Abstract: Co-expression of a pRb-binding-deficient mutant (E7C24G) and p14ARF resulted in EC24G nucleolar accumulation, but not in a significant higher activation of rDNA transcription, suggesting that the inactivation of pRb is involved in this phenomenon.
Intratypic variants of human papillomavirus type 16 and risk of cervical neoplasia in Taiwan.
Abstract: Similar significant associations with cervical intraepithelial neoplasia grade 3 or worse were also observed for distinct nucleotide substitutions, including T178A/G, A647G, A7730C/G, T7781C, G7842A, and C24T/G.
The human papillomavirus type 16 E7 oncoprotein targets Myc-interacting zinc-finger protein-1.
Result: C33A cells were transiently transfected either with pX-HPV-16 E7 wild-type, pX-HPV-16 E7Delta79LEDLL83, pX-HPV-16 E7Delta52YNIVT56, pX-HPV-16 E7C24G or pX, as indicated.
Result: While co-transfection of Miz-1 and the
Discussion: Another E7 mutant, C24G, which is impaired in binding and inactivating the pRB family members, can bind to Miz-1 and inhibit Miz-1-dependent p21Cip1 expression similar to wild-type E7.
Discussion: In keeping with these data, we showed in the present study that the E7 cd2 mutant C24G, which is deficient in binding to pRB, behaves as wild-type E7 in the functional interaction between E7 and Miz-1.
Characterization and whole genome analysis of human papillomavirus type 16 e1-1374^63nt variants.
Discussion: The only differences were the silent variations at position 24 C>G within the LCR and 109 T>C within the E6 region.
Expression of human papillomavirus type 16 E7 is sufficient to significantly increase expression of angiogenic factors but is not sufficient to induce endothelial cell migration.
Result: Although the HPV 16 E7C24G mutant has been reported to retain the ability to target another pRb family member, p107, for degradation, the ability of this mutant to target p130 for degradation has not been reported.
Result: By changing the cysteine at amino acid 24 to a glycine (C24G), HPV 16 E7 loses affinity for pRb and the ability to target pRb for degradation.
Result: In contrast, VEGF expression was increased 8.7-fold (p< 0.0001) in cells expressing HPV 16E6E7C24G compared to retrovirus control LXSN (p< 0.0001) (Figure 4B) and to a greater extent than conditioned media from HPV 16E6E7-expressing cells (Figure 4B).
Discussion: Alternatively, the pRb-independent activity of E7 could be due to degradation of p107 or the inter
Induction of tetrasomy by human papillomavirus type 16 E7 protein is independent of pRb binding and disruption of differentiation.
Result: Only the C24G mutant E7 protein was able to induce levels of tetrasomy similar to wild-type HPV16 E7 in monolayer culture (Figure 2B).
Discussion: Furthermore, recent quantitative binding studies have shown that the C24G mutant retains 30% of the pRb-binding affinity of the wild-type E7 protein (apparent KDs of 14 and 4.5 nM respectively) (Dong et al, 2001).
Discussion: However, if C24G retains or accentuates some difference in binding preference between the pocket proteins then the direct involvement of p107 or p130 cannot be excluded.
Discussion: However, the C24G mutant protein is able to stimulate proliferation in immortalized rodent fibroblasts (Caldeira et al, 2000).
Discussion: In organotypic raft culture
Determination of the binding affinity of different human papillomavirus E7 proteins for the tumour suppressor pRb by a plate-binding assay.
PMID: 11543887
2001
Journal of virological methods
Abstract: Point mutation C24G in the high affinity pRb-binding domain of HPV16 E7 results in a 3-fold affinity reduction.
Mutational analysis of human papillomavirus type 16 E7 functions.
HPV mutation literature information.
PMID: 
2014
PloS one
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