%

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

Tormo¹,

Stadler²,

Skern³

et al. 1992

Protein Science

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show abstract

“…2A right pa nel). It is likely that the 39 kDa band common to each RV preparation is VP1 since it has been shown previously to migrate at this molecular weight (Skern et al, 1987). To confirm the presence of antibodies against VP1 in sera from mice infected twice with RV1B we performed ELISA using purified recombinant VP1 from RV serotypes RV14 and RV89 (Edlmayr et al, 2011) as the antigen since recombinant VP1 from RV1B was unavailable.…”

Section: Rv Capsid Protein Vp1 Is a Major Antibody Targetmentioning

confidence: 99%

Rhinovirus infections and immunisation induce cross-serotype reactive antibodies to VP1

et al. 2012

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“…ND, not determined. recognizing a linear sequence from the same region of VP2 as the anti-peptide MAbs (Skern et al, 1987) were included in this study.…”

Section: Functional Affinity Measurementsmentioning

confidence: 99%

Characterization of monoclonal antibodies raised against a synthetic peptide capable of inducing a neutralizing response to human rhinovirus type 2

Barnett

Rowlands

Parry

1993

Journal of General Virology

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Synthetic peptides incorporating the derived amino acid sequence of VP2 residues 156 to 170 of human rhinovirus type 2 (HRV2) have previously been shown to elicit antibodies that neutralize virus infectivity. The proportion of virus-reactive antibodies present in polyclonal antisera to these peptides is, however, very low. Moreover, neutralization titrations of such antisera correlate poorly with other assays of either anti-virus or anti-peptide activity, suggesting the presence of antibodies with different specificities. To investigate these findings further, we produced a panel of monoclonal antibodies (MAbs) to VP2 peptides of residues 156 to 170 and characterized their reactions with a range of antigens in ELISA, precipitation and neutralization titrations. All the MAbs obtained recognized the homologous peptide, but could be divided into four main reaction groups according to their specificity for viral antigens. Antibodies in the first group recognized and neutralized native virus, apparently by preventing attachment to cells. A second group of MAbs bound to intact particles with similar affinities to the first group, but failed to neutralize infectivity. Antibodies in the third group recognized virus only after capsid distortions incurred by heating or by previous reaction with polyclonal antibodies. The fourth group comprised MAbs that were mainly peptide-specific. Some possible applications of anti-peptide MAbs to improving the design of peptide immunogens are considered.

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A Neutralizing Epitope on Human Rhinovirus Type 2 Includes Amino Acid Residues between 153 and 164 of Virus Capsid Protein VP2

Cited by 63 publications

References 20 publications

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

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

Rhinovirus infections and immunisation induce cross-serotype reactive antibodies to VP1

Characterization of monoclonal antibodies raised against a synthetic peptide capable of inducing a neutralizing response to human rhinovirus type 2

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