Characterization of a human papillomavirus type 16 variant-dependent neutralizing epitope

R. B.S. Roden; A. Armstrong; P. Haderer; N. D. Christensen; N. L. Hubbert; D. R. Lowy; J. T. Schiller; R. Kirnbauer

doi:10.1128/jvi.71.8.6247-6252.1997

Characterization of a human papillomavirus type 16 variant-dependent neutralizing epitope

R. B.S. Roden, A. Armstrong, P. Haderer, N. D. Christensen, N. L. Hubbert, D. R. Lowy, J. T. Schiller, R. Kirnbauer

Research output: Contribution to journal › Article › peer-review

106 Scopus citations

Abstract

We have determined that three type-specific and conformationally dependent monoclonal antibodies, H16.E70, H16.U4, and H16.V5, neutralize pseudotype human papillomavirus type 16 (HPV16) virions in vitro. H16.U4 and H16.V5 neutralized pseudotype virions derived from the German HPV16 variant 114K and the Zairian variant Z-1194 with equal efficiency. In contrast, neutralization of Z-1194 pseudotype virions by H16.E70 was two orders of magnitude weaker than neutralization of 114K pseudotype virions. This difference correlated with enzyme-linked immunosorbent assay reactivity of H16.E70 to L1 virus-like particles of the two variants. A substitution at residue 282 of L1 was responsible for this differential reactivity, suggesting that this residue constitutes part of the H16. E70 epitope.

Original language	English (US)
Pages (from-to)	6247-6252
Number of pages	6
Journal	Journal of virology
Volume	71
Issue number	8
DOIs	https://doi.org/10.1128/jvi.71.8.6247-6252.1997
State	Published - 1997
Externally published	Yes

ASJC Scopus subject areas

Microbiology
Immunology
Insect Science
Virology

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10.1128/jvi.71.8.6247-6252.1997

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title = "Characterization of a human papillomavirus type 16 variant-dependent neutralizing epitope",

abstract = "We have determined that three type-specific and conformationally dependent monoclonal antibodies, H16.E70, H16.U4, and H16.V5, neutralize pseudotype human papillomavirus type 16 (HPV16) virions in vitro. H16.U4 and H16.V5 neutralized pseudotype virions derived from the German HPV16 variant 114K and the Zairian variant Z-1194 with equal efficiency. In contrast, neutralization of Z-1194 pseudotype virions by H16.E70 was two orders of magnitude weaker than neutralization of 114K pseudotype virions. This difference correlated with enzyme-linked immunosorbent assay reactivity of H16.E70 to L1 virus-like particles of the two variants. A substitution at residue 282 of L1 was responsible for this differential reactivity, suggesting that this residue constitutes part of the H16. E70 epitope.",

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AU - Roden, R. B.S.

AU - Armstrong, A.

AU - Haderer, P.

AU - Christensen, N. D.

AU - Hubbert, N. L.

AU - Lowy, D. R.

AU - Schiller, J. T.

AU - Kirnbauer, R.

PY - 1997

Y1 - 1997

N2 - We have determined that three type-specific and conformationally dependent monoclonal antibodies, H16.E70, H16.U4, and H16.V5, neutralize pseudotype human papillomavirus type 16 (HPV16) virions in vitro. H16.U4 and H16.V5 neutralized pseudotype virions derived from the German HPV16 variant 114K and the Zairian variant Z-1194 with equal efficiency. In contrast, neutralization of Z-1194 pseudotype virions by H16.E70 was two orders of magnitude weaker than neutralization of 114K pseudotype virions. This difference correlated with enzyme-linked immunosorbent assay reactivity of H16.E70 to L1 virus-like particles of the two variants. A substitution at residue 282 of L1 was responsible for this differential reactivity, suggesting that this residue constitutes part of the H16. E70 epitope.

AB - We have determined that three type-specific and conformationally dependent monoclonal antibodies, H16.E70, H16.U4, and H16.V5, neutralize pseudotype human papillomavirus type 16 (HPV16) virions in vitro. H16.U4 and H16.V5 neutralized pseudotype virions derived from the German HPV16 variant 114K and the Zairian variant Z-1194 with equal efficiency. In contrast, neutralization of Z-1194 pseudotype virions by H16.E70 was two orders of magnitude weaker than neutralization of 114K pseudotype virions. This difference correlated with enzyme-linked immunosorbent assay reactivity of H16.E70 to L1 virus-like particles of the two variants. A substitution at residue 282 of L1 was responsible for this differential reactivity, suggesting that this residue constitutes part of the H16. E70 epitope.

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Characterization of a human papillomavirus type 16 variant-dependent neutralizing epitope

Abstract

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