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Article ; Online: Targeting Human Papillomavirus-Associated Cancer by Oncoprotein-Specific Recombinant Antibodies.

Donà, Maria Gabriella / Di Bonito, Paola / Chiantore, Maria Vincenza / Amici, Carla / Accardi, Luisa

International journal of molecular sciences

2021 Volume 22, Issue 17

Abstract: In recent decades, recombinant antibodies against specific antigens have shown great promise for the therapy of infectious diseases and cancer. Human papillomaviruses (HPVs) are involved in the development of around 5% of all human cancers and HPV16 is ... ...

Abstract	In recent decades, recombinant antibodies against specific antigens have shown great promise for the therapy of infectious diseases and cancer. Human papillomaviruses (HPVs) are involved in the development of around 5% of all human cancers and HPV16 is the high-risk genotype with the highest prevalence worldwide, playing a dominant role in all HPV-associated cancers. Here, we describe the main biological activities of the HPV16 E6, E7, and E5 oncoproteins, which are involved in the subversion of important regulatory pathways directly associated with all known hallmarks of cancer. We then review the state of art of the recombinant antibodies targeted to HPV oncoproteins developed so far in different formats, and outline their mechanisms of action. We describe the advantages of a possible antibody-based therapy against the HPV-associated lesions and discuss the critical issue of delivery to tumour cells, which must be addressed in order to achieve the desired translation of the antibodies from the laboratory to the clinic.
MeSH term(s)	Animals ; Antibodies, Viral/immunology ; Antibodies, Viral/therapeutic use ; Humans ; Neoplasms/drug therapy ; Neoplasms/virology ; Oncogene Proteins, Viral/immunology ; Papillomavirus E7 Proteins/immunology ; Recombinant Proteins/immunology ; Recombinant Proteins/therapeutic use ; Repressor Proteins/immunology ; Single-Domain Antibodies/immunology ; Single-Domain Antibodies/therapeutic use
Chemical Substances	Antibodies, Viral ; E6 protein, Human papillomavirus type 16 ; Oncogene Proteins, Viral ; Papillomavirus E7 Proteins ; Recombinant Proteins ; Repressor Proteins ; Single-Domain Antibodies ; oncogene protein E5, Human papillomavirus type 16 ; oncogene protein E7, Human papillomavirus type 16
Language	English
Publishing date	2021-08-24
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms22179143
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Epitope Mapping and Computational Analysis of Anti-HPV16 E6 and E7 Antibodies in Single-Chain Format for Clinical Development as Antitumor Drugs.

Amici, Carla / Donà, Maria Gabriella / Chirullo, Barbara / Di Bonito, Paola / Accardi, Luisa

Cancers

2020 Volume 12, Issue 7

Abstract: Human Papillomavirus 16-associated cancer, affecting primarily the uterine cervix but, increasingly, other body districts, including the head-neck area, will long be a public health problem, despite there being a vaccine. Since the virus oncogenic ... ...

Abstract	Human Papillomavirus 16-associated cancer, affecting primarily the uterine cervix but, increasingly, other body districts, including the head-neck area, will long be a public health problem, despite there being a vaccine. Since the virus oncogenic activity is fully ascribed to the viral E6 and E7 oncoproteins, one of the therapeutic approaches for HPV16 cancer is based on specific antibodies in single-chain format targeting the E6/E7 activity. We analyzed the Complementarity Determining Regions, repositories of antigen-binding activity, of four anti-HPV16 E6 and -HPV16 E7 scFvs, to highlight possible conformity to biophysical properties, recognized to be advantageous for therapeutic use. By epitope mapping, using E7 mutants with amino acid deletions or variations, we investigated differences among the anti-16E7 scFvs in terms of antigen-binding capacity. We also performed computational analyses to determine whether length, total net charge, surface hydrophobicity, polarity and charge distribution conformed well to those of the antibodies that had already reached clinical use, through the application of developability guidelines derived from recent literature on clinical-stage antibodies, and the Therapeutic Antibodies Profiler software. Overall, our findings show that the scFvs investigated may represent valid candidates to be developed as therapeutic molecules for clinical use, and highlight characteristics that could be improved by molecular engineering.
Language	English
Publishing date	2020-07-06
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2527080-1
ISSN	2072-6694
ISSN	2072-6694
DOI	10.3390/cancers12071803
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Article ; Online: Intrabodies targeting human papillomavirus 16 E6 and E7 oncoproteins for therapy of established HPV-associated tumors.

Paolini, Francesca / Amici, Carla / Carosi, Mariantonia / Bonomo, Claudia / Di Bonito, Paola / Venuti, Aldo / Accardi, Luisa

Journal of experimental & clinical cancer research : CR

2021 Volume 40, Issue 1, Page(s) 37

Abstract: Background: The oncogenic activity of the high risk human papillomavirus type 16 (HPV16) is fully dependent on the E6 and E7 viral oncoproteins produced during viral infection. The oncoproteins interfere with cellular homeostasis by promoting ... ...

Abstract	Background: The oncogenic activity of the high risk human papillomavirus type 16 (HPV16) is fully dependent on the E6 and E7 viral oncoproteins produced during viral infection. The oncoproteins interfere with cellular homeostasis by promoting proliferation, inhibiting apoptosis and blocking epithelial differentiation, driving the infected cells towards neoplastic progression. The causal relationship between expression of E6/E7 and cellular transformation allows inhibiting the oncogenic process by hindering the activity of the two oncoproteins. We previously developed and characterized some antibodies in single-chain format (scFvs) against the HPV16 E6 and E7 proteins, and demonstrated both in vitro and in vivo their antitumor activity consisting of protective efficacy against tumor progression of HPV16-positive cells. Methods: Envisioning clinical application of the best characterized anti-HPV16 E6 and -HPV16 E7 scFvs, we verified their activity in the therapeutic setting, on already implanted tumors. Recombinant plasmids expressing the anti-HPV16 E6 scFvI7 with nuclear targeting sequence, or the anti-HPV16 E7 scFv43M2 with endoplasmic reticulum targeting sequence were delivered by injection followed by electroporation to three different preclinical models using C57/BL6 mice, and their effect on tumor growth was investigated. In the first model, the HPV16+ TC-1 Luc cells were used to implant tumors in mice, and tumor growth was measured by luciferase activity; in the second model, a fourfold number of TC-1 cells was used to obtain more aggressively growing tumors; in the third model, the HPV16+ C3 cells where used to rise tumors in mice. To highlight the scFv possible mechanism of action, H&E and caspase-3 staining of tumor section were performed. Results: We showed that both the anti-HPV16 E6 and HPV16 E7 scFvs tested were efficacious in delaying tumor progression in the three experimental models and that their antitumor activity seems to rely on driving tumor cells towards the apoptotic pathway. Conclusion: Based on our study, two scFvs have been identified that could represent a safe and effective treatment for the therapy of HPV16-associated lesions. The mechanism underlying the scFv effectiveness appears to be leading cells towards death by apoptosis. Furthermore, the validity of electroporation, a methodology allowed for human treatment, to deliver scFvs to tumors was confirmed.
MeSH term(s)	Animals ; Cell Line, Tumor ; Female ; Human papillomavirus 16/immunology ; Humans ; Mice ; Oncogene Proteins, Viral/immunology ; Papillomavirus E7 Proteins/immunology
Chemical Substances	Oncogene Proteins, Viral ; Papillomavirus E7 Proteins
Language	English
Publishing date	2021-01-23
Publishing country	England
Document type	Journal Article
ZDB-ID	803138-1
ISSN	1756-9966 ; 0392-9078
ISSN (online)	1756-9966
ISSN	0392-9078
DOI	10.1186/s13046-021-01841-w
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Article ; Online: Inhibition of viral protein translation by indomethacin in vesicular stomatitis virus infection: role of eIF2α kinase PKR.

Amici, Carla / La Frazia, Simone / Brunelli, Claudia / Balsamo, Mirna / Angelini, Mara / Santoro, M Gabriella

Cellular microbiology

2015 Volume 17, Issue 9, Page(s) 1391–1404

Abstract: Indomethacin, a cyclooxygenase-1 and -2 inhibitor widely used in the clinic for its potent anti-inflammatory/analgesic properties, possesses antiviral activity against several viral pathogens; however, the mechanism of antiviral action remains elusive. ... ...

Abstract	Indomethacin, a cyclooxygenase-1 and -2 inhibitor widely used in the clinic for its potent anti-inflammatory/analgesic properties, possesses antiviral activity against several viral pathogens; however, the mechanism of antiviral action remains elusive. We have recently shown that indomethacin activates the double-stranded RNA (dsRNA)-dependent protein kinase R (PKR) in human colon cancer cells. Because of the important role of PKR in the cellular defence response against viral infection, herein we investigated the effect of indomethacin on PKR activity during infection with the prototype rhabdovirus vesicular stomatitis virus. Indomethacin was found to activate PKR in an interferon- and dsRNA-independent manner, causing rapid (< 5 min) phosphorylation of eukaryotic initiation factor-2 α-subunit (eIF2α). These events resulted in shutting off viral protein translation and blocking viral replication (IC50 = 2 μM) while protecting host cells from virus-induced damage. Indomethacin did not affect eIF2α kinases PKR-like endoplasmic reticulum-resident protein kinase (PERK) and general control non-derepressible-2 (GCN2) kinase, and was unable to trigger eIF2α phosphorylation in the presence of PKR inhibitor 2-aminopurine. In addition, small-interfering RNA-mediated PKR gene silencing dampened the antiviral effect in indomethacin-treated cells. The results identify PKR as a critical target for the antiviral activity of indomethacin and indicate that eIF2α phosphorylation could be a key element in the broad spectrum antiviral activity of the drug.
MeSH term(s)	Antiviral Agents/metabolism ; Cell Line ; Enzyme Activators/metabolism ; Eukaryotic Initiation Factor-2/metabolism ; Humans ; Indomethacin/metabolism ; Inhibitory Concentration 50 ; Phosphorylation ; Protein Biosynthesis/drug effects ; Protein Processing, Post-Translational ; Vesiculovirus/drug effects ; Viral Proteins/biosynthesis ; eIF-2 Kinase/metabolism
Chemical Substances	Antiviral Agents ; Enzyme Activators ; Eukaryotic Initiation Factor-2 ; Viral Proteins ; eIF-2 Kinase (EC 2.7.11.1) ; Indomethacin (XXE1CET956)
Keywords	covid19
Language	English
Publishing date	2015-05-13
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1468320-9
ISSN	1462-5822 ; 1462-5814
ISSN (online)	1462-5822
ISSN	1462-5814
DOI	10.1111/cmi.12446
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Zs.A 5288: Show issues

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Article ; Online: The non-steroidal anti-inflammatory drug indomethacin activates the eIF2α kinase PKR, causing a translational block in human colorectal cancer cells.

Brunelli, Claudia / Amici, Carla / Angelini, Mara / Fracassi, Chiara / Belardo, Giuseppe / Santoro, M Gabriella

The Biochemical journal

2012 Volume 443, Issue 2, Page(s) 379–386

Abstract: The NSAID (non-steroidal anti-inflammatory drug) indomethacin, a cyclo-oxygenase-1 and -2 inhibitor with anti-inflammatory and analgesic properties, is known to possess anticancer activity against CRC (colorectal cancer) and other malignancies in humans; ...

Abstract	The NSAID (non-steroidal anti-inflammatory drug) indomethacin, a cyclo-oxygenase-1 and -2 inhibitor with anti-inflammatory and analgesic properties, is known to possess anticancer activity against CRC (colorectal cancer) and other malignancies in humans; however, the mechanism underlying the anticancer action remains elusive. In the present study we show that indomethacin selectively activates the dsRNA (double-stranded RNA)-dependent protein kinase PKR in a cyclo-oxygenase-independent manner, causing rapid phosphorylation of eIF2α (the α-subunit of eukaryotic translation initiation factor 2) and inhibiting protein synthesis in colorectal carcinoma and other types of cancer cells. The PKR-mediated translational block was followed by inhibition of CRC cell proliferation and apoptosis induction. Indomethacin did not affect the activity of the eIF2α kinases PERK (PKR-like endoplasmic reticulum-resident kinase), GCN2 (general control non-derepressible-2) and HRI (haem-regulated inhibitor kinase), and induced eIF2α phosphorylation in PERK-knockout and GCN2-knockout cells, but not in PKR-knockout cells or in human PKR-silenced CRC cells, identifying PKR as a selective target for indomethacin-induced translational inhibition. The fact that indomethacin induced PKR activity in vitro, an effect reversed by the PKR inhibitor 2-aminopurine, suggests a direct effect of the drug in kinase activation. The results of the present study identify PKR as a novel target of indomethacin, suggesting new scenarios on the molecular mechanisms underlying the pleiotropic activity of this traditional NSAID.
MeSH term(s)	Anti-Inflammatory Agents, Non-Steroidal/pharmacology ; Cell Line, Tumor ; Cell Proliferation/drug effects ; Cisplatin/pharmacology ; Colonic Neoplasms/enzymology ; Colonic Neoplasms/pathology ; Enzyme Activation ; Humans ; Indomethacin/pharmacology ; Protein Biosynthesis/drug effects ; eIF-2 Kinase/metabolism
Chemical Substances	Anti-Inflammatory Agents, Non-Steroidal ; eIF-2 Kinase (EC 2.7.11.1) ; Cisplatin (Q20Q21Q62J) ; Indomethacin (XXE1CET956)
Language	English
Publishing date	2012-04-15
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2969-5
ISSN	1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
ISSN (online)	1470-8728
ISSN	0006-2936 ; 0306-3275 ; 0264-6021
DOI	10.1042/BJ20111236
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Uc I Zs.110: Show issues

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Article: Antiviral activity of proteasome inhibitors in herpes simplex virus-1 infection: role of nuclear factor-kappaB.

La Frazia, Simone / Amici, Carla / Santoro, M Gabriella

Antiviral therapy

2006 Volume 11, Issue 8, Page(s) 995–1004

Abstract: Background: Herpes simplex virus type 1 (HSV-1) is a potent inducer of nuclear factor-KB (NF-kappaB), a cellular transcription factor with a crucial role in promoting inflammation and controlling cell proliferation and survival.: Objectives: On the ... ...

Abstract	Background: Herpes simplex virus type 1 (HSV-1) is a potent inducer of nuclear factor-KB (NF-kappaB), a cellular transcription factor with a crucial role in promoting inflammation and controlling cell proliferation and survival. Objectives: On the basis of the recent demonstration that HSV-1-induced NF-kappaB is actively recruited to KB-binding sites in the HSV-1 infected-cell protein 0 (ICPO) promoter enhancing viral transcription and replication, we investigated the effect of proteasome inhibitors MG132, MG115 and epoxomicin, which block NF-kappaB function by preventing the degradation of the inhibitory proteins IkappaBalpha, on HSV-1-induced NF-kappaB activation and viral replication. Methods: Antiviral activity of proteasome inhibitors was analysed in HSV-1-infected HEp2 cells by determining infective virus titres by CPE50%, viral RNA synthesis by RT-PCR, and viral protein synthesis by immunoblot analysis or immunofluorescence. ICPO transcription was studied in transient transfection experiments using the ICPO promoter-luciferase IE1-Luc construct. IkappaBalpha degradation and NF-kappaB activity were determined by immunoblot analysis and EMSA, respectively. Results: Proteasome inhibitors were found to prevent HSV-1-induced NF-kappaB activation in the early phase of infection. Block of virus-induced NF-kappaB activation resulted in inhibiting HSV-1 ICPO gene expression, in decreasing the level of immediate-early and late viral proteins, and ultimately in greatly suppressing viral replication. The antiviral effect was lost if treatment was started after NF-kappaB activation, and appeared to be independent of the HSV-1-induced activation of the JNK pathway. Conclusions: Proteasome inhibitors possess NF-kappaB-dependent antiherpetic activity. The results described further identify the IKK/NF-kappaB pathway as a suitable target for novel antiherpetic drugs.
MeSH term(s)	Animals ; Antiviral Agents/pharmacology ; Cell Line, Tumor ; Cercopithecus aethiops ; Down-Regulation ; Herpesvirus 1, Human/drug effects ; Humans ; Immediate-Early Proteins/metabolism ; Leupeptins/pharmacology ; NF-kappa B/metabolism ; Oligopeptides/pharmacology ; Proteasome Endopeptidase Complex/metabolism ; Proteasome Inhibitors ; Transcription Factor AP-1/metabolism ; Vero Cells
Chemical Substances	Antiviral Agents ; IE1 protein, Human herpesvirus 1 ; Immediate-Early Proteins ; Leupeptins ; NF-kappa B ; Oligopeptides ; Proteasome Inhibitors ; Transcription Factor AP-1 ; carbobenzoxy-leucyl-leucyl-norvalinal ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; benzyloxycarbonylleucyl-leucyl-leucine aldehyde (RF1P63GW3K) ; epoxomicin (Y0900I3U8U)
Language	English
Publishing date	2006
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1339842-8
ISSN	1359-6535
ISSN	1359-6535
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Zs.A 4877: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MO 174: Show issues

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Article ; Online: Role of Heat Shock Proteins in Viral Infection

Santoro, M. Gabriella / Amici, Carla / Rossi, Antonio

Prokaryotic and Eukaryotic Heat Shock Proteins in Infectious Disease

Abstract: One of the most intriguing and less known aspects of the interaction between viruses and their host is the impact of the viral infection on the heat shock response (HSR). While both a positive and a negative role of different heat shock proteins (HSP) in ...

Abstract	One of the most intriguing and less known aspects of the interaction between viruses and their host is the impact of the viral infection on the heat shock response (HSR). While both a positive and a negative role of different heat shock proteins (HSP) in the control of virus replication has been hypothesized, HSP function during the virus replication cycle is still not well understood. This chapter describes different aspects of the interactions between viruses and heat shock proteins during infection of mammalian cells: the first part focuses on the modulation of the heat shock response by human viral pathogens; the second describes the interactions of HSP and other chaperones with viral components, and their function during different steps of the virus replication cycle; the last part summarizes our knowledge on the effect of hyperthermia and HSR modulators on virus replication.
Keywords	covid19
Publisher	PMC
Document type	Article ; Online
DOI	10.1007/978-90-481-2976-8_3
Database	COVID19

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Article ; Online: A novel intracellular antibody against the E6 oncoprotein impairs growth of human papillomavirus 16-positive tumor cells in mouse models.

Amici, Carla / Visintin, Michela / Verachi, Francesca / Paolini, Francesca / Percario, Zulema / Di Bonito, Paola / Mandarino, Angela / Affabris, Elisabetta / Venuti, Aldo / Accardi, Luisa

Oncotarget

2016 Volume 7, Issue 13, Page(s) 15539–15553

Abstract: Single-chain variable fragments (scFvs) expressed as "intracellular antibodies" (intrabodies) can target intracellular antigens to hamper their function efficaciously and specifically. Here we use an intrabody targeting the E6 oncoprotein of Human ... ...

Abstract	Single-chain variable fragments (scFvs) expressed as "intracellular antibodies" (intrabodies) can target intracellular antigens to hamper their function efficaciously and specifically. Here we use an intrabody targeting the E6 oncoprotein of Human papillomavirus 16 (HPV16) to address the issue of a non-invasive therapy for HPV cancer patients.A scFv against the HPV16 E6 was selected by Intracellular Antibody Capture Technology and expressed as I7nuc in the nucleus of HPV16-positive SiHa, HPV-negative C33A and 293T cells. Colocalization of I7nuc and recombinant E6 was observed in different cell compartments, obtaining evidence of E6 delocalization ascribable to I7nuc. In SiHa cells, I7nuc expressed by pLNCX retroviral vector was able to partially inhibit degradation of the main E6 target p53, and induced p53 accumulation in nucleus. When analyzing in vitro activity on cell proliferation and survival, I7nuc was able to decrease growth inducing late apoptosis and necrosis of SiHa cells.Finally, I7nuc antitumor activity was demonstrated in two pre-clinical models of HPV tumors. C57BL/6 mice were injected subcutaneously with HPV16-positive TC-1 or C3 tumor cells, infected with pLNCX retroviral vector expressing or non-expressing I7nuc. All the mice injected with I7nuc-expressing cells showed a clear delay in tumor onset; 60% and 40% of mice receiving TC-1 and C3 cells, respectively, remained tumor-free for 17 weeks of follow-up, whereas 100% of the controls were tumor-bearing 20 days post-inoculum. Our data support the therapeutic potential of E6-targeted I7nuc against HPV tumors.
Language	English
Publishing date	2016-03-29
Publishing country	United States
Document type	Journal Article
ZDB-ID	2560162-3
ISSN	1949-2553 ; 1949-2553
ISSN (online)	1949-2553
ISSN	1949-2553
DOI	10.18632/oncotarget.6925
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Article: NF-kappaB and virus infection: who controls whom.

Santoro, M Gabriella / Rossi, Antonio / Amici, Carla

The EMBO journal

2003 Volume 22, Issue 11, Page(s) 2552–2560

Abstract: Among the different definitions of viruses, 'pirates of the cell' is one of the most picturesque, but also one of the most appropriate. Viruses have been known for a long time to utilize a variety of strategies to penetrate cells and, once inside, to ... ...

Abstract	Among the different definitions of viruses, 'pirates of the cell' is one of the most picturesque, but also one of the most appropriate. Viruses have been known for a long time to utilize a variety of strategies to penetrate cells and, once inside, to take over the host nucleic acid and protein synthesis machinery to build up their own components and produce large amounts of viral progeny. As their genomes carry a minimal amount of information, encoding only a few structural and regulatory proteins, viruses are largely dependent on their hosts for survival; however, despite their apparent simplicity, viruses have evolved different replicative strategies that are regulated in a sophisticated manner. During the last years, the study of the elaborate relationship between viruses and their hosts has led to the understanding of how viral pathogens not only are able to alter the host metabolism via their signaling proteins, but are also able to hijack cellular signaling pathways and transcription factors, and control them to their own advantage. In particular, the nuclear factor-kappaB (NF-kappaB) pathway appears to be an attractive target for common human viral pathogens. This review summarizes what is known about the control of NF-kappaB by viruses, and discusses the possible outcome of NF-kappaB activation during viral infection, which may benefit either the host or the pathogen.
MeSH term(s)	Animals ; Humans ; Models, Biological ; NF-kappa B/physiology ; Signal Transduction ; Virus Diseases/physiopathology ; Virus Diseases/virology ; Virus Physiological Phenomena ; Viruses/pathogenicity
Chemical Substances	NF-kappa B
Language	English
Publishing date	2003-06-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	586044-1
ISSN	1460-2075 ; 0261-4189
ISSN (online)	1460-2075
ISSN	0261-4189
DOI	10.1093/emboj/cdg267
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Zs.A 1808: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 100: Show issues

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Book: Il Foro di Cesare

Amici, Carla Maria

(Il linguaggio dell'architettura romana ; ...)

1991

Author's details	Carla Maria Amici
Series title	Il linguaggio dell'architettura romana ...
Language	Italian
Dates of publication	1991-9999
Publisher	Olschki
Publishing place	Firenze
Document type	Book
ISBN	8822238303 ; 9788822238306
Database	Former special subject collection: coastal and deep sea fishing

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