Neutralization epitopes of human rhinovirus type 2

Appleyard, G.; Russell, S. M.; Clarke, Berwyn; Speller, S. A.; Trowbridge, M.; Vadolas, Jim

doi:10.1099/0022-1317-71-6-1275

Cited by 52 publications

(58 citation statements)

References 22 publications

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“…This group raised approximately 250 MAbs to peptides representing an antigenic site on poliovirus type 3, but found that the vast majority were peptide-specific, and the two that bound to virus did not recognize immobilized peptide. Conversely, all of the anti-viral MAbs raised to HRV2 by Appleyard et al (1990) were specific for virus particles (S. Russell, personal communication) as they were directed against conformational determinants. The only anti-HRV2 antibody that also bound peptide was the 8F5 MAb described by Skern et al (1987).…”

Section: Discussionmentioning

confidence: 99%

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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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Section: Discussionmentioning

confidence: 99%

“…HRV2 was obtained from the MRC Common Cold Research Unit, Salisbury, U.K., grown in HeLa (OH5) cells and plaque-purified as previously reported (Appleyard et al, 1990). Virus used for neutralization assays was stored as clarified tissue culture harvest in an equal volume of glycerol at -20 °C.…”

Section: Methodsmentioning

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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“…These data define four neutralizing immunogenic sites (NIm-Ia, Ib, 11, and 111) for HRV14 (Sherry et al, 1986), and three (designated A, B, and C) for HRV2 (Appleyard et al, 1990). Site A and B correspond to NIm-IA and NIm-11; however, whereas in HRV14 VP2 contributes most of the amino acid residues to NIm-11, in HRV2 VP1 is primarily involved in the architecture of site B.…”

mentioning

confidence: 91%

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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“…These are referred to as NIm Ia, NIm Ib, NIm II and NIm III, according to the viral protein on which they are principally located. Sites corresponding to, but significantly different from, NIm Ia and NIm II also appear on human rhinovirus serotype 2 (HRV-2) (Appleyard et al, 1990). Synthetic peptides representing linear portions of the protein sequence of HRV-2 have previously been shown to be recognized by antisera raised against HRV-2 (Francis et al, 1987a).…”

mentioning

confidence: 99%

Neutralizing Antibodies to Human Rhinovirus Produced in Laboratory Animals and Humans that Recognize a Linear Sequence from VP2

Hastings

Speller²,

Francis³

1990

Journal of General Virology

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Synthetic peptides representing amino acids 156 to 170 of virus capsid protein VP2 from human rhinovirus (HRV) type 2 have previously been used to elicit a neutralizing antibody response; polyclonal antisera against this peptide have been compared with a virusneutralizing monoclonal antibody (8F5) which recognizes the same linear sequence. The neutralizing activity of both antibodies against virus is abolished by an amino acid substitution in VP2 at position 163 but only the peptide antiserum neutralizing activity is affected by a change in VP2 at position 158. The minimal binding site of 8F5 has been mapped, using overlapping peptides, to a sequence TRLNPD covering VP2 residues 160 to 165. Using affinity purification it has been shown that 8 to 10% of total neutralizing activity of polyclonal rabbit or guinea-pig antivirus antiserum is due to recognition of this linear VP2 156 to 170 determinant. Furthermore, a similar population of neutralizing antibodies appears to be associated with an immune response to recent HRV infection in humans. These results confirm the existence of linear determinants on the surface of HRV which may be mimicked by suitable synthetic peptides.

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Neutralization epitopes of human rhinovirus type 2

Cited by 52 publications

References 22 publications

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

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

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

Neutralizing Antibodies to Human Rhinovirus Produced in Laboratory Animals and Humans that Recognize a Linear Sequence from VP2

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