Disease relevance of L2

• Expression of the highly immunogenic capsid proteins, L1 and L2, is restricted to only the most differentiated cells, where immune surveillance is limited [1].
• HPV1a L1- and L2-encoded polypeptides expressed in Saccharomyces cerevisiae and by in vitro translation were equivalent in size to the major and minor virion capsid proteins, respectively [2].
• By analysing 3'-deletion mutants of the HPV-16 LUR, we identified 78 bp within the sequence between the E5 and L2 ORFs to be critical for the promoter activity [3].
• Using stand-specific probes synthesized from subgenomic fragments of the HPV-6 genome in conjunction with nuclease digestions, we were able to demonstrate that HPV-6 transcripts specific to open reading frames (ORFs) E6, E7, E1, L1, and L2 occur in maturing superficial cells [4].

High impact information on L2

• HPV11 L2 contains two nuclear localization signals (NLSs)-in the N terminus and the C terminus-that could mediate its nuclear import via a classical pathway [5].
• The minor capsid protein L2 contributes to two steps in the human papillomavirus type 31 life cycle [6].
• Late genes encode E1-E4, a cytosolic protein, and capsid proteins L1 and L2 [7].
• Expression of the human papillomavirus (HPV) capsid genes, L1 and L2, as well as amplification of viral DNA and virion assembly occur in the terminally differentiated layers of infected stratified squamous epithelium in vivo [8].
• One RNA species originating from a novel HPV promoter in the upstream regulatory region has the potential to encode the minor capsid protein L2 [9].

Biological context of L2

• The regulation of human papillomavirus (HPV) late gene expression is difficult to analyse because the late proteins L1 and L2 are only produced in the upper layers of terminally differentiated keratinocytes [3].
• In order to dissect L2 domains involved in nuclear translocation, ND10 homing, loss of Sp100, and recruitment of Daxx, a detailed deletion mutagenesis of L2 was performed [10].

Anatomical context of L2

• Among the viral proteins expressed in differentiated epithelial cells are the viral capsid proteins, L1 and L2, as well as the E1E4 fusion proteins [11].

Associations of L2 with chemical compounds

• The organization of epitopes on the minor capsid protein L2 of human papillomavirus (HPV) type 33 has been analysed using three monoclonal antibodies (MAbs) generated against a large fragment of the L2 protein (amino acids 82-259) expressed as a glutathione S-transferase fusion protein [12].

Other interactions of L2

• Anti-DDV antiserum contained type-specific HPV1 L1-reactive and HPV1 L2-reactive antibodies [2].

Analytical, diagnostic and therapeutic context of L2

• Dissection of human papillomavirus type 33 L2 domains involved in nuclear domains (ND) 10 homing and reorganization [10].
• Using immunofluorescence and green fluorescent protein fusions, we have identified two nuclear localization signals (NLS) in the central and C-terminal part of L2, respectively, homologous to previously identified NLS in HPV6B L2 (Sun et al., 1995) [10].

References