scholarly journals E7 Oncoprotein of Human Papillomavirus Type 16 Expressed Constitutively in the Epidermis Has No Effect on E7-Specific B- or Th-Repertoires or on the Immune Response Induced or Sustained after Immunization with E7 Protein

Virology ◽  
1997 ◽  
Vol 231 (1) ◽  
pp. 155-165 ◽  
Author(s):  
K. Herd ◽  
G.J.P. Fernando ◽  
L.A. Dunn ◽  
I.H. Frazer ◽  
P. Lambert ◽  
...  
Keyword(s):  
Immune Response ◽  
Human Papillomavirus ◽  
E7 Oncoprotein ◽  
Human Papillomavirus Type 16

scholarly journals Structure-function analysis of the human papillomavirus type 16 E7 oncoprotein.

1992 ◽  
Vol 66 (4) ◽  
pp. 2418-2427 ◽  
Author(s):  
W C Phelps ◽  
K Münger ◽  
C L Yee ◽  
J A Barnes ◽  
P M Howley
Keyword(s):  
Human Papillomavirus ◽  
Structure Function ◽  
Function Analysis ◽  
E7 Oncoprotein ◽  
Human Papillomavirus Type 16

scholarly journals Human Papillomavirus Type 16 E7 Peptide-Directed CD8+ T Cells from Patients with Cervical Cancer Are Cross-Reactive with the Coronavirus NS2 Protein

2003 ◽  
Vol 77 (9) ◽  
pp. 5464-5474 ◽  
Author(s):  
Katja Nilges ◽  
Hanni Höhn ◽  
Henryk Pilch ◽  
Claudia Neukirch ◽  
Kirsten Freitag ◽  
...  
Keyword(s):  
Cervical Cancer ◽  
Immune Response ◽  
T Cells ◽  
Human Papillomavirus ◽  
T Cell ◽  
T Cell Responses ◽  
Cross Reactivity ◽  
Antiviral Immune Response ◽  
Human Papillomavirus Type 16 ◽  
Cell Responses

ABSTRACT Human papillomavirus type 16 (HPV16) E6 and E7 oncoproteins are required for cellular transformation and represent candidate targets for HPV-specific and major histocompatibility complex class I-restricted CD8+-T-cell responses in patients with cervical cancer. Recent evidence suggests that cross-reactivity represents the inherent nature of the T-cell repertoire. We identified HLA-A2 binding HPV16 E7 variant peptides from human, bacterial, or viral origin which are able to drive CD8+-T-cell responses directed against wild-type HPV16 E7 amino acid 11 to 19/20 (E711-19/20) epitope YMLDLQPET(T) in vitro. CD8+ T cells reacting to the HLA-A2-presented peptide from HPV16 E711-19(20) recognized also the HLA-A2 binding peptide TMLDIQPED (amino acids 52 to 60) from the human coronavirus OC43 NS2 gene product. Establishment of coronavirus NS2-specific, HLA-A2-restricted CD8+-T-cell clones and ex vivo analysis of HPV16 E7 specific T cells obtained by HLA-A2 tetramer-guided sorting from PBL or tumor-infiltrating lymphocytes obtained from patients with cervical cancer showed that cross-reactivity with HPV16 E711-19(20) and coronavirus NS252-60 represents a common feature of this antiviral immune response defined by cytokine production. Zero of 10 patients with carcinoma in situ neoplasia and 3 of 18 patients with cervical cancer showed ≥0.1% HPV16 E7-reactive T cells in CD8+ peripheral blood lymphocytes. In vivo priming with HPV16 was confirmed in patients with cervical cancer or preinvasive HPV16-positive lesions using HLA-A2 tetramer complexes loaded with the E6-derived epitope KLPQLCTEL. In contrast, we could not detect E6-reactive T cells in healthy individuals. These data imply that the measurement of the HPV16 E711-19(20) CD8+-T-cell response may reflect cross-reactivity with a common pathogen and that variant peptides may be employed to drive an effective cellular immune response against HPV.

scholarly journals Cervical Cancers Require the Continuous Expression of the Human Papillomavirus Type 16 E7 Oncoprotein Even in the Presence of the Viral E6 Oncoprotein

2012 ◽  
Vol 72 (16) ◽  
pp. 4008-4016 ◽  
Author(s):  
Sean F. Jabbar ◽  
Soyeong Park ◽  
Johannes Schweizer ◽  
Marthe Berard-Bergery ◽  
Henry C. Pitot ◽  
...  
Keyword(s):  
Human Papillomavirus ◽  
Cervical Cancers ◽  
E7 Oncoprotein ◽  
Human Papillomavirus Type 16 ◽  
E6 Oncoprotein

Human Papillomavirus Type 16 E7 Oncoprotein Binds and Inactivates Growth-Inhibitory Insulin-Like Growth Factor Binding Protein 3

2000 ◽  
Vol 20 (17) ◽  
pp. 6483-6495
Author(s):  
Boris Mannhardt ◽  
Stuart A. Weinzimer ◽  
Mechthild Wagner ◽  
Marc Fiedler ◽  
Pinchas Cohen ◽  
...  
Keyword(s):  
Human Papillomavirus ◽  
Growth Factor ◽  
Binding Protein ◽  
Insulin Like Growth Factor ◽  
Factor Binding ◽  
E7 Oncoprotein ◽  
Human Papillomavirus Type 16 ◽  
Growth Inhibitory

scholarly journals Stabilization and Functional Impairment of the Tumor Suppressor p53 by the Human Papillomavirus Type 16 E7 Oncoprotein

Virology ◽  
2002 ◽  
Vol 295 (1) ◽  
pp. 74-85 ◽  
Author(s):  
Alexandra Eichten ◽  
Matthew Westfall ◽  
Jennifer A. Pietenpol ◽  
Karl Münger
Keyword(s):  
Human Papillomavirus ◽  
Tumor Suppressor ◽  
Functional Impairment ◽  
Tumor Suppressor P53 ◽  
E7 Oncoprotein ◽  
Human Papillomavirus Type 16

scholarly journals Human Papillomavirus Type 16 E7 Oncoprotein Associates with the Centrosomal Component γ-Tubulin

2007 ◽  
Vol 81 (24) ◽  
pp. 13533-13543 ◽  
Author(s):  
Christine L. Nguyen ◽  
Catherine Eichwald ◽  
Max L. Nibert ◽  
Karl Münger
Keyword(s):  
Human Papillomavirus ◽  
Gradient Centrifugation ◽  
Sucrose Density Gradient ◽  
Sucrose Density Gradient Centrifugation ◽  
E7 Oncoprotein ◽  
Human Papillomavirus Type 16 ◽  
Retinoblastoma Tumor Suppressor ◽  
Mitotic Abnormalities ◽  
Small Pool ◽  
Retinoblastoma Tumor

ABSTRACT Expression of a high-risk human papillomavirus (HPV) E7 oncoprotein is sufficient to induce aberrant centrosome duplication in primary human cells. The resulting centrosome-associated mitotic abnormalities have been linked to the development of aneuploidy. HPV type 16 (HPV16) E7 induces supernumerary centrosomes through a mechanism that is at least in part independent of the inactivation of the retinoblastoma tumor suppressor pRb and is dependent on cyclin-dependent kinase 2 activity. Here, we show that HPV16 E7 can concentrate around mitotic spindle poles and that a small pool of HPV16 E7 is associated with centrosome fractions isolated by sucrose density gradient centrifugation. The targeting of HPV16 E7 to the centrosome, however, was not sufficient for centrosome overduplication. Nonetheless, we found that HPV16 E7 can associate with the centrosomal regulator γ-tubulin and that the recruitment of γ-tubulin to the centrosome is altered in HPV16 E7-expressing cells. Since the association of HPV16 E7 with γ-tubulin is independent of pRb, p107, and p130, our results suggest that the association with γ-tubulin contributes to the pRb/p107/p130-independent ability of HPV16 E7 to subvert centrosome homeostasis.

Production of human papillomavirus type 16 E7 oncoprotein fused with β-glucuronidase in transgenic tomato and potato plants

2007 ◽  
Vol 51 (2) ◽  
pp. 268-276 ◽  
Author(s):  
J. Bříza ◽  
D. Pavingerová ◽  
J. Vlasák ◽  
V. Ludvíková ◽  
H. Niedermeierová
Keyword(s):  
Human Papillomavirus ◽  
Transgenic Tomato ◽  
E7 Oncoprotein ◽  
Human Papillomavirus Type 16 ◽  
Potato Plants
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