Nucleotide sequence of the HPV16 L1 open reading frame

Parton, A.

doi:10.1093/nar/18.12.3631

Cited by 13 publications

(10 citation statements)

References 3 publications

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“…HPV-16 nucleotide position numbering. HPV-16 DNA nucleotide positions are numbered according to the published sequence of the reference clone (53), but revised to include corrections reported by Bubb et al (6), Halbert and Galloway (19), and Parton (47). As in our earlier work on HPV-16 variants (70), we have included an additional correction, replacing the published GC at position 7432 with CGG, communicated to us by Bernard (4) and observed in the LCR sequences of our HPV-16 isolates.…”

Section: Methodsmentioning

confidence: 99%

Human papillomavirus type 16 sequence variants: identification by E6 and L1 lineage-specific hybridization

et al. 1997

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A catalog of human papillomavirus (HPV) type 16 (HPV-16) E6 and L1 signature nucleotides was used to develop PCR-based oligonucleotide probe systems capable of distinguishing HPV-16 class and subclass variants. Twenty-three E6-specific oligonucleotide probes targeting 13 variant nucleotide positions and 12 L1specific oligonucleotide probes targeting 6 variant nucleotide positions were used to characterize HPV-16containing cervicovaginal lavage specimens. Nucleotide positions that could be distinguished included E6

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Section: Methodsmentioning

confidence: 99%

Human papillomavirus type 16 sequence variants: identification by E6 and L1 lineage-specific hybridization

et al. 1997

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“…Sequencing was carried out for the vector-HPV junctions and, for HPV16, the entire Li and L2 ORFs of the baculovirus vectors. Numbering refers to the prototype HPV16 sequence, which is not corrected for the missing T at nt 3903 in the E5 ORF (8) and for the sequencing errors in the Li ORF (14). Recombinant baculovirus stocks were generated by cotransfection with baculovirus DNA (Baculo-Gold; PharMingen, San Diego, Calif.), by using lipofectin (GIBCO/BRL, Gaithersburg, Md.…”

Section: Methodsmentioning

confidence: 99%

Efficient self-assembly of human papillomavirus type 16 L1 and L1-L2 into virus-like particles

Kirnbauer

Taub

Greenstone

et al. 1993

J Virol

548

190

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The L1 genes of two human papillomavirus type 16 (HPV16) isolates derived from condylomata acuminata were used to express the L1 major capsid protein in insect cells via recombinant baculoviruses. Both L1 major capsid proteins self-assembled into virus-like particles (VLP) with high efficiency and could be purified in preparative amounts on density gradients. The yield of VLP was 3 orders of magnitude higher than what has been obtained previously, using L1 derived from the prototype HPV16. DNA sequence comparison identified a single nonconserved amino acid change to be responsible for the inefficient self-assembly of the prototype L1. VLP were also obtained by expressing L1 of HPV6, HPV11, and cottontail rabbit papillomavirus, indicating that L1 from a variety of papillomaviruses has the intrinsic capacity to self-assemble into VLP. Coexpression of HPV16 L1 plus L2 by using a baculovirus double-expression vector also resulted in efficient self-assembly of VLP, and the average particle yield increased about fourfold in comparison to when L1 only was expressed. Coimmunoprecipitation of L1 and L2 and cosedimentation of the two proteins in a sucrose gradient demonstrated that L2 was incorporated into the particles. The ability to generate preparative amounts of HPV16 L1 and L1-L2 VLP may have implications for the development of a serological assay to detect anti-HPV16 virion immune responses to conformational epitopes and for immunoprophylaxis against HPV16 infection.

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“…Such an approach has been previously used for identification of HPV16 molecular variants (Chan et al, 1992a). The numbering of the sequences below corresponds to the published sequence (Seedorf et al, 1985; GenBank accession (Halbert & Galloway, 1988), and sequencing errors in the L1 and L20RFs (Parton, 1990;Xi & Banks, 1991). In the L1 genes the majority of changes found were silent (at positions 6152, 6188, 6389, 6860 and 7058) or induced conservative amino acid (aa) changes (Table 1).…”

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confidence: 99%

Sequence variation in the capsid protein genes of human papillomavirus type 16

Pushko

Sasagawa

Cuzick

et al. 1994

Journal of General Virology

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We have cloned and sequenced the L1 and L2 genes from human papillomavirus type 16 (HPV16) DNA-containing cervical cytology samples collected from the U.K. and Trinidad. Samples containing high copy numbers of HPV16 DNA were selected as being likely to contain fully functional virus DNA molecules in an episomal state, rather than in an integrated and possibly altered state. In comparison with the previously published sequence of HPV16 isolated from an invasive cancer a variety of differences were detected in both L1 and L2. The pattern of changes appears to be different in samples from the two geographic regions. One of the differences (resulting in D at position 202 of the L1 protein) reported recently to be functionally important for virus particle assembly was found to occur in all the samples examined. Variations in LI found within known immunoreactive regions or hydrophobic domains should be taken into account in design of prophylactic vaccines for HPV16 based on virus-like particles. All variations within L2 protein were found in hydrophilic domains in the carboxy-terminal half of L2. These positions were highly variable among other types ofpapillomavirus and are located outside the known L2 immunoreactive region. Infection of the human cervix with human papilloma-virus type 16 (HPV 16) is strongly associated with cervical cancer (Diirst et al., 1983; Fuchs et al., 1988). The main targets for potential prophylactic vaccines against HPV16 would be the major (L1) and minor (L2) coat proteins of the viral particle (for a review, see Crawford, 1993). Papillomavirus particles are T = 7 icosahedral structures composed of 72 pentameric capsomers of the major coat protein L1 (Baker et al., 1991). Both L1 and L2 are products of virus iate genes directing the synthesis of coat proteins in the superficial cell layers of the cervix which then undergo assembly into progeny virions in nuclei of dying cells. Unlike low-risk HPV types (such as HPV6 and-ii) HPV16 produces low yields of virus particles even in naturally occurring lesions. Therefore, virus-like particles that are candidates for antiviral vaccines have been produced by recombinant vaccinia virus vectors (Zhou et al., 1991) and baculovirus vectors (Xi & Banks, 1991; Kirnbauer et al,, 1993). However, yields of these particles have generally been low. This may be either intrinsic to HPVI6 or a consequence of the sequence of the virus DNA as initially isolated (Dfirst et t Permanent address: Institute of Molecular Biology, 53 Krustpils Street, Riga LV1065, Latvia. al., 1983). Since the cloned DNA most widely used came from an invasive cancer rather than from a lesion producing virus particles, there is no guarantee that the L1 and L2 genes were functional in this isolate, i.e. capable of generating proteins that can assemble correctly to give infectious virus particles. In order to identify the consensus genotype(s) of HPV 16 L1 and L2 occurring in high copy number lesions of infected individuals, we cloned and sequenced the L1 and L2 genes from HPV16 DNA-contain...

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Nucleotide sequence of the HPV16 L1 open reading frame

Cited by 13 publications

References 3 publications

Human papillomavirus type 16 sequence variants: identification by E6 and L1 lineage-specific hybridization

Human papillomavirus type 16 sequence variants: identification by E6 and L1 lineage-specific hybridization

Efficient self-assembly of human papillomavirus type 16 L1 and L1-L2 into virus-like particles

Sequence variation in the capsid protein genes of human papillomavirus type 16

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