Antibody responses to human papillomavirus type‐16 infections

Cason, John; Best, Jennifer M.

doi:10.1002/rmv.1980010404

Cited by 7 publications

(1 citation statement)

References 47 publications

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“…However, certain types of human and animal PVs are associated with squamous epithelial cell carcinomas of animals (Sundberg, 1987) and humans (zur Hausen & Schneider, 1987). Antibody studies of PVs associated with cancer have been problematic as it is difficult to obtain sufficient quantities of native viral proteins for immunoassays (Cason & Best, 1991). PVs are difficult to propagate in vitro or in vivo (Meyers et al, 1992;Sterling et al, 1990); precancerous lesions contain few virions and, in cancers, expression of PV capsid proteins may be precluded by PV DNA integration into host DNA (Gissmann & Schwartz, 1986).…”

Section: Introductionmentioning

confidence: 99%

Mapping of linear B cell epitopes on capsid proteins of bovine papillomavirus: identification of three external type-restricted epitopes

Cason¹,

Kambo²,

Jewers³

et al. 1993

Journal of General Virology

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Immunodominant, conserved and type-restricted external epitopes of bovine papillomavirus (BPV) major (L1) capsid protein have been identified using BPV particles and synthetic peptides. Antisera to disrupted BP¥-I recognized BPV-1 and BPV-2 particles in immune electron microscopy (IEM) studies and inhibited BPV-2-induced focus formation of NIH/3T3 cells. Thus BPV-1/BPV-2 cross-reactive epitopes occur on the surface of virions. The L1 protein appeared to be immunodominant as the antisera reacted with three dominant BPV-1/BPV-2 conserved B cell epitopes (amino acids 111 to 125, 131 to 145 and 191 to 205) in Pepscan assays of BPV-1 L1, whereas no common epitopes and less frequent antibody binding to peptides were detected in Pepscans of the L2 protein of BPV-1.Four discrete variable regions were identified in the sequences of L1 proteins of BPV-1 and BPV-2. Antisera against synthetic peptides corresponding to three of the four variable regions (amino acids 42 to 56, 435 to 449 and 485 to 499) of BPV-2 L1 caused clumping of BPV-2, but not of BPV-1, particles as examined by IEM, and antisera to one peptide (amino acids 485 to 499) inhibited BPV-2-induced focus formation of NIH/3T3 cells. These data suggest that these regions are typespecific BPV-2 L1 epitopes and that they occur on the virion surface. Although conformation-dependent epitopes remain to be identified on papillomaviruses, the linear epitopes identified in this study may be worthy of further study as constituents of experimental prophylactic vaccines.

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