Disease relevance of Human papillomavirus 11

• We examined the functions of human papillomavirus type 11 (HPV-11) E1 and E2 proteins purified from Sf9 cells infected with recombinant baculoviruses in cell-free HPV-11 origin (ori) replication [1].
• This study investigated the human c-fos promoter characteristics by mapping the c-fos promoter sequence with several deletion and point mutants that confer responsiveness to E5 of HPV-11 or HPV-16 [2].
• The human papillomavirus type 11 (HPV-11) L1 major capsid protein can be trypsinized to generate recombinant capsomeres that retain HPV genotype-restricted capsid antigenicity (M. Li, T. P. Cripe, P. A. Estes, M. K. Lyon, R. C. Rose, and R. L. Garcea, J. Virol. 71:2988-2995, 1997) [3].
• The trypsin susceptibility of HPV-11 L1 capsids suggests a possible mechanism for virion disassembly [4].
• The carboxy terminus of L1 therefore constitutes the interpentamer linker arm responsible for HPV-11 capsid formation, much like the carboxy-terminal domain of the polyomavirus VP1 protein [4].

High impact information on Human papillomavirus 11

• Tandem copies of portions of the constitutive enhancer function as an E2-independent enhancer, whereas multiple copies of HPV-11 DNA restriction fragments or synthetic oligonucleotides containing the E2-responsive sequence (E2-RS) act as an enhancer in the presence of the E2 protein encoded by HPV-1, HPV-11, or bovine papillomavirus type 1 (BPV-1) [5].
• Exogenously added p180 inhibits both E2-dependent and E2-independent cell-free replication of HPV-11, whereas p70 inhibits E2-dependent but stimulates E2-independent replication [6].
• By using a variety of physical assays, we show that both 180- (p180) and 70-kDa (p70) subunits of pol alpha/primase interact with HPV-11 E1 [6].
• In addition, KSF may interact with related or identical cis-regulatory elements found in human papillomavirus-11 E6 and cytokeratin K3 promoters that are active in keratinocytes [7].
• Finally, the HPV-11 E2C protein lacking the transacting domain of the full-length E2 protein partially inhibits E2-dependent ori replication [1].

Chemical compound and disease context of Human papillomavirus 11

• Polystyrene sulfonate prevented subsequent infection of HPV-11 after virus-cell binding, and this inactivation was observed up to 4 h after addition of virus [8].
• High-titer cesium chloride gradient-purified HPV 11 virions infected 100% of recovered xenografts [9].
• Moreover, viral enhancer assays indicated that the observed stimulatory effect of pregnancy on condylomata and of estradiol on experimental cysts is likely an indirect one and could not be attributed to up-regulation of the HPV-11 transcriptional enhancer [10].
• HPV- 11 replication is significantly inhibited by BrdU and sodium butyrate; however 5-FU and alpha-IFN did not give consistent dose response results [11].
• In immunocompromised mice, papilloma cysts formed in HPV-11 infected laryngeal tissue implanted under the renal capsules in 100% of control mice but only in 25% of mice fed indole-3-carbinol [12].

Biological context of Human papillomavirus 11

• The HPV-11 E2 protein appears not to be essential for elongation, but it must be present in the preinitiation complex for the E1 protein to recruit host DNA replication machinery to the ori [1].
• For HPV-11, only RNAs initiated at the P264 promoter, located within the E6 open reading frame, were capable of providing an efficient template for E7 synthesis [13].
• Using an inducible system, we demonstrate that increased induction of the HPV-11 E5 gene in cells led to increased transactivation of the NF1 element [2].
• However, the HPV-11 E2 protein did not associate with Brd4 during mitosis [14].
• However, inhibition did not appear to be mediated by binding to its cognate site in the ori as YY1 also inhibited the replication of the HPV-11 ori, which does not have a known or suspected YY1 binding site [15].

Anatomical context of Human papillomavirus 11

• When HPV type 11 (HPV-11) expression is examined in epithelial cell lines, the HPV-11 E2-C protein, which lacks the amino-terminal transactivating domain of the full-length E2 protein, invariably represses the homologous viral E6 promoter [16].
• Human papillomavirus type 11 (HPV-11) and HPV-16 contain an E5 gene that can induce c-fos gene expression in mouse fibroblasts [2].
• The intact HPV-11 genome also replicated in both cell lines when supplied with E1 and E2 proteins [17].
• PCNA may be induced maximally in differentiated epithelium by HPV 11 prior to significant HPV DNA replication [18].
• Antisense oligodeoxynucleotides to c-jun inhibits proliferation of transformed NIH 3T3 cells induced by E5a of HPV-11 [19].

Gene context of Human papillomavirus 11

• On the other hand, low-risk HPV 11 E6 does not interact with E6AP even at relatively high concentrations [20].
• In contrast to HPV 11 and 16 L2, the HPV 18 L2 protein seems to require L1 for efficient nuclear accumulation [21].
• Our data are consistent with phosphorylation of HPV 11 E1(wedge)E4 protein by MAPK and PKA in infected tissue [22].
• The authors' data indicated that the p53 genetic mutation was associated with integration of HPV-11 in histologically malignant lesions [23].
• These differences could be explained in part by the inability of HPV-11 E7 to inhibit the induction of an IFN-responsive element, whereas HPV-6 E7 almost completely inhibited the activity of this promoter in transient transfection experiments [24].

Analytical, diagnostic and therapeutic context of Human papillomavirus 11

• Immuno-dot blot assays using human sera obtained from individuals with biopsy-proven condyloma acuminatum correlated closely with results previously obtained in HPV-11 whole virus particle-based enzyme-linked immunosorbent assays [25].
• Both proteins were detected on Western blots as immunoreactive bands which migrated with apparent Mrs of 76K and 78K, respectively, and contained both cross-reactive and type-specific epitopes, as determined by polyclonal antisera directed against defined subregions of the HPV-6b and HPV-11 L2 ORFs [26].
• Electron microscopy determined that the HPV-11 L1 VLPs were variable in size with a surface topography similar to that of infectious HPV-11 [27].
• All three fungiform papillomas were positive by all three techniques: immunohistochemistry, in situ hybridization for HPV 6/11, and the polymerase chain reaction for HPV 11 [28].
• The affinity purified HPV 11 anti-E4 antibodies identified putative E4 gene products in one of these same six lesions, which was shown to contain HPV 11 sequences by the Southern blot method [29].

References